|
Name |
Accession |
Description |
Interval |
E-value |
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
67-171 |
6.82e-75 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 244.62 E-value: 6.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 67 DRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKLVNI 146
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1988774676 147 RNDDIADGNPKLTLGLIWTIILHFQ 171
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
64-186 |
2.84e-70 |
|
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409084 Cd Length: 119 Bit Score: 232.22 E-value: 2.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 64 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKL 143
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1988774676 144 VNIRNDDIADGNPKLTLGLIWTIILHFQvsssISDIQVNGQSE 186
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQ----ISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
61-184 |
6.60e-67 |
|
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 222.94 E-value: 6.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 61 RIADERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQ 140
Cdd:cd21236 9 RYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQ 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1988774676 141 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQvsssISDIQVNGQ 184
Cdd:cd21236 89 VKLVNIRNDDITDGNPKLTLGLIWTIILHFQ----ISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
188-293 |
3.27e-65 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 217.20 E-value: 3.27e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 188 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 267
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1988774676 268 PEDVDVPHPDEKSIITYVSSLYDAMP 293
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
189-293 |
6.80e-63 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 210.33 E-value: 6.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 189 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 268
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1988774676 269 EDVDVPHPDEKSIITYVSSLYDAMP 293
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
64-185 |
9.56e-59 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 199.10 E-value: 9.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 64 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKL 143
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1988774676 144 VNIRNDDIADGNPKLTLGLIWTIILHFQvsssISDIQVNGQS 185
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQ----ISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
189-293 |
3.45e-57 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 194.05 E-value: 3.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 189 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 268
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1988774676 269 EDVDVPHPDEKSIITYVSSLYDAMP 293
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
69-172 |
8.22e-51 |
|
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 176.03 E-value: 8.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 69 VQKKTFTKWVNKHLIKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKLVNIR 147
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1988774676 148 NDDIADGNPKLTLGLIWTIILHFQV 172
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
62-168 |
8.12e-49 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 170.63 E-value: 8.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 62 IADERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLRHRQ 140
Cdd:cd21246 9 LADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQR 88
|
90 100
....*....|....*....|....*...
gi 1988774676 141 VKLVNIRNDDIADGNPKLTLGLIWTIIL 168
Cdd:cd21246 89 VHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
187-293 |
9.88e-49 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 170.22 E-value: 9.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 187 DMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLL 266
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1988774676 267 DPEDVDVPHPDEKSIITYVSSLYDAMP 293
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
189-289 |
1.27e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 163.74 E-value: 1.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 189 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 268
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1988774676 269 EDVDVPHPDEKSIITYVSSLY 289
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
57-168 |
3.54e-44 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 157.46 E-value: 3.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 57 RAVIR-IADERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALD 134
Cdd:cd21193 3 KGRIRaLQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALA 82
|
90 100 110
....*....|....*....|....*....|....
gi 1988774676 135 FLrHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 168
Cdd:cd21193 83 FL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
189-289 |
3.66e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 156.79 E-value: 3.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 189 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 268
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1988774676 269 EDVDVPHPDEKSIITYVSSLY 289
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
65-172 |
5.50e-44 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 156.77 E-value: 5.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 65 ERDRVQKKTFTKWVNKHLIKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLRHRQ 140
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1988774676 141 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 172
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
62-168 |
4.41e-42 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409167 Cd Length: 139 Bit Score: 152.49 E-value: 4.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 62 IADERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLRHRQ 140
Cdd:cd21318 31 LADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQR 110
|
90 100
....*....|....*....|....*...
gi 1988774676 141 VKLVNIRNDDIADGNPKLTLGLIWTIIL 168
Cdd:cd21318 111 VHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
62-168 |
5.74e-41 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 149.05 E-value: 5.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 62 IADERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLRHRQ 140
Cdd:cd21317 24 LADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLKEQK 103
|
90 100
....*....|....*....|....*...
gi 1988774676 141 VKLVNIRNDDIADGNPKLTLGLIWTIIL 168
Cdd:cd21317 104 VHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
65-172 |
9.28e-41 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 147.33 E-value: 9.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 65 ERDRVQKKTFTKWVNKHLIKAQRH--VTDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLRHRQ 140
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 1988774676 141 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 172
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
63-289 |
1.16e-39 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 159.34 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 63 ADERDRVQKKTFTKWVNKHLIKA-QRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLRHR 139
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 140 QVKLVNIRNDDIADGNPKLTLGLIWTIILhfqvSSSISDIQvngQSEDMTAKEKLLLWSQRMTDGYQ-GIRCDNFTTSWR 218
Cdd:COG5069 83 GVKLFNIGPQDIVDGNPKLILGLIWSLIS----RLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774676 219 DGKLFNAVIHKHYPRLINMGKVYQQTNLE--NLEQAFSVAEKDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLY 289
Cdd:COG5069 156 DGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
924-1001 |
1.38e-39 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 142.74 E-value: 1.38e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774676 924 LSWQYLMRDFTQIRSWNITMLKTMKPEEYRLIMRNLELHYQDFMRDSQDSQLFGPDDRMQVEDDYTKSTQHFDNLLRS 1001
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
176-291 |
2.40e-39 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 143.66 E-value: 2.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 176 ISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 255
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774676 256 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 291
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
185-289 |
5.08e-39 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 142.45 E-value: 5.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 185 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTR 264
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1988774676 265 LLDPEDVDVPHPDEKSIITYVSSLY 289
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
188-293 |
8.36e-39 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 141.69 E-value: 8.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 188 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 267
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1988774676 268 PEDVDVPHPDEKSIITYVSSLYDAMP 293
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
69-170 |
9.79e-38 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 138.69 E-value: 9.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 69 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLRHRQVKLVNI 146
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1988774676 147 RNDDIADGNPKLTLGLIWTIILHF 170
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
67-168 |
1.00e-37 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 138.68 E-value: 1.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 67 DRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLRHRQVKLVN 145
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1988774676 146 IRNDDIADGNPKLTLGLIWTIIL 168
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
65-172 |
1.81e-37 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409091 Cd Length: 111 Bit Score: 138.04 E-value: 1.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 65 ERDRVQKKTFTKWVNKHLIKAQ--RHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVK 142
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1988774676 143 LVNIRNDDIADGNPKLTLGLIWTIILHFQV 172
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
188-289 |
4.60e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 136.92 E-value: 4.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 188 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 267
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1988774676 268 PEDVDVPHPDEKSIITYVSSLY 289
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1344-1923 |
1.55e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 152.78 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1344 QEYVTLRTRYSEL-MTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQlaeahakAIAKAEKEAQE 1422
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL-------ELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1423 LKLKMQEEVSKreiaavdAEKQKTNIQLELQELKNLSEQQIKDKSQqvdealhsRTKIEEEIRLIRIQLETTEKQKYTAE 1502
Cdd:COG1196 286 AQAEEYELLAE-------LARLEQDIARLEERRRELEERLEELEEE--------LAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1503 SELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQV 1582
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1583 KQAEIEKEKQIkvAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELE 1662
Cdd:COG1196 431 AELEEEEEEEE--EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1663 KWRQKANEALR------LRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQ 1736
Cdd:COG1196 509 GVKAALLLAGLrglagaVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1737 QKLTAEQELIRLRA-------DFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtm 1809
Cdd:COG1196 589 AAALARGAIGAAVDlvasdlrEADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS-- 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1810 snTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEK 1889
Cdd:COG1196 667 --RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
570 580 590
....*....|....*....|....*....|....
gi 1988774676 1890 EAENERLRRQAEDEAYQRKALEDQASQHKQEIEE 1923
Cdd:COG1196 745 EELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1368-2610 |
8.18e-36 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 151.13 E-value: 8.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1368 TDTQRRLDDEEKAAEKLKAEERKKMAEMQAELdkqkqlaeaHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEkqktn 1447
Cdd:NF041483 90 ADAERELRDARAQTQRILQEHAEHQARLQAEL---------HTEAVQRRQQLDQELAERRQTVESHVNENVAWAE----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1448 iqlelqELKNLSEQQIKdksQQVDEalhSRTKIEEEIRLIRIQLE--TTE-KQKYTAESELKQlrdraAEAEKLRKLAQD 1524
Cdd:NF041483 156 ------QLRARTESQAR---RLLDE---SRAEAEQALAAARAEAErlAEEaRQRLGSEAESAR-----AEAEAILRRARK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1525 EAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQaeEAERQVKQAEIEKEKQIKVAHEAAQKS- 1603
Cdd:NF041483 219 DAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAAAKQl 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1604 AAAELQSKHMSfaeKTSKLEeslkqehgaVLQLQQEAERlkkqqeDAENSREEAEKELEKWRQkanEALRLRLQAEDEAh 1683
Cdd:NF041483 297 ASAESANEQRT---RTAKEE---------IARLVGEATK------EAEALKAEAEQALADARA---EAEKLVAEAAEKA- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1684 kKTLAQEEAEKQKEEAEREAKK-RAKAEESALKQKEMAEEELERQRKIAESTAQqkltaeqeliRLRAD-FDNAEQQRSL 1761
Cdd:NF041483 355 -RTVAAEDTAAQLAKAARTAEEvLTKASEDAKATTRAAAEEAERIRREAEAEAD----------RLRGEaADQAEQLKGA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1762 LEDELYRLKNEVAAAQQQRKQLEDELAKVRSE-MDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEAsrlrais 1840
Cdd:NF041483 424 AKDDTKEYRAKTVELQEEARRLRGEAEQLRAEaVAEGERIRGEARREAVQQIEEAARTAEELLTKAKADADEL------- 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1841 eeakhqRQIAEEEAARQRAEAerilkeklaaISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQE 1920
Cdd:NF041483 497 ------RSTATAESERVRTEA----------IERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1921 IEEKIVQLKKS----------------------------SEAEMERQKAiVDDTLKQRRVVEEEIRILKLNFEK------ 1966
Cdd:NF041483 561 ETERAIAARQAeaaeeltrlhteaeerltaaeealadarAEAERIRREA-AEETERLRTEAAERIRTLQAQAEQeaerlr 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1967 ------ASSGKLDLE-----------LELNKLKNIADETQQsKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEE 2029
Cdd:NF041483 640 teaaadASAARAEGEnvavrlrseaaAEAERLKSEAQESAD-RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEET 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2030 AARQRKAALEELERLRKKAEE----ARKQKDEADKEAEKQIVVA-QQAAQKCSAAEQQvqsvlAQQIEDSIT--QKKLKE 2102
Cdd:NF041483 719 LGSARAEADQERERAREQSEEllasARKRVEEAQAEAQRLVEEAdRRATELVSAAEQT-----AQQVRDSVAglQEQAEE 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2103 EYEKakklakeaeaakekaereaalLRQQAEE-AERQKTaaeeeaanqaKAQEDAERLRKEAeFEAAKRAQAEAAALMQK 2181
Cdd:NF041483 794 EIAG---------------------LRSAAEHaAERTRT----------EAQEEADRVRSDA-YAERERASEDANRLRRE 841
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2182 QQADTEMAkhKKLAEQTLKQKFQvEQEltkvKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVK----VQ 2257
Cdd:NF041483 842 AQEETEAA--KALAERTVSEAIA-EAE----RLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQ 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2258 MEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMR-KLAEDAARLSVEAQ-EAARLRQIAEDDLNQQRALAEKMLKE 2335
Cdd:NF041483 915 ADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRaDAAAQAEQLIAEATgEAERLRAEAAETVGSAQQHAERIRTE 994
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2336 KMQAIQEASrlkAEAEMLQKQkdlAQEQAQKLL-EDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSqls 2414
Cdd:NF041483 995 AERVKAEAA---AEAERLRTE---AREEADRTLdEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTT--- 1065
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2415 eaqARAEEEAKKFKKQADKVATRLHETeiATQEKMTVVERleferlnTSKEADDL-----RKAIA---DLENEKARLKKE 2486
Cdd:NF041483 1066 ---TEAEAQADTMVGAARKEAERIVAE--ATVEGNSLVEK-------ARTDADELlvgarRDATAireRAEELRDRITGE 1133
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2487 AEELQNKSK-EMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQE 2565
Cdd:NF041483 1134 IEELHERARrESAEQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKAELVRE 1213
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....*
gi 1988774676 2566 KKTLQATMDAalskqkEAEEEMLRKQKEMQELERQRleqERILAE 2610
Cdd:NF041483 1214 AEKIKAEAEA------EAKRTVEEGKRELDVLVRRR---EDINAE 1249
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
185-289 |
1.23e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 133.26 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 185 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTR 264
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1988774676 265 LLDPEDVDVPHPDEKSIITYVSSLY 289
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
64-172 |
1.30e-35 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 132.74 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 64 DERDRVQKKTFTKWVNKHLIKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVK 142
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1988774676 143 LVNIRNDDIADGNPKLTLGLIWTIILHFQV 172
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1429-2004 |
9.53e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 147.01 E-value: 9.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1429 EEVSKR----EIAAVDAEKQKTnIQLELQELK-NLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAES 1503
Cdd:COG1196 196 GELERQleplERQAEKAERYRE-LKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1504 ELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVK 1583
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1584 QAEIEKEKQIKVAHEAAQKSAAAE-----LQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAE 1658
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEeeleeLAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1659 KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK 1738
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1739 LTAEQELIRLRAD---FDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKS 1815
Cdd:COG1196 515 LLAGLRGLAGAVAvliGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1816 KQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAE--EEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAEn 1893
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAArlEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA- 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1894 ERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEkassgKLD 1973
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE-----ELL 748
|
570 580 590
....*....|....*....|....*....|.
gi 1988774676 1974 LELELNKLKNIADETQQskiraEEEAEKLRK 2004
Cdd:COG1196 749 EEEALEELPEPPDLEEL-----ERELERLER 774
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
192-293 |
9.84e-35 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 129.86 E-value: 9.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 192 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 270
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1988774676 271 VDVPHPDEKSIITYVSSLYDAMP 293
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1334-2089 |
4.34e-34 |
|
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: 145.20 E-value: 4.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1334 KLDSASDNIIQEYVTLRTRYSELMTLTSQY---IKFitdtqRRLDDEEKAAEKL-----KAEERKKMAEMQAELDKQKQL 1405
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLERQAekaERY-----KELKAELRELELAllvlrLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1406 AEAHAKAIAKAEKEAQELKLKMQE------------EVSKREIAAVDAEKQKTNiqlelQELKNLsEQQIKDKSQQVDEA 1473
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSEleeeieelqkelYALANEISRLEQQKQILR-----ERLANL-ERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1474 LHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEA 1553
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1554 EKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHgav 1633
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA--- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1634 lQLQQEAERLKKQQEDAENsREEAEKELEKWRQKANEAL-----RLRLQAEDEAHKKTLAQEEAEKQKEeaerEAKKRAK 1708
Cdd:TIGR02168 486 -QLQARLDSLERLQENLEG-FSEGVKALLKNQSGLSGILgvlseLISVDEGYEAAIEAALGGRLQAVVV----ENLNAAK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1709 AEESALKQKE-----MAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLK--NEVAAAQQQRK 1781
Cdd:TIGR02168 560 KAIAFLKQNElgrvtFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvDDLDNALELAK 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1782 QLEDELAKVRSEMDIL----IQLKtKAEKETMSNTEKSKQLLEAEaAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQ 1857
Cdd:TIGR02168 640 KLRPGYRIVTLDGDLVrpggVITG-GSAKTNSSILERRREIEELE-EKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1858 RAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEdQASQHKQEIEEKIVQLkkssEAEME 1937
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEEL----EAQIE 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1938 RQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAE 2017
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 2018 EKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQ 2089
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1369-2004 |
6.93e-34 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 145.28 E-value: 6.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1369 DTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAiAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTni 1448
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD-- 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1449 qlELQELKNLSEQQIKDKSQQVDEALHSRTKIEEeirliriqlettekqKYTAESELKQLRDRAAEAEKLRKLAqdEAEK 1528
Cdd:PTZ00121 1358 --EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE---------------KKKADEAKKKAEEDKKKADELKKAA--AAKK 1418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1529 LRKQVSEETQKKRQAeEELKRKSEAEKEAAKQKQKALEdleklrmqAEEAERQVKQAEiEKEKQIKVAHEAAQKSAAAEL 1608
Cdd:PTZ00121 1419 KADEAKKKAEEKKKA-DEAKKKAEEAKKADEAKKKAEE--------AKKAEEAKKKAE-EAKKADEAKKKAEEAKKADEA 1488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1609 QSKhmsfAEKTSKLEESLKQEHGAvlqlQQEAERLKKQQE--DAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKT 1686
Cdd:PTZ00121 1489 KKK----AEEAKKKADEAKKAAEA----KKKADEAKKAEEakKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1687 LAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRaDFDNAEQQRSLLEDEL 1766
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLK 1639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1767 YRLKNEVAAAQQQRKqlEDELAKVRSEmdiliQLKTKAEKEtmsnTEKSKQLLEAEAAKMKdlAEEASRLRAisEEAKHQ 1846
Cdd:PTZ00121 1640 KKEAEEKKKAEELKK--AEEENKIKAA-----EEAKKAEED----KKKAEEAKKAEEDEKK--AAEALKKEA--EEAKKA 1704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1847 RQIAEEEAARQRaEAERILKEKLAAISEATRLKTEAEialkEKEAENERLRRQAEDeayqrkalEDQASQHKQEIEEKIV 1926
Cdd:PTZ00121 1705 EELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEAE----EDKKKAEEAKKDEEE--------KKKIAHLKKEEEKKAE 1771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1927 QLKKSSEAEMErqKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAD----ETQQSKIRAEEEAEKL 2002
Cdd:PTZ00121 1772 EIRKEKEAVIE--EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDsaikEVADSKNMQLEEADAF 1849
|
..
gi 1988774676 2003 RK 2004
Cdd:PTZ00121 1850 EK 1851
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
179-289 |
8.13e-34 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 128.25 E-value: 8.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 179 IQVNGQSEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEK 258
Cdd:cd21322 7 IETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQ 86
|
90 100 110
....*....|....*....|....*....|.
gi 1988774676 259 DLGVTRLLDPEDVDVPHPDEKSIITYVSSLY 289
Cdd:cd21322 87 HLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
62-168 |
1.30e-33 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 128.62 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 62 IADERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLRHRQ 140
Cdd:cd21316 46 LADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQR 125
|
90 100
....*....|....*....|....*...
gi 1988774676 141 VKLVNIRNDDIADGNPKLTLGLIWTIIL 168
Cdd:cd21316 126 VHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
189-289 |
2.83e-33 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 125.98 E-value: 2.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 189 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 268
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1988774676 269 EDVDVPHPDEKSIITYVSSLY 289
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1799-2669 |
8.84e-33 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 141.82 E-value: 8.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1799 QLKTKAEKETmsnTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAE---EEAARQRAEAERILKEKLAAISEA 1875
Cdd:PTZ00121 1083 AKEDNRADEA---TEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEarkAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1876 TRLKTEAEIALKEKEAENERLRRQAEDeayQRKALEDQASQHKQEIE-----EKIVQLKKSSEAEMERQKAIVDDTLKQR 1950
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEaarkaEEERKAEEARKAEDAKKAEAVKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1951 RVVEEEIRIlklnfEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEA 2030
Cdd:PTZ00121 1237 KDAEEAKKA-----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2031 ARQRKA---------ALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSV--LAQQIEDSITQKK 2099
Cdd:PTZ00121 1312 EEAKKAdeakkkaeeAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkKADAAKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2100 LKEEyekakklakeaeaakekaereaalLRQQAEEAERQktaaEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALM 2179
Cdd:PTZ00121 1392 KADE------------------------AKKKAEEDKKK----ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA 1443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2180 QKQQADTEMAKHKKLAEQtLKQKFQVEQELTKVKLKLDETDKQksvldEELQRLKDEVDDAVKQRGQVEEElfkvKVQME 2259
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEE-AKKKAEEAKKADEAKKKAEEAKKA-----DEAKKKAEEAKKKADEAKKAAEA----KKKAD 1513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2260 ELLKLKNKIEEENQRLIKKDKDSTQKLLAEE---AENMRKLAE----DAARLSVEAQEAARLRQIAEDDLNQQRALAEKM 2332
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEkkkADELKKAEElkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2333 LKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERkrqleimaEAERLRLQVSQ 2412
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK--------AEEENKIKAAE 1665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2413 LSEAQARAEEEAKKFKKqADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQN 2492
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKK-AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2493 KSKEMA--DAQQKKIEH---EKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQfeeevKKAKALKDEQERQKQQMEQEKK 2567
Cdd:PTZ00121 1745 KAEEAKkdEEEKKKIAHlkkEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD-----KKIKDIFDNFANIIEGGKEGNL 1819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2568 TLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQK----LREKLQQLEDAQKDQHTRETDKVLHKDIi 2643
Cdd:PTZ00121 1820 VINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKeadfNKEKDLKEDDEEEIEEADEIEKIDKDDI- 1898
|
890 900
....*....|....*....|....*.
gi 1988774676 2644 hltTIETTKTVYNGQNVGDVVDGIDK 2669
Cdd:PTZ00121 1899 ---EREIPNNNMAGKNNDIIDDKLDK 1921
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
68-173 |
1.59e-31 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 121.40 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 68 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLRHRQ-VKLV 144
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 1988774676 145 NIRNDDIADGNPKLTLGLIWTIILHFQVS 173
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1522-2375 |
1.88e-31 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 137.19 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1522 AQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRmQAEEAERQVKQAEIEKEKQIKVAHEAAQ 1601
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEAR-KAEDAKRVEIARKAEDARKAEEARKAED 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1602 -KSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDaenSREEAEKELEKWRQKANEALRLRLQAED 1680
Cdd:PTZ00121 1175 aKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA---KKAEAVKKAEEAKKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1681 EAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEEL---ERQRKIAESTAQQKLTAEQELIRLRADFDNAEQ 1757
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1758 QRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDiliQLKTKAEKEtmsntekskqllEAEAAKMKdlAEEASRLR 1837
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA---EKKKEEAKK------------KADAAKKK--AEEKKKAD 1394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1838 AISEEAKHQRQIAEE----EAARQRAEAeriLKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQ 1913
Cdd:PTZ00121 1395 EAKKKAEEDKKKADElkkaAAAKKKADE---AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1914 ASQHKQEIEEKIVQLKKSSEAEMERQKAivdDTLKQRrvveEEIRILKLNFEKASSGKLDLELELNKLKNIADETQqski 1993
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKA---DEAKKA----AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK---- 1540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1994 RAEE--EAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQ----RKAALEELERLRKKAEEARKQKDEADKEAEKQIV 2067
Cdd:PTZ00121 1541 KAEEkkKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2068 VAQQAAQkcsaaEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAA 2147
Cdd:PTZ00121 1621 KAEELKK-----AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2148 NQAKAQEDAERLRKEAEFEAAkraqaeaaalmQKQQADTEMAKHKKLAEQTLKQKfqvEQELTKV-KLKLDETDKQKsvl 2226
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKK-----------KAEELKKAEEENKIKAEEAKKEA---EEDKKKAeEAKKDEEEKKK--- 1758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2227 deeLQRLKDEVDDAVKQRGQVEEELFKvkvqmEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSV 2306
Cdd:PTZ00121 1759 ---IAHLKKEEEKKAEEIRKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDS 1830
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774676 2307 EAQEAArlrqiaeDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQ 2375
Cdd:PTZ00121 1831 AIKEVA-------DSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEK 1892
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
69-172 |
2.07e-31 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 120.50 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 69 VQKKTFTKWVNKHLIKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKLVNIR 147
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1988774676 148 NDDIADGNPKLTLGLIWTIILHFQV 172
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
188-286 |
2.82e-31 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 120.22 E-value: 2.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 188 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 267
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1988774676 268 PEDVDVPHPDEKSIITYVS 286
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
69-172 |
1.19e-30 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 118.54 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 69 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLRHRQVKLVNI 146
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1988774676 147 RNDDIADGNPKLTLGLIWTIILHFQV 172
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
176-291 |
1.28e-30 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 118.78 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 176 ISDIQvngqSEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 255
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774676 256 AEKDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLYDA 291
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
188-286 |
2.63e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 117.63 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 188 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 267
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1988774676 268 PEDVDVPHPDEKSIITYVS 286
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
192-294 |
3.41e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 117.34 E-value: 3.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 192 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLGVTRLLDPE 269
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1988774676 270 DVDVPHPDEKSIITYVSSLYDAMPR 294
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
65-172 |
9.14e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 116.14 E-value: 9.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 65 ERDRVQKKTFTKWVNKHLIKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLRHRQ 140
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|..
gi 1988774676 141 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 172
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQI 112
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
192-293 |
9.41e-30 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 115.83 E-value: 9.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 192 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 270
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1988774676 271 VDVPHPDEKSIITYVSSLYDAMP 293
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
68-170 |
2.19e-29 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 114.89 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 68 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 144
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1988774676 145 NIRNDDIADGNPKLTLGLIWTIILHF 170
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
194-289 |
3.52e-29 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 113.98 E-value: 3.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 194 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED-VD 272
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1988774676 273 VPHPDEKSIITYVSSLY 289
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1528-2138 |
6.82e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 128.13 E-value: 6.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1528 KLRKqvsEETQKK-RQAEEELKRKSEAEKEAAKQkqkaledLEKLRMQAEEAER--QVKQAEIEKEKQIKVAH------- 1597
Cdd:COG1196 171 KERK---EEAERKlEATEENLERLEDILGELERQ-------LEPLERQAEKAERyrELKEELKELEAELLLLKlreleae 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1598 EAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQ 1677
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1678 AEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQ 1757
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1758 QRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLR 1837
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1838 AISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQH 1917
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1918 KQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEE 1997
Cdd:COG1196 561 AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1998 EAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCS 2077
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774676 2078 AAEQQVQSVLAQQIEdsITQKKLKEEYEKAKKLAKEAEAAKEKAEReaalLRQQAEEAERQ 2138
Cdd:COG1196 721 LEEEALEEQLEAERE--ELLEELLEEEELLEEEALEELPEPPDLEE----LERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1513-2369 |
4.12e-28 |
|
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: 125.55 E-value: 4.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1513 AEAEKLRKLAQDEAEKLR-KQVSEETQKK-RQAEEELKRKSEAEKEAAKQkqkaledLEKLRMQAEEAER------QVKQ 1584
Cdd:TIGR02168 152 AKPEERRAIFEEAAGISKyKERRKETERKlERTRENLDRLEDILNELERQ-------LKSLERQAEKAERykelkaELRE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1585 AEIE---KEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAEN--SREEAEK 1659
Cdd:TIGR02168 225 LELAllvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeiSRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1660 ELEKWRQKANEALRLRLQAEDEAHKKTLAQEEaekqkeeaeREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKL 1739
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELA---------EELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1740 TAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDiliqlkTKAEKETMSNTEKSKQLL 1819
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE------EAELKELQAELEELEEEL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1820 EAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEaerilKEKLAAISEATRLKTEAEIALKEKEAE------- 1892
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR-----LDSLERLQENLEGFSEGVKALLKNQSGlsgilgv 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1893 -NERLRRQAEDE----AYQRKALEDQASQHKQEIEEKIVQLKKSS-------EAEMERQKAIVDDTLKQRRVVEEEIRIL 1960
Cdd:TIGR02168 525 lSELISVDEGYEaaieAALGGRLQAVVVENLNAAKKAIAFLKQNElgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1961 KLNFEKASSGKLDLELELNKL---KNIADETQQSKIRAEEE-------------------AEKLRKLALEEEKRRREAEE 2018
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYLLGGVlvvDDLDNALELAKKLRPGYrivtldgdlvrpggvitggSAKTNSSILERRREIEELEE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2019 KVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDeadkEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQiedSITQK 2098
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELE----ELSRQISALRKDLARLEAEVEQLEERIAQL---SKELT 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2099 KLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTaaeEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAAL 2178
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK---ALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2179 MQKQQADTEMAKHKKLAEQTLK---QKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVK 2255
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESlaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2256 vqmEELLKLKNKIEEENQRLikkdkdstQKLLAEEAENMRKLAEDAarlSVEAQEAARLRQIAEDDLNQQRALAEKmLKE 2335
Cdd:TIGR02168 915 ---RELEELREKLAQLELRL--------EGLEVRIDNLQERLSEEY---SLTLEEAEALENKIEDDEEEARRRLKR-LEN 979
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1988774676 2336 K--------MQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLE 2369
Cdd:TIGR02168 980 KikelgpvnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
176-291 |
5.61e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 108.63 E-value: 5.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 176 ISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 255
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774676 256 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 291
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
68-170 |
7.67e-27 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 107.57 E-value: 7.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 68 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 144
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1988774676 145 NIRNDDIADGNPKLTLGLIWTIILHF 170
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
175-291 |
1.32e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 107.48 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 175 SISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFS 254
Cdd:cd21290 3 AIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFE 78
|
90 100 110
....*....|....*....|....*....|....*...
gi 1988774676 255 VAEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 291
Cdd:cd21290 79 VAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1371-1930 |
3.94e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 119.86 E-value: 3.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1371 QRRLDDEEKAAEKL--KAEERKKMAEMQAELDKQKQLAEAHAKAiAKAEKEAQELKlKMQEEVSKREIAAVDAEKQKTNI 1448
Cdd:PTZ00121 1370 EKKKEEAKKKADAAkkKAEEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAK-KKAEEKKKADEAKKKAEEAKKAD 1447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1449 QLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAE----SELKQLRDRAAEAEKLRKL--A 1522
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkaAEAKKKADEAKKAEEAKKAdeA 1527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1523 QDEAEKLRKQVSEETQKKRQAEEELK----RKSEaEKEAAKQKQKALEDLEKLRMQAEEAeRQVKQAEIEK-----EKQI 1593
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKaeelKKAE-EKKKAEEAKKAEEDKNMALRKAEEA-KKAEEARIEEvmklyEEEK 1605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1594 KVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGavlQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALR 1673
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA---EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1674 lrlqAEDEAHKKtlaqeeaekqKEEAEREAKKRAKAEEsaLKQKEmaEEELERQRKIAESTAQQKLTAEQELIRLRADFD 1753
Cdd:PTZ00121 1683 ----AEEDEKKA----------AEALKKEAEEAKKAEE--LKKKE--AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1754 NAEQQRSLLEDelyrlKNEVaaaQQQRKQLEDELAKVRSEMDILIQ--LKTKAEKETMSNTEKSKQLL------------ 1819
Cdd:PTZ00121 1745 KAEEAKKDEEE-----KKKI---AHLKKEEEKKAEEIRKEKEAVIEeeLDEEDEKRRMEVDKKIKDIFdnfaniieggke 1816
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1820 ---------EAEAAKMKDLAEEASRLRAISEE-AKHQRQIAEEEAARQRAEA----ERILKEKLAAISEATRLKTEAEIA 1885
Cdd:PTZ00121 1817 gnlvindskEMEDSAIKEVADSKNMQLEEADAfEKHKFNKNNENGEDGNKEAdfnkEKDLKEDDEEEIEEADEIEKIDKD 1896
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1988774676 1886 LKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKK 1930
Cdd:PTZ00121 1897 DIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIKISK 1941
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1702-2621 |
4.16e-26 |
|
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: 119.31 E-value: 4.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1702 EAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRadfDNAEQQRSLLEDELYRLKNEVAAAQQQRK 1781
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALE---YYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1782 QLEDELAKVRSEMDILIQLKTKAEKETmsntEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEA 1861
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKL----AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1862 ERILKEKLAAISEATRLKTEAEIALKEKEaENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKa 1941
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEIEELEKELK-ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1942 ivddtlKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIaDETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVK 2021
Cdd:pfam02463 395 ------EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI-LEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2022 KIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVaqqaaqkcsaaeQQVQSVLAQQIEDSITQKKLK 2101
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA------------LIKDGVGGRIISAHGRLGDLG 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2102 EEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQK 2181
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2182 QQADTEMAKHKKLAEQTLKQKFQveqelTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEEL 2261
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLK-----ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2262 lKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRklaedaarlsveaqeaARLRQIAEDDLNQQRALAEKMLKEKMQAIQ 2341
Cdd:pfam02463 691 -KEEILRRQLEIKKKEQREKEELKKLKLEAEELL----------------ADRVQEAQDKINEELKLLKQKIDEEEEEEE 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2342 EASRLKAEAEMLQKQkdlaQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAE 2421
Cdd:pfam02463 754 KSRLKKEEKEEEKSE----LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2422 EEAKKFKKQADKVATRLHETEIATQEKMTVverLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQ 2501
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAEEELERL---EEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEES 906
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2502 QKKIEHEKTVLQQTFMTEKEmlLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTL------------ 2569
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEE--AEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELgkvnlmaieefe 984
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 1988774676 2570 --QATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQ 2621
Cdd:pfam02463 985 ekEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFF 1038
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
68-173 |
7.78e-26 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 105.50 E-value: 7.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 68 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLRHRQVKLV 144
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1988774676 145 NIRNDDIADGNPKLTLGLIWTIILHFQVS 173
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
61-172 |
9.22e-26 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 105.23 E-value: 9.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 61 RIADERDRVQKKTFTKWVNKHLIKAQRHV--TDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLR 137
Cdd:cd21247 12 KLQEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLK 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 1988774676 138 HR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQV 172
Cdd:cd21247 92 TKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1852-2635 |
1.21e-25 |
|
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: 117.46 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1852 EEAA------RQRAEAERilkeKLAAISEA-TRLkteaEIALKEKEAENERLRRQAEdEAYQRKALEDQASQHK------ 1918
Cdd:TIGR02168 162 EEAAgiskykERRKETER----KLERTRENlDRL----EDILNELERQLKSLERQAE-KAERYKELKAELRELElallvl 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1919 --QEIEEKIVQLKkSSEAEMERQKAIVDDTLKqrrVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAE 1996
Cdd:TIGR02168 233 rlEELREELEELQ-EELKEAEEELEELTAELQ---ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1997 EEAEKLRKlaleeekrrreaeeKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKC 2076
Cdd:TIGR02168 309 ERLANLER--------------QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2077 SAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDA 2156
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2157 ERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQE----LTKVKLKLD----------ETDKQ 2222
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEgvkaLLKNQSGLSgilgvlseliSVDEG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2223 KS-----VLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKL 2297
Cdd:TIGR02168 535 YEaaieaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2298 A----------------EDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAI---QEASRLKAEAEMLQKQKD 2358
Cdd:TIGR02168 615 RkalsyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILerrREIEELEEKIEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2359 LAQEQAQKLLEDkqlmQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRL 2438
Cdd:TIGR02168 695 ELEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2439 HETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKsKEMADAQQKKIEHEKTVLQQTFMT 2518
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-LESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2519 EKEMLLKKEKLIEDEKKRLEsQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQ--E 2596
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIE-ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAqlE 928
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1988774676 2597 LERQRLEQEriLAEENQKLREKLQ-QLEDAQKDQHTRETD 2635
Cdd:TIGR02168 929 LRLEGLEVR--IDNLQERLSEEYSlTLEEAEALENKIEDD 966
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
192-291 |
1.70e-25 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 103.52 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 192 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED- 270
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1988774676 271 VDVPHPDEKSIITYVSSLYDA 291
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1654-2288 |
2.38e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 116.57 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1654 REEAEKELEKWRQKANEALR-LRLQAEDEAHKKTLAQEEAekqkeeaeREAKKRAKAEESALKQKEMAEEELERQRKIAE 1732
Cdd:COG1196 195 LGELERQLEPLERQAEKAERyRELKEELKELEAELLLLKL--------RELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1733 STAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNT 1812
Cdd:COG1196 267 AELEE---LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1813 EKSKQLLEAEAAKMKDLAEEASRL----RAISEEAKHQRQIAEEEAARQRAEAErILKEKLAAISEATRLKTEAEIALKE 1888
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALleaeAELAEAEEELEELAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1889 KEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRI-LKLNFEKA 1967
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLlLLLEAEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1968 SSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKK 2047
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKI 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2048 AEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAqqiEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAAL 2127
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL---GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2128 LRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQ 2207
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2208 ELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQR---GQV----EEELFKVKVQMEELLKLKNKIEEENQRL---IK 2277
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIealGPVnllaIEEYEELEERYDFLSEQREDLEEARETLeeaIE 819
|
650
....*....|..
gi 1988774676 2278 K-DKDSTQKLLA 2288
Cdd:COG1196 820 EiDRETRERFLE 831
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1262-1931 |
2.70e-25 |
|
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: 116.31 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1262 KIQAVPITDSKTLKEQLAQEKK--LLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVspLKKTKLDSAS 1339
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1340 DNIIQEYVTLRTRYSELmtltSQYIKFITDTQRRLDDEEKAAEKLKAEERKK-------MAEMQAELDKQKQLAEAHAKA 1412
Cdd:TIGR02168 284 EELQKELYALANEISRL----EQQKQILRERLANLERQLEELEAQLEELESKldelaeeLAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1413 IAKAEKEAQELKLKM---QEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEE-EIRLIR 1488
Cdd:TIGR02168 360 LEELEAELEELESRLeelEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1489 IQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAE---EELKRKSEAEKEAAKQK---- 1561
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLErlqENLEGFSEGVKALLKNQsgls 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1562 ----------------QKALEDLEKLRMQA---EEAERQVKQAEIEKEKQI-KVAHEAAQKSAAAELQSKHM-------- 1613
Cdd:TIGR02168 520 gilgvlselisvdegyEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELgRVTFLPLDSIKGTEIQGNDReilknieg 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1614 ---------SFAEKTSKLEESL--------------------------------------------KQEHGAVLQLQQEA 1640
Cdd:TIGR02168 600 flgvakdlvKFDPKLRKALSYLlggvlvvddldnalelakklrpgyrivtldgdlvrpggvitggsAKTNSSILERRREI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1641 ERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMA 1720
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1721 EEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSL-------LEDELYRLKNEVAAAQQQRKQLEDELAKVRSE 1793
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealdeLRAELTLLNEEAANLRERLESLERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1794 MDILIQlKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAIS 1873
Cdd:TIGR02168 840 LEDLEE-QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 1874 EATRLKTEAEIALKEKEAE----NERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKS 1931
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRidnlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
176-291 |
5.12e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 102.88 E-value: 5.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 176 ISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 255
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774676 256 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 291
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1371-2244 |
5.52e-25 |
|
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: 115.45 E-value: 5.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1371 QRRLDDEEKAAE----KLKAEERKKMAEMQAELDKQ---KQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEK 1443
Cdd:pfam02463 153 ERRLEIEEEAAGsrlkRKKKEALKKLIEETENLAELiidLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1444 QKTNIQLELQELKNLSEQQIKDKSQQVDEalhsrtKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQ 1523
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIE------KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1524 DEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKS 1603
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1604 AAA------ELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQ 1677
Cdd:pfam02463 387 SSAaklkeeELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1678 AEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQ-----KLTAEQELIRLRADF 1752
Cdd:pfam02463 467 LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISahgrlGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1753 DNAEQQRSLLEDELYRLKNEVAA-------AQQQRKQLEDELAKVRS----EMDILIQLKTKAEKETMSNTEKSKQLLEA 1821
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRAltelplgARKLRLLIPKLKLPLKSiavlEIDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1822 EAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKlaaiseaTRLKTEAEIALKEKEAENERLRRQAE 1901
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTK-------ELLEIQELQEKAESELAKEEILRRQL 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1902 DEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRilklnfEKASSGKLDLELELNKL 1981
Cdd:pfam02463 700 EIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSR------LKKEEKEEEKSELSLKE 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1982 KNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKE 2061
Cdd:pfam02463 774 KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2062 AEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAErqkta 2141
Cdd:pfam02463 854 EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE----- 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2142 AEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMaKHKKLAEQTLKQKFQVEQELTKVKLKLDETDK 2221
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKV-NLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007
|
890 900
....*....|....*....|...
gi 1988774676 2222 QKSVLDEELQRLKDEVDDAVKQR 2244
Cdd:pfam02463 1008 IRAIIEETCQRLKEFLELFVSIN 1030
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
188-294 |
5.58e-25 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 102.36 E-value: 5.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 188 MTAKEKLLLWSQRMTDGY-QGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQT--NLENLEQAFSVAEKDLGVTR 264
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEfdKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1988774676 265 -LLDPEDVDvpHPDEKSIITYVSSLYDAMPR 294
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
194-289 |
1.30e-24 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 101.07 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 194 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED-VD 272
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1988774676 273 VPHPDEKSIITYVSSLY 289
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1415-2345 |
2.34e-24 |
|
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: 113.23 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1415 KAEKEAQELKL-KMQEEVSKREIAAVDAEKQKTNIQL------ELQELKN-LSEQQIKDKSQQVDEALHSRTKIEEEIRL 1486
Cdd:TIGR02168 171 KERRKETERKLeRTRENLDRLEDILNELERQLKSLERqaekaeRYKELKAeLRELELALLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1487 IRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALE 1566
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1567 DLEKLrmQAEEAERQVKQAEIEKEKQikvaheaAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQ 1646
Cdd:TIGR02168 331 KLDEL--AEELAELEEKLEELKEELE-------SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1647 QEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAqeeaekqkeeaereakKRAKAEESALKQKEMAEEELER 1726
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE----------------ELEEELEELQEELERLEEALEE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1727 QRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDeLYRLKNEVAAAQQQRKQLED---ELAKVRS--EMDILIQLK 1801
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEG-FSEGVKALLKNQSGLSGILGvlsELISVDEgyEAAIEAALG 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1802 TKAEKETMSNTEKSKQLLEA--EAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRA--------EAERILKEKLAA 1871
Cdd:TIGR02168 545 GRLQAVVVENLNAAKKAIAFlkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAkdlvkfdpKLRKALSYLLGG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1872 ISEATRLKTEAEIALKEKEAEN------ERLRRQAedeayqrkaledqasqhkqeieekiVQLKKSSEAEMERqkaivdd 1945
Cdd:TIGR02168 625 VLVVDDLDNALELAKKLRPGYRivtldgDLVRPGG-------------------------VITGGSAKTNSSI------- 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1946 tLKQRRvveeEIRILKLNFEKASSGKLDLELELNKLKNIADEtqqskirAEEEAEKLRKLALEEEKRRREAEEKVKKIAA 2025
Cdd:TIGR02168 673 -LERRR----EIEELEEKIEELEEKIAELEKALAELRKELEE-------LEEELEQLRKELEELSRQISALRKDLARLEA 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2026 AEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQqiedsitQKKLKEEYE 2105
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA-------LDELRAELT 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2106 KAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEaakraqaEAAALMQKQQAD 2185
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE-------LEALLNERASLE 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2186 TEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDdavKQRGQVEEElfkVKVQMEELLKLK 2265
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID---NLQERLSEE---YSLTLEEAEALE 960
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2266 NKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEdaarlsveaqeaarLRQIAE--DDLNQQRALAEKMLKEKMQAIQEA 2343
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKELGPVNLAAIEE--------------YEELKEryDFLTAQKEDLTEAKETLEEAIEEI 1026
|
..
gi 1988774676 2344 SR 2345
Cdd:TIGR02168 1027 DR 1028
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
72-169 |
3.00e-24 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 99.70 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 72 KTFTKWVNKHLIKA-QRHVTDLYEDLRDGHNLISLLEVLSGETLPREK---GRMRFHKLQNVQIALDFLRHRQVKLVNIR 147
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1988774676 148 NDDIADGnPKLTLGLIWTIILH 169
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1812-2487 |
3.62e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.72 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1812 TEKSKQL--LEAEAAKmkdlaeeASRLRAISEEAKhQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEK 1889
Cdd:COG1196 196 GELERQLepLERQAEK-------AERYRELKEELK-ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1890 EAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAivdDTLKQRRVVEEEIRILKLNFEKASS 1969
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE---ELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1970 GKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLrkkaE 2049
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL----E 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2050 EARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLR 2129
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2130 QQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAaLMQKQQADTEMAKHKKLAEQTLKQKFQVEQEL 2209
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA-LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2210 TKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNK-IEEENQRLIKKDKDSTQKLLA 2288
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRrAVTLAGRLREVTLEGEGGSAG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2289 EEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLL 2368
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2369 EDKQLMQQRLEEETEEYHKSLEVErkrqlEIMAEAERLRLQVSQLSeaqaraeeeakkfkkqadKVATRlheteiATQEK 2448
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLE-----ELERELERLEREIEALG------------------PVNLL------AIEEY 790
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1988774676 2449 MTVVERLEF--ERLNT-SKEADDLRKAIADLENEKARLKKEA 2487
Cdd:COG1196 791 EELEERYDFlsEQREDlEEARETLEEAIEEIDRETRERFLET 832
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1639-2635 |
6.40e-24 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 112.23 E-value: 6.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1639 EAERLKKQQEDAENSREEAEKELEKWRQKANEALR------------LRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKR 1706
Cdd:NF041483 23 EMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRslasrpaydgadIGYQAEQLLRNAQIQADQLRADAERELRDARAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1707 AK------AEESALKQKEMAEEELERQRKIAESTAQQKLTAEQ---------ELIRLRADfdnaEQQRSLLEDELYRLKN 1771
Cdd:NF041483 103 TQrilqehAEHQARLQAELHTEAVQRRQQLDQELAERRQTVEShvnenvawaEQLRARTE----SQARRLLDESRAEAEQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1772 EVAAA--------QQQRKQLEDELAKVRSEMD-ILIQLKTKAEK----------ETMSNTEKSKQLLEAEAAKMKDLAEE 1832
Cdd:NF041483 179 ALAAAraeaerlaEEARQRLGSEAESARAEAEaILRRARKDAERllnaastqaqEATDHAEQLRSSTAAESDQARRQAAE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1833 ASR------------LRAISEEAKHQRQIAEEEAARQRAEAE-------RILKEKLA-----AISEATRLKTEAEIALKE 1888
Cdd:NF041483 259 LSRaaeqrmqeaeeaLREARAEAEKVVAEAKEAAAKQLASAEsaneqrtRTAKEEIArlvgeATKEAEALKAEAEQALAD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1889 KEAENERLRRQAEDEAyQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRilKLNFEKAS 1968
Cdd:NF041483 339 ARAEAEKLVAEAAEKA-RTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEAD--RLRGEAAD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1969 SGkldlelelNKLKNIA-DETQQSKIRA---EEEAEKLRKLAleeekrrreaeekvkkiaaaeeeaARQRKAALEELERL 2044
Cdd:NF041483 416 QA--------EQLKGAAkDDTKEYRAKTvelQEEARRLRGEA------------------------EQLRAEAVAEGERI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2045 RKKA-EEARKQKDEADKEAEKQIVVAQQAAQKC-SAAEQQVQSVLAQQIEDSITQKKLKEEyekakklakeaeaakekae 2122
Cdd:NF041483 464 RGEArREAVQQIEEAARTAEELLTKAKADADELrSTATAESERVRTEAIERATTLRRQAEE------------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2123 reaaLLRQQAEEAERQKTaaeeeaanqaKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQ-QADTEMAKHKKLAEQTLKq 2201
Cdd:NF041483 525 ----TLERTRAEAERLRA----------EAEEQAEEVRAAAERAARELREETERAIAARQaEAAEELTRLHTEAEERLT- 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2202 kfQVEQELTKVKlklDETDKQKSVLDEELQRLKDEVDDAVKQ-RGQVEEELFKVKVQMEE------------LLKLKNKI 2268
Cdd:NF041483 590 --AAEEALADAR---AEAERIRREAAEETERLRTEAAERIRTlQAQAEQEAERLRTEAAAdasaaraegenvAVRLRSEA 664
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2269 EEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQ-EAARLRQIAEDDLNQQRALAEkmlKEKMQAIQEASRLK 2347
Cdd:NF041483 665 AAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQeEAARRRREAEETLGSARAEAD---QERERAREQSEELL 741
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2348 AEAemlQKQKDLAQEQAQKLLED------------KQLMQQ------RLEEETEEYHKSLE------VERKRQlEIMAEA 2403
Cdd:NF041483 742 ASA---RKRVEEAQAEAQRLVEEadrratelvsaaEQTAQQvrdsvaGLQEQAEEEIAGLRsaaehaAERTRT-EAQEEA 817
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2404 ERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIAtqEKMTVVERLefeRLNTSKEADDLR----KAIADLENE 2479
Cdd:NF041483 818 DRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVS--EAIAEAERL---RSDASEYAQRVRteasDTLASAEQD 892
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2480 KARLKKEAEELQNKSKEMADAQQKKIEHEKTVlqqtfmtekemllkkekliEDEKKRLESQFEEEVKKAKALKDEQERQK 2559
Cdd:NF041483 893 AARTRADAREDANRIRSDAAAQADRLIGEATS-------------------EAERLTAEARAEAERLRDEARAEAERVRA 953
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2560 QQMEQEKKTLQATMDAALSKQKEAEEEMLRKQkemQELERQRLEQERILAE---ENQKLREKLQQ-----LEDAQKDQHT 2631
Cdd:NF041483 954 DAAAQAEQLIAEATGEAERLRAEAAETVGSAQ---QHAERIRTEAERVKAEaaaEAERLRTEAREeadrtLDEARKDANK 1030
|
....
gi 1988774676 2632 RETD 2635
Cdd:NF041483 1031 RRSE 1034
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
192-292 |
9.12e-24 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 98.69 E-value: 9.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 192 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPEDV 271
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1988774676 272 DVPHPDEKSIITYVSSLYDAM 292
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1548-2490 |
1.05e-23 |
|
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: 111.30 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1548 KRKSEAEK--EAAKQKQKALED-LEKLRMQAEEAERQVKQAEieKEKQIKVAHEAAQKS-AAAELQSKHmsfaEKTSKLE 1623
Cdd:TIGR02168 172 ERRKETERklERTRENLDRLEDiLNELERQLKSLERQAEKAE--RYKELKAELRELELAlLVLRLEELR----EELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1624 ESLKQehgavlqLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREA 1703
Cdd:TIGR02168 246 EELKE-------AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1704 KKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQL 1783
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1784 EDELAKVRSEMDiliQLKTKAEKETmsnTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAER 1863
Cdd:TIGR02168 399 NNEIERLEARLE---RLEDRRERLQ---QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1864 ILKEKLAAISEATRLKTEAEIAlkekeaenERLRRQAEDEAYQRKALEDQASQHKQEIEE--KIVQLKKSSEAEME---- 1937
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSL--------ERLQENLEGFSEGVKALLKNQSGLSGILGVlsELISVDEGYEAAIEaalg 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1938 -RQKAIVDDTLKQrrvVEEEIRILKlnfeKASSGKLDLeLELNKLKniADETQQSKIRAEEEAEKLRKLALEEEKRRREA 2016
Cdd:TIGR02168 545 gRLQAVVVENLNA---AKKAIAFLK----QNELGRVTF-LPLDSIK--GTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2017 EEKVKKIAAAEEEAARQRKAaleeLERLRKKAEEARKQKDEADKEAEKQIVVAqqaaqkcsAAEQQVQSVLAQQIEdsit 2096
Cdd:TIGR02168 615 RKALSYLLGGVLVVDDLDNA----LELAKKLRPGYRIVTLDGDLVRPGGVITG--------GSAKTNSSILERRRE---- 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2097 qkkLKEeyekakklakeaeaakekaereaalLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAA 2176
Cdd:TIGR02168 679 ---IEE-------------------------LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2177 ALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKV 2256
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2257 QMEELLKLKNKIEEENQRLiKKDKDSTQKLLAEEAENMRKLAEDAARLSVEaqeaarlrqiaeddLNQQRALAEKM---- 2332
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESL-ERRIAATERRLEDLEEQIEELSEDIESLAAE--------------IEELEELIEELesel 875
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2333 ---LKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKsLEVERKRQLEIMAEAERLRLQ 2409
Cdd:TIGR02168 876 ealLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLE 954
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2410 -VSQLSEAQARAEEEAKKFKKQADKVATRLHETEI-ATQEKMTVVERLEFerlnTSKEADDLRKAIADLENEKARLKKEA 2487
Cdd:TIGR02168 955 eAEALENKIEDDEEEARRRLKRLENKIKELGPVNLaAIEEYEELKERYDF----LTAQKEDLTEAKETLEEAIEEIDREA 1030
|
...
gi 1988774676 2488 EEL 2490
Cdd:TIGR02168 1031 RER 1033
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
189-289 |
1.14e-23 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 98.27 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 189 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 268
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1988774676 269 EDV---DVphPDEKSIITYVSSLY 289
Cdd:cd21198 80 ADMvllSV--PDKLSVMTYLHQIR 101
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
176-291 |
1.22e-23 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 98.99 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 176 ISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 255
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774676 256 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 291
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1701-2574 |
2.71e-23 |
|
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: 109.76 E-value: 2.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1701 REAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKltaeQELIRLRADFDNAEQQRSL-----LEDELYRLKNEVAA 1775
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKA----ERYKELKAELRELELALLVlrleeLREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1776 AQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtmsntekskqlLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAA 1855
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1856 RQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHkQEIEEKIVQLKKSSEAE 1935
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL-ETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1936 MERQKAIvDDTLKQ--RRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRR 2013
Cdd:TIGR02168 399 NNEIERL-EARLERleDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2014 REAEEKVKKIaaaeeeaaRQRKAALEEL-ERLRKKAEEARKQKDEADKEAEKQIVVAQQ--AAQKCSAAeqqVQSVLAQQ 2090
Cdd:TIGR02168 478 DAAERELAQL--------QARLDSLERLqENLEGFSEGVKALLKNQSGLSGILGVLSELisVDEGYEAA---IEAALGGR 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2091 IEDSITQKKlkeeyekAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKR 2170
Cdd:TIGR02168 547 LQAVVVENL-------NAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2171 AQAEAAALMQKQQADTEMAKHKK-------LAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQ 2243
Cdd:TIGR02168 620 YLLGGVLVVDDLDNALELAKKLRpgyrivtLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKA 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2244 RGQVEEELfkvkVQMEELLKLKNKIEEENQRLIkkdkDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLN 2323
Cdd:TIGR02168 700 LAELRKEL----EELEEELEQLRKELEELSRQI----SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2324 QQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKL---LEDKQLMQQRLEEETEEYHKSLEVERKRQLEIM 2400
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2401 AEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEK 2480
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2481 ARLKKEAEELQnkskemadaqqKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFE----------EEVKKAKA 2550
Cdd:TIGR02168 932 EGLEVRIDNLQ-----------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaiEEYEELKE 1000
|
890 900
....*....|....*....|....
gi 1988774676 2551 LKDEQERQKQQMEQEKKTLQATMD 2574
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEEAIE 1024
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1274-1868 |
3.02e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 109.64 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1274 LKEQLAQEKKLLEEIEQNKDKVDECQKyakayidTIKDYELQLVAYKAQVEplvsplkktKLDSASDNIIQEYVTLRTRY 1353
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEA-------ELAELEAELEELRLELE---------ELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1354 SELmtltSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSK 1433
Cdd:COG1196 298 ARL----EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1434 REiAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAA 1513
Cdd:COG1196 374 LA-EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1514 EA-EKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQ 1592
Cdd:COG1196 453 ELeEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1593 IKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKqehgavlqlQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAL 1672
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLK---------AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1673 RLRLQAEDEAHKKTLAQEEAEKQKEEAERE-AKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRAD 1751
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLEaALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1752 fdnAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAE 1831
Cdd:COG1196 684 ---LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1988774676 1832 EASRLRAISEEAKhqRQI---------AEEEAARQRAEAERILKEK 1868
Cdd:COG1196 761 DLEELERELERLE--REIealgpvnllAIEEYEELEERYDFLSEQR 804
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1796-2629 |
3.21e-23 |
|
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: 109.68 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1796 ILIQLKtKAEKETMSNTEKSKQLLEAEA-AKMKDLAEEASR--LRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAI 1872
Cdd:pfam02463 137 FLVQGG-KIEIIAMMKPERRLEIEEEAAgSRLKRKKKEALKklIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1873 SEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKalEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIvddtlkqrrv 1952
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE--EIESSKQEIEKEEEKLAQVLKENKEEEKEKKL---------- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1953 VEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAAR 2032
Cdd:pfam02463 284 QEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2033 QRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAA--EQQVQSVLAQQIEDSITQKKLKEEYEKAKKL 2110
Cdd:pfam02463 364 LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLleLARQLEDLLKEEKKEELEILEEEEESIELKQ 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2111 AKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAK 2190
Cdd:pfam02463 444 GKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGR 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2191 HKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKvqmeeLLKLKNKIEE 2270
Cdd:pfam02463 524 IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLK-----LPLKSIAVLE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2271 ENQRLIKKDKDSTqKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEA 2350
Cdd:pfam02463 599 IDPILNLAQLDKA-TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2351 EMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERL--RLQVSQLSEAQARAEEEAKKFK 2428
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKinEELKLLKQKIDEEEEEEEKSRL 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2429 KQADKVATRLHETEiatQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHE 2508
Cdd:pfam02463 758 KKEEKEEEKSELSL---KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2509 KtvlqqtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKtLQATMDAALSKQKEAEEEML 2588
Cdd:pfam02463 835 L---------EELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKL-KDELESKEEKEKEEKKELEE 904
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1988774676 2589 RKQKEMQELERQRLEQERI--LAEENQKLREKLQQLEDAQKDQ 2629
Cdd:pfam02463 905 ESQKLNLLEEKENEIEERIkeEAEILLKYEEEPEELLLEEADE 947
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
69-171 |
3.71e-23 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 96.97 E-value: 3.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 69 VQKKTFTKWVNKHLIKAQRH--VTDLYEDLRDGHNLISLLEVLSGETLP-REKGRMRFHKLQNVQIALDFLRHRQ-VKLV 144
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*..
gi 1988774676 145 NIRNDDIADGNPKLTLGLIWTIILHFQ 171
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQ 108
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
189-293 |
4.85e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 96.78 E-value: 4.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 189 TAKEKLLLWSQRMTDGYqGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 268
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1988774676 269 EDVDVPHPDEKSIITYVSSLYDAMP 293
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1487-2383 |
2.28e-22 |
|
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: 106.98 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1487 IRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRqaEEELKRKSEAEKEAAKQKQKALE 1566
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQ--ELKLKEQAKKALEYYQLKEKLEL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1567 DLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKsaaAELQSKHMSFAEKTSKLEESLKQEhgavlQLQQEAERLKKQ 1646
Cdd:pfam02463 222 EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSK---QEIEKEEEKLAQVLKENKEEEKEK-----KLQEEELKLLAK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1647 QEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELER 1726
Cdd:pfam02463 294 EEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1727 QRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEK 1806
Cdd:pfam02463 374 ELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1807 ETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKhqRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIAL 1886
Cdd:pfam02463 454 EKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS--RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1887 KEKEAENERLRRQ---AEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVE-EEIRILKL 1962
Cdd:pfam02463 532 GDLGVAVENYKVAistAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPIlNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1963 NFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKiaAAEEEAARQRKAALEELE 2042
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSEL--TKELLEIQELQEKAESEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2043 RLRKKAEEARKQKDEADKEAEKQIVVAQQaAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAE 2122
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLE-AEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2123 REAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQK 2202
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2203 FQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQrgQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDS 2282
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELE--SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2283 TQKLLAEEAENMRKLAEDAArlSVEAQEAARLRQIAEDDLNQQrALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQE 2362
Cdd:pfam02463 927 AEILLKYEEEPEELLLEEAD--EKEKEENNKEEEEERNKRLLL-AKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
890 900
....*....|....*....|.
gi 1988774676 2363 QAQKLLEDKQLMQQRLEEETE 2383
Cdd:pfam02463 1004 KKKLIRAIIEETCQRLKEFLE 1024
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
68-176 |
1.70e-21 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 93.22 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 68 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 144
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100 110
....*....|....*....|....*....|..
gi 1988774676 145 NIRNDDIADGNPKLTLGLIWTIILHFQVSSSI 176
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSISMPV 127
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1254-1729 |
2.39e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 104.07 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1254 ADAKQRQEKIQAVPITDSKTLKE----QLAQEKKLLEEIE---QNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPL 1326
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEaaekKKEEAKKKADAAKkkaEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1327 VSPLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDD-EEKAAEKLKAEERKKMAE---MQAELDKQ 1402
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEaKKKAEEAKKADEAKKKAEeakKKADEAKK 1504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1403 KQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEE 1482
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1483 EIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSeetQKKRQAEEELKRKSEAEKEAAKQKQ 1562
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE---QLKKKEAEEKKKAEELKKAEEENKI 1661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1563 KAledlEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKsaaaelqskhmsfAEKTSKLEESLKQEHGAVlqlqQEAER 1642
Cdd:PTZ00121 1662 KA----AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-------------AEEAKKAEELKKKEAEEK----KKAEE 1720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1643 LKKQQEDAENSREEAEKELEKWRQKANEAlrlrlqAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEE 1722
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEA------KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
....*..
gi 1988774676 1723 ELERQRK 1729
Cdd:PTZ00121 1795 EVDKKIK 1801
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
68-173 |
2.51e-21 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 92.46 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 68 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 144
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1988774676 145 NIRNDDIADGNPKLTLGLIWTIILHFQVS 173
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1152-1912 |
2.68e-21 |
|
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: 103.21 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1152 VKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRE 1231
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1232 LEQLGRQLGYYRESYDWLIRWIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKD 1311
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1312 YELQLVAYKAQVEPLVSplKKTKLDSASDNIIQEYVTLRTRYSELMtltsqyikfITDTQRRLDDEEKAAEKLKAEErkk 1391
Cdd:TIGR02168 391 LELQIASLNNEIERLEA--RLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEELEELQEEL--- 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1392 mAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLK------MQEEVSKREIAAVDAEKQKTNIQLELQELKNL------- 1458
Cdd:TIGR02168 457 -ERLEEALEELREELEEAEQALDAAERELAQLQARldslerLQENLEGFSEGVKALLKNQSGLSGILGVLSELisvdegy 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1459 -------------------SEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLR 1519
Cdd:TIGR02168 536 eaaieaalggrlqavvvenLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1520 KLAQ------------DEAEKLRKQVSEE---------------------------TQKKRQAEEELKRKSEAEKEAAKQ 1560
Cdd:TIGR02168 616 KALSyllggvlvvddlDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEELEEKIAE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1561 KQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIkvaheaaqksaaaelqskhmsfaektSKLEESLKQEHGAVLQLQQEA 1640
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQI--------------------------SALRKDLARLEAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1641 ERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAhkktlaqeEAEKQKEEAEREAKKRAKAEESALKQK--- 1717
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI--------EQLKEELKALREALDELRAELTLLNEEaan 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1718 -----EMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRS 1792
Cdd:TIGR02168 822 lrerlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1793 EMDILIQLKTKAEKETMSNTEKSKQL-LEAEAAKMKdLAEEASRLRA----ISEEAKHQRQIAEEEAARQRAEAERiLKE 1867
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLeLRLEGLEVR-IDNLQERLSEeyslTLEEAEALENKIEDDEEEARRRLKR-LEN 979
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1988774676 1868 KLAAISEATRLkteaeiALKEKEAENER---LRRQAEDEAYQRKALED 1912
Cdd:TIGR02168 980 KIKELGPVNLA------AIEEYEELKERydfLTAQKEDLTEAKETLEE 1021
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
823-889 |
3.12e-21 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 90.01 E-value: 3.12e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774676 823 QLKPRNptTSIKGKLPIQAVCDFKQQEITVHKGDECALLNNSQPFKWKVLNRSGHEAMVPSVCFIVP 889
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2032-2628 |
4.48e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.32 E-value: 4.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2032 RQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSvLAQQIEDsitqkkLKEEYEKAKKLA 2111
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE-LELELEE------AQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2112 KEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKH 2191
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2192 KKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEE 2271
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2272 NQRLIKKDKDSTQKLLAEEAEnmrklaEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAE 2351
Cdd:COG1196 458 EEALLELLAELLEEAALLEAA------LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2352 MLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQA 2431
Cdd:COG1196 532 VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2432 DKVATRLHETEIATQEkmtVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTV 2511
Cdd:COG1196 612 DARYYVLGDTLLGRTL---VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2512 LQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLrkQ 2591
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL--E 766
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1988774676 2592 KEMQELERQR----------LEQERILAEENQKLREKLQQLEDAQKD 2628
Cdd:COG1196 767 RELERLEREIealgpvnllaIEEYEELEERYDFLSEQREDLEEARET 813
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
189-289 |
6.83e-21 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 90.48 E-value: 6.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 189 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 268
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1988774676 269 EDVDV--PHPDEKSIITYVSSLY 289
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1852-2574 |
7.32e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.94 E-value: 7.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1852 EEAA------RQRAEAERilkeKLAAISEatRLkTEAEIALKEKEAENERLRRQAEDeayQRKALEDQASQHKQEIEEKI 1925
Cdd:COG1196 162 EEAAgiskykERKEEAER----KLEATEE--NL-ERLEDILGELERQLEPLERQAEK---AERYRELKEELKELEAELLL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1926 VQLKKSsEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKl 2005
Cdd:COG1196 232 LKLREL-EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2006 aleeekrrreaeekvkkiaaaeeeaarQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQS 2085
Cdd:COG1196 310 ---------------------------RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2086 VLAQQIEDSITQKKLKEEyekakklakeaeaakekaereaaLLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEF 2165
Cdd:COG1196 363 AEEALLEAEAELAEAEEE-----------------------LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2166 EAAKRAQAEaaalmQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRg 2245
Cdd:COG1196 420 EEELEELEE-----ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL- 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2246 qveeelfkvkvqmEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRkLAEDAARLSVEAQEAARLRQIAEDDLNQQ 2325
Cdd:COG1196 494 -------------LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI-GVEAAYEAALEAALAAALQNIVVEDDEVA 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2326 RALAEKMLKEKM--QAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEA 2403
Cdd:COG1196 560 AAAIEYLKAAKAgrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2404 ERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARL 2483
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2484 KKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLiEDEKKRLESQFE----------EEVKKAKALKD 2553
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL-ERELERLEREIEalgpvnllaiEEYEELEERYD 798
|
730 740
....*....|....*....|.
gi 1988774676 2554 EQERQKQQMEQEKKTLQATMD 2574
Cdd:COG1196 799 FLSEQREDLEEARETLEEAIE 819
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
190-289 |
1.00e-20 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 89.93 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 190 AKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPE 269
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1988774676 270 D-VDVPHPDEKSIITYVSSLY 289
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
189-288 |
1.34e-20 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 89.46 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 189 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINmgkvYQQTNLENLE----QAFSVAEKdLGVTR 264
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVD----YESLDPLDIKennkKAFEAFAS-LGVPR 75
|
90 100
....*....|....*....|....*
gi 1988774676 265 LLDPED-VDVPHPDEKSIITYVSSL 288
Cdd:cd21255 76 LLEPADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
193-290 |
3.54e-20 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 88.56 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 193 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD-PEDV 271
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1988774676 272 DVPHPDEKSIITYVSSLYD 290
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1367-2383 |
6.49e-20 |
|
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: 98.71 E-value: 6.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1367 ITDTQRRLDDEEKAAEKLKAE---------------------------ERKKMAEMQAELDKQKQLAEAHAKAIAKAEKE 1419
Cdd:pfam01576 105 IQDLEEQLDEEEAARQKLQLEkvtteakikkleedillledqnsklskERKLLEERISEFTSNLAEEEEKAKSLSKLKNK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1420 AQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKnlseQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKY 1499
Cdd:pfam01576 185 HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ----EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1500 TAESELKQLRDRAAEAEK---LRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKlrmqAE 1576
Cdd:pfam01576 261 NALKKIRELEAQISELQEdleSERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKK----AL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1577 EAERQVKQAEIEKEKQikvaheaAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREE 1656
Cdd:pfam01576 337 EEETRSHEAQLQEMRQ-------KHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1657 AEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQrkiaestAQ 1736
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE-------TR 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1737 QKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtmsnTEKSK 1816
Cdd:pfam01576 483 QKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE----LEALT 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1817 QLLEAEAAKMKDLAEEASRLRA----ISEEAKHQRQIAEEEAARQRaEAERILKEKLAAISEATRLKTEAEIALKEKEAE 1892
Cdd:pfam01576 559 QQLEEKAAAYDKLEKTKNRLQQelddLLVDLDHQRQLVSNLEKKQK-KFDQMLAEEKAISARYAEERDRAEAEAREKETR 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1893 NERLRRQAEDEAYQRKALEDQASQHKQEIEEkIVQLKKS---SEAEMERQKAIVDDTLKQRRVVEEEiriLKLNFEKASS 1969
Cdd:pfam01576 638 ALSLARALEEALEAKEELERTNKQLRAEMED-LVSSKDDvgkNVHELERSKRALEQQVEEMKTQLEE---LEDELQATED 713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1970 GKLDLELELNKLKNIADETQQSkiRAEEEAEKLRKLAleeekrrreaeEKVKKIAAAEEEAARQRKAALE-------ELE 2042
Cdd:pfam01576 714 AKLRLEVNMQALKAQFERDLQA--RDEQGEEKRRQLV-----------KQVRELEAELEDERKQRAQAVAakkklelDLK 780
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2043 RLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEdsiTQKKLKeeyekakklakeaeaakekae 2122
Cdd:pfam01576 781 ELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKE---SEKKLK--------------------- 836
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2123 reaallrqqAEEAErqktaaeeeaanQAKAQED---AERLRKEAEFEaakraqaeaaalmqKQQADTEMAKHKKLAEQTL 2199
Cdd:pfam01576 837 ---------NLEAE------------LLQLQEDlaaSERARRQAQQE--------------RDELADEIASGASGKSALQ 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2200 KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKV---KVQMEELLK-LKNKIEEENQRL 2275
Cdd:pfam01576 882 DEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSesaRQQLERQNKeLKAKLQEMEGTV 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2276 IKKDKDSTQKLLAeeaenmrKLAEDAARLSVEAQE---AARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEM 2352
Cdd:pfam01576 962 KSKFKSSIAALEA-------KIAQLEEQLEQESRErqaANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQ 1034
|
1050 1060 1070
....*....|....*....|....*....|.
gi 1988774676 2353 LQKQKDLAQEQAQKLLEDKQLMQQRLEEETE 2383
Cdd:pfam01576 1035 LKRQLEEAEEEASRANAARRKLQRELDDATE 1065
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
70-170 |
2.29e-19 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 86.10 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 70 QKKTFTKWVNKHLIKA--QRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLRHRQVKLVN 145
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1988774676 146 IRNDDIADGNPKLTLGLIWTIILHF 170
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1377-1998 |
3.30e-19 |
|
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: 96.68 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1377 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVS------KREIAAVDAEKQKT--NI 1448
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrvKEKIGELEAEIASLerSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1449 QLELQELKNLSEQQIKDKSQqVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEK 1528
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAE-IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1529 LRKQVSEETQKKRQAEEELKRKSE-------------AEKEAAKQKQKALED-LEKLRMQAEEAERQVKQ--AEIEKEKQ 1592
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEelqrlseeladlnAAIAGIEAKINELEEeKEDKALEIKKQEWKLEQlaADLSKYEQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1593 IKVA------------HEAAQKSAAAELQSKHMSFAEKTSK-----LEESLKQEHGAVLQLQQEAERLKKQQEDAENSR- 1654
Cdd:TIGR02169 470 ELYDlkeeydrvekelSKLQRELAEAEAQARASEERVRGGRaveevLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRl 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1655 --------EEAEKELEKWRQ-KANEA--LRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKA-------------E 1710
Cdd:TIGR02169 550 nnvvveddAVAKEAIELLKRrKAGRAtfLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAfkyvfgdtlvvedI 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1711 ESALKQK------EMAEEELERQRKI------AESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 1778
Cdd:TIGR02169 630 EAARRLMgkyrmvTLEGELFEKSGAMtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQ 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1779 QRKQLEDELAKVRSEMDILIQLKTKAE---KETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAisEEAKHQRQIAEEEAA 1855
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKerlEELEEDLSSLEQEIENVKSELKELEARIEELEE--DLHKLEEALNDLEAR 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1856 RQRAEAERI------LKEKLAAISEATRlktEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLK 1929
Cdd:TIGR02169 788 LSHSRIPEIqaelskLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774676 1930 KsSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEE 1998
Cdd:TIGR02169 865 E-LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
192-288 |
6.37e-19 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 84.67 E-value: 6.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 192 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN----LENLEQAFSVAEKDLGVTRLLD 267
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1988774676 268 PEDVDVPHPDEKSIITYVSSL 288
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1379-2619 |
6.58e-19 |
|
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: 95.63 E-value: 6.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1379 KAAEKLKAEERKKMAEMQ-AELD-KQKQLAE----------AHAKAIAKAEKEAQELKLKMQ--EEVSKREIAAVDAEKQ 1444
Cdd:pfam01576 10 KEEELQKVKERQQKAESElKELEkKHQQLCEeknalqeqlqAETELCAEAEEMRARLAARKQelEEILHELESRLEEEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1445 KTNiqlELQELKNLSEQQIKDKSQQVDEALHSRTK--------------IEEEIRLIRIQLETTEKQKYTAESELKQLRD 1510
Cdd:pfam01576 90 RSQ---QLQNEKKKMQQHIQDLEEQLDEEEAARQKlqlekvtteakikkLEEDILLLEDQNSKLSKERKLLEERISEFTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1511 RAAEAEKLRKLAQDEAEKLRKQVSE------ETQKKRQAEEELKRKSEAEKEAAKqkqkalEDLEKLRMQAEEAERQVKQ 1584
Cdd:pfam01576 167 NLAEEEEKAKSLSKLKNKHEAMISDleerlkKEEKGRQELEKAKRKLEGESTDLQ------EQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1585 AEIE-KEKQIKVAHEAAQKSAAaelQSKHMSFAEKTSKLEESLKQEHGAvlqlQQEAERLKKQ-QEDAENSREEAEKELE 1662
Cdd:pfam01576 241 KEEElQAALARLEEETAQKNNA---LKKIRELEAQISELQEDLESERAA----RNKAEKQRRDlGEELEALKTELEDTLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1663 KwrQKANEALRLRLQAEDEAHKKTLAqeeaekqkeeaerEAKKRAKAEESALKQK-----EMAEEELERQRKIAESTAQQ 1737
Cdd:pfam01576 314 T--TAAQQELRSKREQEVTELKKALE-------------EETRSHEAQLQEMRQKhtqalEELTEQLEQAKRNKANLEKA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1738 KLTAEQELIRLRADF-------DNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMS 1810
Cdd:pfam01576 379 KQALESENAELQAELrtlqqakQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1811 NTEKSKQLLEAEAAKMKDLAEE-------ASRLRAISEE-AKHQRQIAEEEAARQRAEaerilkeklaaiseatRLKTEA 1882
Cdd:pfam01576 459 LSKDVSSLESQLQDTQELLQEEtrqklnlSTRLRQLEDErNSLQEQLEEEEEAKRNVE----------------RQLSTL 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1883 EIALKEkeaenerLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEA--EMERQKAIVDDTLKQRRVVEEEIRIL 1960
Cdd:pfam01576 523 QAQLSD-------MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAydKLEKTKNRLQQELDDLLVDLDHQRQL 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1961 KLNFEKASSgKLDLELElnKLKNIADETQQSKIRAEEEAEKLRKLALEEEKrrreaeekvkkiaaaeeeaarqrkaALEE 2040
Cdd:pfam01576 596 VSNLEKKQK-KFDQMLA--EEKAISARYAEERDRAEAEAREKETRALSLAR-------------------------ALEE 647
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2041 LERLRKKAEEARKQKdEADKEaekQIVVAQQAAQKCSAAEQQVQSVLAQQIEDsitqkklkeeyekakklakeaeaakek 2120
Cdd:pfam01576 648 ALEAKEELERTNKQL-RAEME---DLVSSKDDVGKNVHELERSKRALEQQVEE--------------------------- 696
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2121 aereaalLRQQAEEAERQKTAAeeeaanqakaqEDAeRLRKEAEFEAAKRAQAeaaalmQKQQADTEMAKHKKlaEQTLK 2200
Cdd:pfam01576 697 -------MKTQLEELEDELQAT-----------EDA-KLRLEVNMQALKAQFE------RDLQARDEQGEEKR--RQLVK 749
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2201 QKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELlklknkieeenQRLIKKDK 2280
Cdd:pfam01576 750 QVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL-----------QRELEEAR 818
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2281 DSTQKLLAEEAENMRKLAedaarlSVEAQeaarLRQIAEDDLNQQRAlaekmlkeKMQAIQEASRLKAEAEMLQKQKDLA 2360
Cdd:pfam01576 819 ASRDEILAQSKESEKKLK------NLEAE----LLQLQEDLAASERA--------RRQAQQERDELADEIASGASGKSAL 880
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2361 QEQAQKLleDKQLMQqrLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHE 2440
Cdd:pfam01576 881 QDEKRRL--EARIAQ--LEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQE 956
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2441 TEIATQEKmtvverleferlntskeaddLRKAIADLEnekARLKKEAEELQNKSKEMADAQQKKIEHEKTVlqqtfmteK 2520
Cdd:pfam01576 957 MEGTVKSK--------------------FKSSIAALE---AKIAQLEEQLEQESRERQAANKLVRRTEKKL--------K 1005
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2521 EMLLkkekliedekkrlesQFEEEVKKAKALKDEQERQKQQMEQEKKTLQatmdaalskqkEAEEEMLRKQKEMQELERQ 2600
Cdd:pfam01576 1006 EVLL---------------QVEDERRHADQYKDQAEKGNSRMKQLKRQLE-----------EAEEEASRANAARRKLQRE 1059
|
1290 1300
....*....|....*....|..
gi 1988774676 2601 ---RLEQERILAEENQKLREKL 2619
Cdd:pfam01576 1060 lddATESNESMNREVSTLKSKL 1081
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1368-2064 |
1.72e-18 |
|
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: 93.88 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1368 TDTQRRLDDEEKAAEK-LKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEvsKREIAAVDAEKQKT 1446
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKsLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQT--QQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1447 NIQLELQELknLSEQQIKDKSQQVDEALHSRTKIEEEIR-------LIRIQLETTEKQKYTAESELK-QLRDRAAEAEKL 1518
Cdd:TIGR00618 253 EEQLKKQQL--LKQLRARIEELRAQEAVLEETQERINRArkaaplaAHIKAVTQIEQQAQRIHTELQsKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1519 RKLAQDEAEKLRKQVSEETQkkRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHE 1598
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTL--HSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1599 AAQksAAAELQskhmsfaektsklEESLKQEHGAVLQLQQEAerlkkQQEDAENSREEAEKELEKWRQKANEALRLRLQA 1678
Cdd:TIGR00618 409 QAT--IDTRTS-------------AFRDLQGQLAHAKKQQEL-----QQRYAELCAAAITCTAQCEKLEKIHLQESAQSL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1679 EDEAHK-KTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRK-IAESTAQQKLTAEQELIRLRADFDNAE 1756
Cdd:TIGR00618 469 KEREQQlQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1757 QQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRL 1836
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1837 RAISEEAKHQRQIAEEEAARQRAE---AERILKEKLAAISEATRLKTEA-EIALKEKEAENERLRRQAEDEAYQRKALED 1912
Cdd:TIGR00618 629 DVRLHLQQCSQELALKLTALHALQltlTQERVREHALSIRVLPKELLASrQLALQKMQSEKEQLTYWKEMLAQCQTLLRE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1913 Q------ASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRvveEEIRILKLNFEKASSGKLDLELELNKLKNIAD 1986
Cdd:TIGR00618 709 LethieeYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR---TVLKARTEAHFNNNEEVTAALQTGAELSHLAA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1987 ETqQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQ--------RKAALEELERLRKKAEEARKQKDEA 2058
Cdd:TIGR00618 786 EI-QFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEqflsrleeKSATLGEITHQLLKYEECSKQLAQL 864
|
....*.
gi 1988774676 2059 DKEAEK 2064
Cdd:TIGR00618 865 TQEQAK 870
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1711-2624 |
2.24e-18 |
|
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: 93.59 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1711 ESALKQKEMAEEELERQRKIAESTAQQkltaeqeLIRLRADFDNAEQQRSLL----EDELYRLKNEVAAAQQQRKQLEDE 1786
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQ-------LERLRREREKAERYQALLkekrEYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1787 LAKVRSEMDILIQLKTKAEKETmsntEKSKQLLEAEAAKMKDLAEEasrlraisEEAKHQRQIAEEEAarQRAEAERILK 1866
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRL----EEIEQLLEELNKKIKDLGEE--------EQLRVKEKIGELEA--EIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1867 EKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHK-------QEIEEKIVQLKKSSEAEMERQ 1939
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKeeledlrAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1940 KAIvDDTLKQRRVVEEEIRILKLNFEKASSGKLDLElelNKLKNIADETQQSKIRAEEEAEKLRKLaleeekrrreaEEK 2019
Cdd:TIGR02169 392 EKL-EKLKREINELKRELDRLQEELQRLSEELADLN---AAIAGIEAKINELEEEKEDKALEIKKQ-----------EWK 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2020 VKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEAdkEAEKQIVvaqQAAQKCSAAEQQVQSVLAQQIEDSITQ-K 2098
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA--EAQARAS---EERVRGGRAVEEVLKASIQGVHGTVAQlG 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2099 KLKEEYEKAKKLAKEAeaakekaereaallRQQAEEAErqktaaeeeaanqakAQEDAERLrkeaefeaakraqaeaaal 2178
Cdd:TIGR02169 532 SVGERYATAIEVAAGN--------------RLNNVVVE---------------DDAVAKEA------------------- 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2179 mqkqqadTEMAKHKKLAEQTLkqkfqveqeLTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKV-- 2256
Cdd:TIGR02169 564 -------IELLKRRKAGRATF---------LPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVve 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2257 QMEELLKLKNKIeeenqRLIKKDKDSTQK--LLAEEAENMRKLAEDAARLSVEAQE-AARLR--QIAEDDLNQQRALAEK 2331
Cdd:TIGR02169 628 DIEAARRLMGKY-----RMVTLEGELFEKsgAMTGGSRAPRGGILFSRSEPAELQRlRERLEglKRELSSLQSELRRIEN 702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2332 MLKEKMQAIQEASR----LKAEAEMLQKQkdlaQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLR 2407
Cdd:TIGR02169 703 RLDELSQELSDASRkigeIEKEIEQLEQE----EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2408 LQVSQLseAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEA 2487
Cdd:TIGR02169 779 EALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2488 EELQNKSKEMaDAQQKKIEhektvlqqtfmtekemllKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKK 2567
Cdd:TIGR02169 857 ENLNGKKEEL-EEELEELE------------------AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774676 2568 tLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERIlAEENQKLREKLQQLED 2624
Cdd:TIGR02169 918 -RLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV-QAELQRVEEEIRALEP 972
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1135-1882 |
3.30e-18 |
|
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: 93.21 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1135 LKQYEDCLREVHTVPSDVKEVETYRAKLKKMRTEAEDE----QPVFDSLEEELKKAS-----AVSDKMVRVHSER---DV 1202
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRleeiEQLLEELNKKIKDLGeeeqlRVKEKIGELEAEIaslER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1203 ELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQLGRQLGYYRESYDWLIRWIADAKQRQEKIQAVPITDSKTLKEQLAQEK 1282
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1283 KLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSplKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQ 1362
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA--KINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1363 YIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQK------------------------QLAEAHAKAIAKAEK 1418
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRggraveevlkasiqgvhgtvaqlgSVGERYATAIEVAAG 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1419 EAQELKLKMQEEVSKREIAAVDAEKQK-------TNIQLELQELKNLSEQQIKD--------------------KSQQVD 1471
Cdd:TIGR02169 547 NRLNNVVVEDDAVAKEAIELLKRRKAGratflplNKMRDERRDLSILSEDGVIGfavdlvefdpkyepafkyvfGDTLVV 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1472 EALHSRTKIEEEIRLIRIQLETTEKQ----------------KYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSE 1535
Cdd:TIGR02169 627 EDIEAARRLMGKYRMVTLEGELFEKSgamtggsraprggilfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1536 ETQKKRQAEEELKRKSeaekeaaKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEkqikvAHEAAQKSAAAELQSKHmsf 1615
Cdd:TIGR02169 707 LSQELSDASRKIGEIE-------KEIEQLEQEEEKLKERLEELEEDLSSLEQEIE-----NVKSELKELEARIEELE--- 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1616 aEKTSKLEESL-----KQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELekwrqkaNEALRLRLQAEDEAHKKtlaqe 1690
Cdd:TIGR02169 772 -EDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL-------NRLTLEKEYLEKEIQEL----- 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1691 eAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAEstaqqkltAEQELIRLRADFDNAEQQRSLLEDELYRLK 1770
Cdd:TIGR02169 839 -QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD--------LESRLGDLKKERDELEAQLRELERKIEELE 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1771 NEVAAAQQQRKQLEDELAKVRSEMDILIQLKtKAEKETMSNT---EKSKQLLEAEAAKMKDLaeEASRLRAISEEAKHQR 1847
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIEDPK-GEDEEIPEEElslEDVQAELQRVEEEIRAL--EPVNMLAIQEYEEVLK 986
|
810 820 830
....*....|....*....|....*....|....*
gi 1988774676 1848 QIAEEEAARQRAEAERilKEKLAAISEATRLKTEA 1882
Cdd:TIGR02169 987 RLDELKEKRAKLEEER--KAILERIEEYEKKKREV 1019
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1576-2633 |
4.51e-18 |
|
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: 92.55 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1576 EEAERQVKQAEIEKEKQIKVAHEAAQKsaaaELQSKHMSFAEKTSKLEESLKQEHgavlQLQQEAERLKKQQEDAENSRE 1655
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELK----ELEKKHQQLCEEKNALQEQLQAET----ELCAEAEEMRARLAARKQELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1656 EAEKELEKwrqkanealrlRLQAEDEAHKKTLAQeeaekqkeeaereaKKRAKAEESALKQkEMAEEELERQR-KIAEST 1734
Cdd:pfam01576 75 EILHELES-----------RLEEEEERSQQLQNE--------------KKKMQQHIQDLEE-QLDEEEAARQKlQLEKVT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1735 AQQKLTAEQELIRLRADFDNAEQ-QRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILiQLKTKAEKETMSNTE 1813
Cdd:pfam01576 129 TEAKIKKLEEDILLLEDQNSKLSkERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDL-EERLKKEEKGRQELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1814 KSKQLLEAEAAkmkDLAEEASRLRAISEEAKHQRQIAEEE----------AARQRAEAERILKEKLAAISEATR------ 1877
Cdd:pfam01576 208 KAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEElqaalarleeETAQKNNALKKIRELEAQISELQEdleser 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1878 -LKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEkivqLKKSSEAEMERQKAIVDD-TLKQRRVVE- 1954
Cdd:pfam01576 285 aARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTE----LKKALEEETRSHEAQLQEmRQKHTQALEe 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1955 -----EEIRILKLNFEKAssgKLDLELELNKLKNIADETQQSKIRAEEEAEKLrklaleeekrrreaEEKVKKIAAAEEE 2029
Cdd:pfam01576 361 lteqlEQAKRNKANLEKA---KQALESENAELQAELRTLQQAKQDSEHKRKKL--------------EGQLQELQARLSE 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2030 AARQRKAALEELERLRKKAEEARKQKDEADKEAEKqivvaqqAAQKCSAAEQQVQSvlAQQIEDSITQKKLKeeyekakk 2109
Cdd:pfam01576 424 SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK-------LSKDVSSLESQLQD--TQELLQEETRQKLN-------- 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2110 lakEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfeAAKRAQAEAAALMQKQQADTEMA 2189
Cdd:pfam01576 487 ---LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAG--TLEALEEGKKRLQRELEALTQQL 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2190 KHKKLAEQTL-KQKFQVEQELTKVKLKLDET--------DKQK---SVLDEE---LQRLKDEVDDAVKQRGQVEEELFKV 2254
Cdd:pfam01576 562 EEKAAAYDKLeKTKNRLQQELDDLLVDLDHQrqlvsnleKKQKkfdQMLAEEkaiSARYAEERDRAEAEAREKETRALSL 641
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2255 KVQMEELLKLKNKIEEENQRL------IKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDdlnqqral 2328
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQLraemedLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATED-------- 713
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2329 AEKMLKEKMQAiqeasrLKAEAEM-LQKQKDLAQEQAQKLLedKQLMQQRLEEETEEYHKSLEVERKRQLEImaEAERLR 2407
Cdd:pfam01576 714 AKLRLEVNMQA------LKAQFERdLQARDEQGEEKRRQLV--KQVRELEAELEDERKQRAQAVAAKKKLEL--DLKELE 783
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2408 LQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKmtvverleferLNTSKEADdlrKAIADLENEKARLKkea 2487
Cdd:pfam01576 784 AQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEI-----------LAQSKESE---KKLKNLEAELLQLQ--- 846
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2488 EELQNKSKEMADAQQKKIEHEKTVLQQTfmTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKK 2567
Cdd:pfam01576 847 EDLAASERARRQAQQERDELADEIASGA--SGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTT 924
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774676 2568 TLQATMDAAlSKQKEAEEEMLRKQKE----MQELERQ-RLEQERILAeenqKLREKLQQLEDaQKDQHTRE 2633
Cdd:pfam01576 925 ELAAERSTS-QKSESARQQLERQNKElkakLQEMEGTvKSKFKSSIA----ALEAKIAQLEE-QLEQESRE 989
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1349-2279 |
4.70e-18 |
|
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: 92.80 E-value: 4.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1349 LRTRYSELMTLTS-----QYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL 1423
Cdd:TIGR00606 171 LKQKFDEIFSATRyikalETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1424 KLKMQE-EVSKREIAAVDAE-KQKTNIQLELQELKNLSEQQIKDKSQQVDEAL------HSRTKIEEEIRLIRIQLETTE 1495
Cdd:TIGR00606 251 KNRLKEiEHNLSKIMKLDNEiKALKSRKKQMEKDNSELELKMEKVFQGTDEQLndlyhnHQRTVREKERELVDCQRELEK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1496 KQKytaeselkqlrdraaeaeKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEdleklrmQA 1575
Cdd:TIGR00606 331 LNK------------------ERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFE-------RG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1576 EEAERQVKQA-EIEKEKQIKVAHEAAQKsaAAELQSKHMSFAEKTSKLEESLKqehGAVLQLQQEAERLKKQQEDAENSR 1654
Cdd:TIGR00606 386 PFSERQIKNFhTLVIERQEDEAKTAAQL--CADLQSKERLKQEQADEIRDEKK---GLGRTIELKKEILEKKQEELKFVI 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1655 EEAE------KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEmaeeelERQR 1728
Cdd:TIGR00606 461 KELQqlegssDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH------TTTR 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1729 KIAESTAQQKLTAEQ-----------ELIRLRADFDNAEQqrslLEDELYRLKNEVaaaqqqrKQLEDELAKVRSEMDIL 1797
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEqirkiksrhsdELTSLLGYFPNKKQ----LEDWLHSKSKEI-------NQTRDRLAKLNKELASL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1798 IQLKTKAEKETMSNTEKSKQLLEA--EAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEA 1875
Cdd:TIGR00606 604 EQNKNHINNELESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVC 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1876 TR-LKTEAEIALKEKEAENerLRRQAEDEayqRKALEDQASQHKQEIEEKIVqLKKSSEAEMERQKAIVDDTLKQRRVVE 1954
Cdd:TIGR00606 684 QRvFQTEAELQEFISDLQS--KLRLAPDK---LKSTESELKKKEKRRDEMLG-LAPGRQSIIDLKEKEIPELRNKLQKVN 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1955 EEIRILKLNFEKASS--GKLDLELELNK--------LKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVK--- 2021
Cdd:TIGR00606 758 RDIQRLKNDIEEQETllGTIMPEEESAKvcltdvtiMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKqhe 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2022 --KIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKK 2099
Cdd:TIGR00606 838 ldTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETF 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2100 LKEEYEKAKKLAKEAEAAKEKAEREAALLRqqaeeaERQKTAAEEEAANQAKAQEDAERlrkeaefeaakraqaeaaalm 2179
Cdd:TIGR00606 918 LEKDQQEKEELISSKETSNKKAQDKVNDIK------EKVKNIHGYMKDIENKIQDGKDD--------------------- 970
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2180 QKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEvdDAVKqrgQVEEELFKVKVQME 2259
Cdd:TIGR00606 971 YLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRE--NELK---EVEEELKQHLKEMG 1045
|
970 980
....*....|....*....|....
gi 1988774676 2260 ELLKLKNKIE----EENQRLIKKD 2279
Cdd:TIGR00606 1046 QMQVLQMKQEhqklEENIDLIKRN 1069
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1272-1843 |
5.01e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 92.43 E-value: 5.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1272 KTLKEQLAQEKKLLEEIEQNKDKVDECQKYakayIDTIKDYELQLVAYKAQVEPLVSPLKKTKLDSASDNIIQEYVTLRT 1351
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLRE----INEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1352 R-YSELMTLTSQYIKFITDTQRRLDDEEKAAEKLK--AEERKKMAEMQAELDKQKQLAEahaKAIAKAEKEAQELKLKMq 1428
Cdd:PRK03918 255 RkLEEKIRELEERIEELKKEIEELEEKVKELKELKekAEEYIKLSEFYEEYLDELREIE---KRLSRLEEEINGIEERI- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1429 EEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQL 1508
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1509 RDRAAEAEKLRKLAQDEAEKLRK----------QVSEETQKKRQAE--EELKRKSEAEKEAAKQKQKALEDLEKLRMQAE 1576
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKakgkcpvcgrELTEEHRKELLEEytAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1577 EAERQVKQAEIEKekQIKVAHEAAQKSAAAELQSKhmsfAEKTSKLEESLKQEHGAVLQLQQEAERLK----------KQ 1646
Cdd:PRK03918 491 KESELIKLKELAE--QLKELEEKLKKYNLEELEKK----AEEYEKLKEKLIKLKGEIKSLKKELEKLEelkkklaeleKK 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1647 QEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEeaeREAKKRAKAEESAlkqkEMAEEELER 1726
Cdd:PRK03918 565 LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELE---REEKELKKLEEEL----DKAFEELAE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1727 QRKIAEStaqqkltAEQELIRLRADFDNAEQQRslLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDiliqlKTKAEK 1806
Cdd:PRK03918 638 TEKRLEE-------LRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLE-----KLKEEL 703
|
570 580 590
....*....|....*....|....*....|....*..
gi 1988774676 1807 ETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEA 1843
Cdd:PRK03918 704 EEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
189-288 |
5.19e-18 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 82.21 E-value: 5.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 189 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 268
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1988774676 269 ED-VDVPHPDEKSIITYVSSL 288
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1482-2240 |
5.60e-18 |
|
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: 92.34 E-value: 5.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1482 EEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEaAKQK 1561
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ-TQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1562 QKALEDLEKLRMQAEEAERQVKQ--AEIEKEKQIKVAHEAAQKsaAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQ-Q 1638
Cdd:TIGR00618 242 HAYLTQKREAQEEQLKKQQLLKQlrARIEELRAQEAVLEETQE--RINRARKAAPLAAHIKAVTQIEQQAQRIHTELQsK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1639 EAERLKKQQEDAENSREEAekELEKWRQKANEALRLRLQAEDEAHKKTLaqeeaekqkeeaEREAKKRAKAEESALKQKE 1718
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQS--SIEEQRRLLQTLHSQEIHIRDAHEVATS------------IREISCQQHTLTQHIHTLQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1719 MAEEELERQRKIAeSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILI 1798
Cdd:TIGR00618 386 QQKTTLTQKLQSL-CKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1799 QLKTKAEKETMSNTEkskQLLEAEAAKMKdlaeeasrlraisEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEA-TR 1877
Cdd:TIGR00618 465 AQSLKEREQQLQTKE---QIHLQETRKKA-------------VVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPlTR 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1878 LKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEiEEKIVQLKKSSEAEMERQKAIVDDTLKQrrvVEEEI 1957
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITVRLQDL---TEKLS 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1958 RILKLNFEKASSGKLDLELELNKLKNIADETQQSKiraEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAA 2037
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQ---ELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLA 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2038 LEELERLRKKA---EEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIED-SITQKKLKEEYEKAKKLAKE 2113
Cdd:TIGR00618 682 LQKMQSEKEQLtywKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAlNQSLKELMHQARTVLKARTE 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2114 AEAAKEKAEREAALLRQQAEEAERQktaaeeEAANQAKAQEDAERLR-KEAEFEAAKRAQAEAAALMQKQQADTEMAKHK 2192
Cdd:TIGR00618 762 AHFNNNEEVTAALQTGAELSHLAAE------IQFFNRLREEDTHLLKtLEAEIGQEIPSDEDILNLQCETLVQEEEQFLS 835
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1988774676 2193 KLAEQTLKQkfqveQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDA 2240
Cdd:TIGR00618 836 RLEEKSATL-----GEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
189-287 |
7.09e-18 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 81.90 E-value: 7.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 189 TAKEKLLLWSQRMTDGYqgiRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLGVTRLLD 267
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENpLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1988774676 268 PEDVDVPHPDEKSIITYVSS 287
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
191-301 |
1.22e-17 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 81.58 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 191 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 270
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|..
gi 1988774676 271 -VDVPHPDEKSIITYVSSLYdampRTDVHDGM 301
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY----RCLVQKGL 110
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
185-290 |
1.24e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 81.53 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 185 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTR 264
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1988774676 265 LLDPEDV-DVPHPDEKSIITYVSSLYD 290
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2289-2626 |
1.72e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.77 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2289 EEAEnmRKLAEDAARLsveaqeaARLRQIAE------DDLNQQRALAEKMlkekmQAIQEASRLKaEAEMLQKQKDLAQE 2362
Cdd:COG1196 175 EEAE--RKLEATEENL-------ERLEDILGelerqlEPLERQAEKAERY-----RELKEELKEL-EAELLLLKLRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2363 QAQKLLEDKQLMQQRLEEETEEY---HKSLEVERKRQLEIMAEAERLRLQVSQLSEAQAraeeeakkfkkQADKVATRLH 2439
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELaelEAELEELRLELEELELELEEAQAEEYELLAELA-----------RLEQDIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2440 ETEIATQEKMtvvERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEmADAQQKKIEHEKTVLQQTFMTE 2519
Cdd:COG1196 309 ERRRELEERL---EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE-AEEALLEAEAELAEAEEELEEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2520 KEMLLKKEKLIEDEKKRLESQfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELER 2599
Cdd:COG1196 385 AEELLEALRAAAELAAQLEEL-EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340
....*....|....*....|....*..
gi 1988774676 2600 QRLEQERILAEENQKLREKLQQLEDAQ 2626
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAA 490
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
71-168 |
2.45e-17 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 80.08 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 71 KKTFTKWVNKHL-IKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLRHRQV-KLVNI 146
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1988774676 147 RNDDI-ADGNPKLTLGLIWTIIL 168
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
191-290 |
4.67e-17 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 79.62 E-value: 4.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 191 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 270
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1988774676 271 VDV--PHPDEKSIITYVSSLYD 290
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2292-2603 |
4.71e-17 |
|
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: 89.03 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2292 ENMRKLAEDAARLSVEAQEAARLRQIAED---DLNQQRALAEKMlKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLL 2368
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEkarEVERRRKLEEAE-KARQAEMDRQAAIYAEQERMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2369 EDKQLMQQRLEEETEEYHKSLEVERkRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEK 2448
Cdd:pfam17380 358 RKRELERIRQEEIAMEISRMRELER-LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2449 MtvvERLEFERlntSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKtvlQQTFMTEKEMLLKKEK 2528
Cdd:pfam17380 437 V---RRLEEER---AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE---QRRKILEKELEERKQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2529 LIEDEKKR--LESQFEEEVK----KAKALKDEQERQKQQMEQEKKTLQATMDAALSKQK-----EAEEEMLRKQKEmQEL 2597
Cdd:pfam17380 508 MIEEERKRklLEKEMEERQKaiyeEERRREAEEERRKQQEMEERRRIQEQMRKATEERSrleamEREREMMRQIVE-SEK 586
|
....*.
gi 1988774676 2598 ERQRLE 2603
Cdd:pfam17380 587 ARAEYE 592
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
191-297 |
7.82e-17 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 79.32 E-value: 7.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 191 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 270
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*....
gi 1988774676 271 VDV--PHPDEKSIITYVSSLYDAMPRTDV 297
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRRHEM 111
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1436-2252 |
9.63e-17 |
|
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: 88.59 E-value: 9.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1436 IAAVDAEKQKTNIQLELQElKNLSEQQ--IKDKSQQVDEALHSRTKIEE--EIRLIRIQLETTE--KQKYTAESELKQLR 1509
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVE-ENIERLDliIDEKRQQLERLRREREKAERyqALLKEKREYEGYEllKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1510 DRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALE-DLEKLRMQAEEAERQVKQAEiE 1588
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERSIAEKERELEDAE-E 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1589 KEKQIKVAHEAaQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKA 1668
Cdd:TIGR02169 323 RLAKLEAEIDK-LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1669 NEALRLRLQAEDEAHKKTlaqeeaekQKEEAEREAKKRAKAEESALK-QKEMAEEELERQRKIAESTAQQKLTAEQELIR 1747
Cdd:TIGR02169 402 NELKRELDRLQEELQRLS--------EELADLNAAIAGIEAKINELEeEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1748 LRADFDNAEQQRSLLEDELYRLKNEVAAAQQ-------QRKQLEDELAKVRSEMDILIQLKTKAEK-------------- 1806
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEErvrggraVEEVLKASIQGVHGTVAQLGSVGERYATaievaagnrlnnvv 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1807 -ETMSNTEKSKQLLEAEAA---------KMKDLAEEASRLRA----------ISEEAKHQRQIA----------EEEAAR 1856
Cdd:TIGR02169 554 vEDDAVAKEAIELLKRRKAgratflplnKMRDERRDLSILSEdgvigfavdlVEFDPKYEPAFKyvfgdtlvveDIEAAR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1857 QRAEAERI------LKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKK 1930
Cdd:TIGR02169 634 RLMGKYRMvtlegeLFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1931 SSEAEMERQKAIvDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKL-RKLALEE 2009
Cdd:TIGR02169 714 ASRKIGEIEKEI-EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2010 EKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQ 2089
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2090 qiedsiTQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQED-AERLRKEAEFEAA 2168
Cdd:TIGR02169 873 ------LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEElSEIEDPKGEDEEI 946
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2169 KRAQAEAAALMQKQQADTEmakhkklAEQTLKQ-KFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQV 2247
Cdd:TIGR02169 947 PEEELSLEDVQAELQRVEE-------EIRALEPvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
....*
gi 1988774676 2248 EEELF 2252
Cdd:TIGR02169 1020 FMEAF 1024
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1377-1843 |
1.48e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.40 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1377 EEKAAEKLKAEERKKMA--------EMQAELDKQKQLAEAHAKAIAKAEKEAQELKlkmqEEVSKREIAAVDAEKQKTNI 1448
Cdd:PRK02224 223 ERYEEQREQARETRDEAdevleeheERREELETLEAEIEDLRETIAETEREREELA----EEVRDLRERLEELEEERDDL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1449 QLELQelknLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEK 1528
Cdd:PRK02224 299 LAEAG----LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1529 LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAEL 1608
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKC 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1609 --------QSKHMSFAEKTSKLEESLKQEhgaVLQLQQEAERLKKQQEDAENSReEAEKELEKWRQKANEALRLRLQAED 1680
Cdd:PRK02224 455 pecgqpveGSPHVETIEEDRERVEELEAE---LEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRE 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1681 EAHKKTLAQEEAEKQKEEAEREAK-KRAKAEESALKQKEMAE-------------EELERQRKIAESTAQQKlTAEQELI 1746
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEeKREAAAEAEEEAEEAREevaelnsklaelkERIESLERIRTLLAAIA-DAEDEIE 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1747 RL---RADFDNAEQQR-----------SLLEDELYrlKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtMSNT 1812
Cdd:PRK02224 610 RLrekREALAELNDERrerlaekrerkRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAE-IGAV 686
|
490 500 510
....*....|....*....|....*....|.
gi 1988774676 1813 EKSKQLLEAEAAKMKDLAEEASRLRAISEEA 1843
Cdd:PRK02224 687 ENELEELEELRERREALENRVEALEALYDEA 717
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
191-292 |
1.81e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 78.20 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 191 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 270
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1988774676 271 -VDVPHPDEKSIITYVSSLYDAM 292
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1475-2099 |
4.76e-16 |
|
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: 86.05 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1475 HSRTKIEEEIRliriQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRqaeEELKRKSEAE 1554
Cdd:pfam12128 241 PEFTKLQQEFN----TLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKR---DELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1555 KEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAeLQSKHMSFAEKTSKLEESLKQEHGAVL 1634
Cdd:pfam12128 314 DAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LTGKHQDVTAKYNRRRSKIKEQNNRDI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1635 QLQQEaeRLKKQQEDAENSREEAEKELEK----WRQKANEALRlRLQAEDEAHKKTLAqeeaekqkeeaerEAKKR---A 1707
Cdd:pfam12128 393 AGIKD--KLAKIREARDRQLAVAEDDLQAleseLREQLEAGKL-EFNEEEYRLKSRLG-------------ELKLRlnqA 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1708 KAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQ-------- 1779
Cdd:pfam12128 457 TATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtl 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1780 ----RKQL---EDELAKVRSEmdiliQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEE 1852
Cdd:pfam12128 537 lhflRKEApdwEQSIGKVISP-----ELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEE 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1853 EAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSS 1932
Cdd:pfam12128 612 ALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQL 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1933 EAEMERQKAIVDDTLKQRRvveeEIRILKLNFEKASSGKLDLELELNKlkniadetqqSKIRAEEEAEKLRKLALEEEKR 2012
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKR----EARTEKQAYWQVVEGALDAQLALLK----------AAIAARRSGAKAELKALETWYK 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2013 RREAEEKVKKIaaAEEEAARQRKAALEELERLRKKAEEARKQKD--EADKEAEKQIVVAQQAAQKCSAAEQQVQsvLAQQ 2090
Cdd:pfam12128 758 RDLASLGVDPD--VIAKLKREIRTLERKIERIAVRRQEVLRYFDwyQETWLQRRPRLATQLSNIERAISELQQQ--LARL 833
|
....*....
gi 1988774676 2091 IEDSITQKK 2099
Cdd:pfam12128 834 IADTKLRRA 842
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1153-1967 |
5.48e-16 |
|
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: 85.79 E-value: 5.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1153 KEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQREL 1232
Cdd:pfam02463 265 EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1233 EQLGRQLGYYRESydwlirwIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDY 1312
Cdd:pfam02463 345 KELEIKREAEEEE-------EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1313 ELQLVAYKAQVEPLVSPLKKTKLdsasdnIIQEYVTLRTRYSELMTLTSqyikfitdtQRRLDDEEKAAEKLKAEERKKM 1392
Cdd:pfam02463 418 EDLLKEEKKEELEILEEEEESIE------LKQGKLTEEKEELEKQELKL---------LKDELELKKSEDLLKETQLVKL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1393 AEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVskREIAAVDAEKQKTNIQLELQELKNLSeqqikdkSQQVDE 1472
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG--GRIISAHGRLGDLGVAVENYKVAIST-------AVIVEV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1473 ALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAeAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSE 1552
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSI-AVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1553 AEKEAAKQKQKALEDLEKLRMQAE-EAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHG 1631
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKGVSLEEgLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1632 AVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKtlaqeeaekqkeeAEREAKKRAKAEE 1711
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEK-------------SELSLKEKELAEE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1712 SALKQKEMAEEELERQRKIAESTaqqkLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEvaaAQQQRKQLEDELAKVR 1791
Cdd:pfam02463 780 REKTEKLKVEEEKEEKLKAQEEE----LRALEEELKEEAELLEEEQLLIEQEEKIKEEELE---ELALELKEEQKLEKLA 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1792 SEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAA 1871
Cdd:pfam02463 853 EEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLK 932
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1872 ISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEdqASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRR 1951
Cdd:pfam02463 933 YEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL--GKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRA 1010
|
810
....*....|....*.
gi 1988774676 1952 VVEEEIRILKLNFEKA 1967
Cdd:pfam02463 1011 IIEETCQRLKEFLELF 1026
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
194-289 |
1.10e-15 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 75.86 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 194 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEkDLGVTRLLDPED-VD 272
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1988774676 273 VPHPDEKSIITYVSSLY 289
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1477-2388 |
1.11e-15 |
|
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: 84.73 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1477 RTKIEEEIRLIriqlETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKqvseETQKKRQAEEELKRKSEAE-K 1555
Cdd:TIGR02169 155 RRKIIDEIAGV----AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRR----EREKAERYQALLKEKREYEgY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1556 EAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKtskleeslkqehgavLQ 1635
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---------------LR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1636 LQQEAERLKKQQEDAENSREEAEKELEKW--RQKANEALRLRLQAEDEAHKKTLAqeeaekqkeeaeREAKKRAKAEESA 1713
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAeeRLAKLEAEIDKLLAEIEELEREIE------------EERKRRDKLTEEY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1714 LKQKEmaEEELERQRKIAESTAQQklTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSE 1793
Cdd:TIGR02169 360 AELKE--ELEDLRAELEEVDKEFA--ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1794 MDILIQLKTKAEKETMSNTEKSKQL---LEAEAAKMKDLAEEASRLRaiSEEAKHQRQIAEEEAARQRAE--------AE 1862
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQEWKLEQLaadLSKYEQELYDLKEEYDRVE--KELSKLQRELAEAEAQARASEervrggraVE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1863 RILKEKL----AAISEATRLKTEAEIALkEKEAENERLRRQAEDEAYQRKALEdQASQHK---------QEIEEKIVQLK 1929
Cdd:TIGR02169 514 EVLKASIqgvhGTVAQLGSVGERYATAI-EVAAGNRLNNVVVEDDAVAKEAIE-LLKRRKagratflplNKMRDERRDLS 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1930 KSSEA----------EMERQ-----KAIVDDTLkqrrVVE--EEIRILKLNFEKASsgkldLELEL-----------NKL 1981
Cdd:TIGR02169 592 ILSEDgvigfavdlvEFDPKyepafKYVFGDTL----VVEdiEAARRLMGKYRMVT-----LEGELfeksgamtggsRAP 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1982 KNIADETQQSKIRAEEEAEKLRKLaleeekrrreaeekvkkiaaaeeeaARQRKAALEELERLRKKAEEARkqkdEADKE 2061
Cdd:TIGR02169 663 RGGILFSRSEPAELQRLRERLEGL-------------------------KRELSSLQSELRRIENRLDELS----QELSD 713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2062 AEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDsitQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTA 2141
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEED---LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH 790
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2142 AEEEAANQAKAQEDAERLRKEAEFEaaKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDEtdk 2221
Cdd:TIGR02169 791 SRIPEIQAELSKLEEEVSRIEARLR--EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE--- 865
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2222 qksvLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKlLAEEAENMRKLAEDA 2301
Cdd:TIGR02169 866 ----LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEIEDPK 940
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2302 ARLSVEAQEAARLRQIAEDDLNQQRALaEKMLKEKMQAIQEAsrlkaeAEMLQKQKDLaQEQAQKLLEDKQLMQQRLEEE 2381
Cdd:TIGR02169 941 GEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEY------EEVLKRLDEL-KEKRAKLEEERKAILERIEEY 1012
|
....*..
gi 1988774676 2382 TEEYHKS 2388
Cdd:TIGR02169 1013 EKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2286-2628 |
1.26e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2286 LLAEEAENMRKLAEDAARlsveAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQ-EASRLKAEAEMLQKQkdlaQEQA 2364
Cdd:COG1196 194 ILGELERQLEPLERQAEK----AERYRELKEELKELEAELLLLKLRELEAELEELEaELEELEAELEELEAE----LAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2365 QKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIA 2444
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2445 TQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQqtfmtEKEMLL 2524
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-----RLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2525 KKEKLIEDEkkrlESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQ 2604
Cdd:COG1196 421 EELEELEEA----LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
330 340
....*....|....*....|....
gi 1988774676 2605 ERILAEENQKLREKLQQLEDAQKD 2628
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLR 520
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1373-2004 |
1.37e-15 |
|
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: 84.39 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1373 RLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSK------------------R 1434
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdlikennatrhlcnllK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1435 EIAAVDAEK----------------------------------QKTNIQLEL-----------QELKNLSEQQIKDKSQQ 1469
Cdd:pfam05483 162 ETCARSAEKtkkyeyereetrqvymdlnnniekmilafeelrvQAENARLEMhfklkedhekiQHLEEEYKKEINDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1470 VDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKR 1549
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1550 KSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSaAAELQSKHMSFAEKTSKLEESLKQE 1629
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN-EDQLKIITMELQKKSSELEEMTKFK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1630 HGAVLQLqQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKK-RAK 1708
Cdd:pfam05483 401 NNKEVEL-EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDlKTE 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1709 AEESALKQKEM---AEEELERQRKIAESTAQQKLtaeqELIRLRADFDNAEQQRSlledelyRLKNEVAAAQQQRKQLED 1785
Cdd:pfam05483 480 LEKEKLKNIELtahCDKLLLENKELTQEASDMTL----ELKKHQEDIINCKKQEE-------RMLKQIENLEEKEMNLRD 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1786 ELAKVRSEM-DILIQLKTKAEKETMSNTEKSKQLLEAEaAKMKDLAEEASRLRA-ISEEAKHQRQIAEE-EAARQRAEAE 1862
Cdd:pfam05483 549 ELESVREEFiQKGDEVKCKLDKSEENARSIEYEVLKKE-KQMKILENKCNNLKKqIENKNKNIEELHQEnKALKKKGSAE 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1863 -------RILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQA-EDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEA 1934
Cdd:pfam05483 628 nkqlnayEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKlLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVA 707
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1935 EMERQKAIVDDTLKQRrvvEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRK 2004
Cdd:pfam05483 708 LMEKHKHQYDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKM 774
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1362-1982 |
1.93e-15 |
|
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: 84.01 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1362 QYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKaIAKAEKEAQElklkmqeevskreiaavDA 1441
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMAD-IRRRESQSQE-----------------DL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1442 EKQKTNIQLELQELKNLSEQQIKDKSQQVDE---ALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRdraaeaekL 1518
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLKEDMLEDSNTQIEQlrkMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMH--------F 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1519 RKLAQDEAEKLRKQVSEETQKKRQ---AEEELkrksEAEKEAAKQKQKALedlekLRMQAEEAERQVKQAEIEKEKQIKV 1595
Cdd:pfam15921 216 RSLGSAISKILRELDTEISYLKGRifpVEDQL----EALKSESQNKIELL-----LQQHQDRIEQLISEHEVEITGLTEK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1596 AHEAaqKSAAAELQSKhMSFAEKTSKLEESLKQEH-----GAVLQLQQEAERLKKQQEDaenSREEAEKELEKWRQKANE 1670
Cdd:pfam15921 287 ASSA--RSQANSIQSQ-LEIIQEQARNQNSMYMRQlsdleSTVSQLRSELREAKRMYED---KIEELEKQLVLANSELTE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1671 ALRLRLQAE------DEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESA-----------LKQKEMAEEELERQRKIAES 1733
Cdd:pfam15921 361 ARTERDQFSqesgnlDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGnsitidhlrreLDDRNMEVQRLEALLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1734 TAQQKLtaEQELIRLRADFDNAEQQRSL---LEDELYRLKNEVAAAQQQRKQLEDELAKVrSEMDILIQLKTKAEKETMS 1810
Cdd:pfam15921 441 ECQGQM--ERQMAAIQGKNESLEKVSSLtaqLESTKEMLRKVVEELTAKKMTLESSERTV-SDLTASLQEKERAIEATNA 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1811 NTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQR-QIAEEEAARQ--RAEAERILkeKLAAISEATRLKTEAEIALK 1887
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVIEilRQQIENMT--QLVGQHGRTAGAMQVEKAQL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1888 EKEAENERLRRQaedeayQRKALEDQASQHKQEIEEKIVQLK----KSSEAEMERQKAIVDdtLKQRR------------ 1951
Cdd:pfam15921 596 EKEINDRRLELQ------EFKILKDKKDAKIRELEARVSDLElekvKLVNAGSERLRAVKD--IKQERdqllnevktsrn 667
|
650 660 670
....*....|....*....|....*....|....
gi 1988774676 1952 ---VVEEEIRILKLNFEKASSgklDLELELNKLK 1982
Cdd:pfam15921 668 elnSLSEDYEVLKRNFRNKSE---EMETTTNKLK 698
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
193-290 |
2.07e-15 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 74.92 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 193 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD-PEDV 271
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1988774676 272 DVPHPDEKSIITYVSSLYD 290
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1701-1958 |
3.05e-15 |
|
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: 82.86 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1701 REAKKRAKAEESALKQ-KEMAEEELERQRKIAES-TAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 1778
Cdd:pfam17380 288 QQQEKFEKMEQERLRQeKEEKAREVERRRKLEEAeKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1779 QRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKH-QRQIAEEEAARq 1857
Cdd:pfam17380 368 EEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQrEVRRLEEERAR- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1858 raEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQE-IEEKivQLKKSSEAEM 1936
Cdd:pfam17380 447 --EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAmIEEE--RKRKLLEKEM 522
|
250 260
....*....|....*....|...
gi 1988774676 1937 E-RQKAIVDDtlKQRRVVEEEIR 1958
Cdd:pfam17380 523 EeRQKAIYEE--ERRREAEEERR 543
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1452-1861 |
3.21e-15 |
|
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: 82.86 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1452 LQELKNLSEQQIKDKSQqvdealhsrtKIEEEirliRIQLETTEKQKytaesELKQlRDRAAEAEKLRKLAQDE-----A 1526
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE----------KMEQE----RLRQEKEEKAR-----EVER-RRKLEEAEKARQAEMDRqaaiyA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1527 EKLRKQVSEETQKKRQAEEELKRkseaEKEAAKQKQKALE-----DLEKLRMQAEEAERQVKQaEIEKEKQIKVAHEAAQ 1601
Cdd:pfam17380 338 EQERMAMERERELERIRQEERKR----ELERIRQEEIAMEisrmrELERLQMERQQKNERVRQ-ELEAARKVKILEEERQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1602 KSAaaelqSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENsreeaEKELEKWRQKANEALRLRLQAEde 1681
Cdd:pfam17380 413 RKI-----QQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQER-----QQQVERLRQQEEERKRKKLELE-- 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1682 ahkktlaqeeaekqkeeaeREAKKRAKAEEsaLKQKEMAEEELERQRKIAEStaqqkltaeqelirlradfdnaEQQRSL 1761
Cdd:pfam17380 481 -------------------KEKRDRKRAEE--QRRKILEKELEERKQAMIEE----------------------ERKRKL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1762 LEDELYRLKNEVAAAQQQRKQLEdelakvrsemdiliqlktkaEKETMSNTEKSKQLLEaeaaKMKDLAEEASRLRAISE 1841
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRREAEE--------------------ERRKQQEMEERRRIQE----QMRKATEERSRLEAMER 573
|
410 420
....*....|....*....|
gi 1988774676 1842 EAKHQRQIAEEEAARQRAEA 1861
Cdd:pfam17380 574 EREMMRQIVESEKARAEYEA 593
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
70-170 |
3.36e-15 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 74.26 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 70 QKKTFTKWVNKHLIK--AQRHVTDLYEDLRDGHNLISLLEVLSGETL------PREKGRMRfhklQNVQIALDFLRHRQV 141
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1988774676 142 KLVNIRNDDIADGNPKLTLGLIWTIILHF 170
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
67-166 |
3.42e-15 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 74.49 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 67 DRVQKKTFTKWVNKHLIKAQ-RHVTDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLRHR-QV 141
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
|
90 100
....*....|....*....|....*
gi 1988774676 142 KLVNIRNDDIADGNPKLTLGLIWTI 166
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1907-2630 |
4.62e-15 |
|
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: 82.71 E-value: 4.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1907 RKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKassgkLDLELELNKLKNIAD 1986
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQ-----LKEKLELEEEYLLYL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1987 ETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQI 2066
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2067 VVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAkekaereaaLLRQQAEEAERQKTAAEEEA 2146
Cdd:pfam02463 310 VDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEE---------LEKLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2147 ANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEqtlkqkfqveqeltkvKLKLDETDKQKSVL 2226
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELE----------------ILEEEEESIELKQG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2227 DEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRlIKKDKDSTQKLLAEEAENMRklaedaaRLSV 2306
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR-QKLEERSQKESKARSGLKVL-------LALI 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2307 EAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYH 2386
Cdd:pfam02463 517 KDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2387 KSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIAtQEKMTVVERLEFERLNTSKEA 2466
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSL-EEGLAEKSEVKASLSELTKEL 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2467 DDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVK 2546
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2547 KAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQErILAEENQKLREKLQQLEDAQ 2626
Cdd:pfam02463 756 RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA-ELLEEEQLLIEQEEKIKEEE 834
|
....
gi 1988774676 2627 KDQH 2630
Cdd:pfam02463 835 LEEL 838
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2330-2629 |
5.35e-15 |
|
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: 82.09 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2330 EKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEdkQLMQQRLEEETEEyhKSLEVERKRQLEimaEAERLR-- 2407
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFE--KMEQERLRQEKEE--KAREVERRRKLE---EAEKARqa 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2408 -------LQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQ-EKMTVVERLEFERLNTS----KEADDLRKAIAD 2475
Cdd:pfam17380 328 emdrqaaIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEiSRMRELERLQMERQQKNervrQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2476 LENEKARLKKEAEELQNKSKEMADAQQKKIEhektVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQ 2555
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVR----RLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK 483
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774676 2556 ERQKQQMEQEKKTLQATMDAalSKQKEAEEEMLRKQKEMQELERQRL---EQERILAEENqklREKLQQLEDAQKDQ 2629
Cdd:pfam17380 484 RDRKRAEEQRRKILEKELEE--RKQAMIEEERKRKLLEKEMEERQKAiyeEERRREAEEE---RRKQQEMEERRRIQ 555
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1003-1789 |
7.04e-15 |
|
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: 82.42 E-value: 7.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1003 EKGQQNETLC--KNYISELKDLRLRIEDCEAgtvarirkpveKEPLKEYIQKTTEQKKVQGELDGLKKDLDKVSVKTQEV 1080
Cdd:TIGR02169 195 EKRQQLERLRreREKAERYQALLKEKREYEG-----------YELLKEKEALERQKEAIERQLASLEEELEKLTEEISEL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1081 lasPQPSASAPVLRSELDLTVQKMDHAHMLSsvYLEKLKTVEMVIRNTQGAEGVLKQYEDCLREvhTVPSDVKEVETYRA 1160
Cdd:TIGR02169 264 ---EKRLEEIEQLLEELNKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1161 KLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQLGRQLG 1240
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1241 YYRESYDWLIRWIADAKQRQEKIQavpiTDSKTLKEQLAQEKKLLEEIEQNKDKVDEcQKYAK-----AYIDTIKDYELQ 1315
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELE----EEKEDKALEIKKQEWKLEQLAADLSKYEQ-ELYDLkeeydRVEKELSKLQRE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1316 LVAYKAQVEPLV--SPLKKTKLDSASDNIIQEYVTLRtrysELMTLTSQYIKFI-TDTQRRL-----DDEEKAAEKLK-A 1386
Cdd:TIGR02169 492 LAEAEAQARASEerVRGGRAVEEVLKASIQGVHGTVA----QLGSVGERYATAIeVAAGNRLnnvvvEDDAVAKEAIElL 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1387 EERK----------KMAEMQAELDKqkqLAEAHAKAIAK-----AEKEAQELKLKMQEEVSKREIAAvdAEKQKTNIQL- 1450
Cdd:TIGR02169 568 KRRKagratflplnKMRDERRDLSI---LSEDGVIGFAVdlvefDPKYEPAFKYVFGDTLVVEDIEA--ARRLMGKYRMv 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1451 ----ELQELK-------NLSEQQIKDKSQQVDEALHSRTKIEEeirlIRIQLETTEKQKYTAESELKQLRDRAAEAEKLR 1519
Cdd:TIGR02169 643 tlegELFEKSgamtggsRAPRGGILFSRSEPAELQRLRERLEG----LKRELSSLQSELRRIENRLDELSQELSDASRKI 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1520 KLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEaEKEAAKQKQKAL--------EDLEKLRMQAEEAER-------QVKQ 1584
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ-EIENVKSELKELearieeleEDLHKLEEALNDLEArlshsriPEIQ 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1585 AEIEKEKQIKVAHEAAQKSAAAELQSKHM--SFAEKTSKLEESLKQE---------------HGAVLQLQQEAERLKKQQ 1647
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLekEYLEKEIQELQEQRIDlkeqiksiekeienlNGKKEELEEELEELEAAL 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1648 EDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKtlaqeeaekQKEEAEREAKKRAKAEESALKQKEMAEEELERQ 1727
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK---------RKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 1728 RKIAESTAQQKLTAEQELIRLRADFDN-AEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAK 1789
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNMlAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1405-1867 |
8.18e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 81.35 E-value: 8.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1405 LAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLsEQQIKDKSQQVDEALHSRTKIEEEI 1484
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEEL-EEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1485 RLIRIQLETTEkqkytAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKA 1564
Cdd:COG4717 126 QLLPLYQELEA-----LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1565 LEDLEKLRMQAEEAERQVKQ------AEIEKEKQIKVAHEAAQK-----------SAAAELQSKHMSFAEKTSKLEESLK 1627
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEeleeleEELEQLENELEAAALEERlkearlllliaAALLALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1628 QEHG----AVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKAnEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREA 1703
Cdd:COG4717 281 LVLGllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELL-AALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1704 KKRAKAEESALKQKEM-----AEEELERQRKIAESTAQQKLTAEQELI--RLRADFDNAEQQ-----RSLLEDELYRLKN 1771
Cdd:COG4717 360 EEELQLEELEQEIAALlaeagVEDEEELRAALEQAEEYQELKEELEELeeQLEELLGELEELlealdEEELEEELEELEE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1772 EVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtmsntekskQLLEAEAAKMKDLAEEASRLRAISEE-AKHQRQIA 1850
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEEDGELAELL---------QELEELKAELRELAEEWAALKLALELlEEAREEYR 510
|
490
....*....|....*..
gi 1988774676 1851 EEEAARQRAEAERILKE 1867
Cdd:COG4717 511 EERLPPVLERASEYFSR 527
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1429-1912 |
8.24e-15 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 81.60 E-value: 8.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1429 EEVSKREIAAVDAEKQKTNIQlELQELKNLSEQQIKDKSQQVDEALHSRTkIEEEIRLIRIqletteKQKYTAESELKQL 1508
Cdd:NF033838 38 EEVRGGNNPTVTSSGNESQKE-HAKEVESHLEKILSEIQKSLDKRKHTQN-VALNKKLSDI------KTEYLYELNVLKE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1509 RDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEeelKRKSEAEKEAAKQKQKALEDL-----EKLRMQAEEAERQVK 1583
Cdd:NF033838 110 KSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEAT---KKVEEAEKKAKDQKEEDRRNYptntyKTLELEIAESDVEVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1584 QAEIEKEKQikvaheaaqksaaaelqskhmsfAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEK 1663
Cdd:NF033838 187 KAELELVKE-----------------------EAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1664 WRQKANEALrlrlqaEDEAHKKTLAQEEAEKQKEEAEREAKKR--AKAEESALKQKEMAEEELERQRKIAEstAQQKLTA 1741
Cdd:NF033838 244 KLKEAVEKN------VATSEQDKPKRRAKRGVLGEPATPDKKEndAKSSDSSVGEETLPSPSLKPEKKVAE--AEKKVEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1742 EQElirlRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELakvrsemdiliqlkTKAEKETMSNTEKSKQLLEA 1821
Cdd:NF033838 316 AKK----KAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELEL--------------VKEEAKEPRNEEKIKQAKAK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1822 EAAKMKdlaeEASRLraisEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAEN---ERLRR 1898
Cdd:NF033838 378 VESKKA----EATRL----EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQpkaEKPAD 449
|
490
....*....|....
gi 1988774676 1899 QAEDEAYQRKALED 1912
Cdd:NF033838 450 QQAEEDYARRSEEE 463
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1559-1911 |
1.07e-14 |
|
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: 81.32 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1559 KQKQKALEDLEKLRMQAE------EAERQVKQAEIEKEKQIKVAHEAAqksaaaeLQSKHMSFAEKTSKLEESLKQEhga 1632
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEkeekarEVERRRKLEEAEKARQAEMDRQAA-------IYAEQERMAMERERELERIRQE--- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1633 vlQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAedeAHKKTLAQEEAEKQKEEAEREAKKRAKAEES 1712
Cdd:pfam17380 357 --ERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEA---ARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1713 AlKQKEMAEEELERQRKIaESTAQQKLTAEQELIRLRADfdnaeqqrslledelyrlknevaAAQQQRKQLEDElakvrs 1792
Cdd:pfam17380 432 A-RQREVRRLEEERAREM-ERVRLEEQERQQQVERLRQQ-----------------------EEERKRKKLELE------ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1793 emdiliqlktKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIA-EEEAARQRAEAER---ILKEK 1868
Cdd:pfam17380 481 ----------KEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAiYEEERRREAEEERrkqQEMEE 550
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1988774676 1869 LAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAyQRKALE 1911
Cdd:pfam17380 551 RRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2362-2633 |
1.20e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2362 EQAQKLLEDkqlMQQRLE------EETEEYHKSLEVERKRQL---EIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQAD 2432
Cdd:COG1196 175 EEAERKLEA---TEENLErledilGELERQLEPLERQAEKAEryrELKEELKELEAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2433 KVATRLHETEIATQEKMTVVERLEFERLNTSKEA--DDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKT 2510
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEaqAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2511 VLQQTfmTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRK 2590
Cdd:COG1196 332 LEELE--EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1988774676 2591 QKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRE 2633
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4063-4101 |
1.59e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.05 E-value: 1.59e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1988774676 4063 LLEAQIATGGIIDPEESHRLPVEVAYNRGFFDEEMNEIL 4101
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1139-1960 |
1.60e-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: 81.27 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1139 EDCLREVHTVPSDVKEVETY----RAKLKKMRTEAEDEQPvFDSLEEELkkasavsdkmvrvhseRDVELDHFRQQLSSL 1214
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIidekRQQLERLRREREKAER-YQALLKEK----------------REYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1215 QDRWKAVFTQIDLRQRELEQLGRQLGYYRESYDWLIRWIADAKQRQEKiqavpitdsKTLKEQLAQEKKLLE---EIEQN 1291
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD---------LGEEEQLRVKEKIGEleaEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1292 KDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKKTKLDSASdnIIQEYVTLRTRYSELmtltsqyikfitdtQ 1371
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK--LTEEYAELKEELEDL--------------R 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1372 RRLDDEEKAAeklkAEERKKMAEMQAELDKqkqlaeahakaiakaekeaqelkLKMQEEVSKREIAAVDAEKQKTNIQLE 1451
Cdd:TIGR02169 371 AELEEVDKEF----AETRDELKDYREKLEK-----------------------LKREINELKRELDRLQEELQRLSEELA 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1452 lqELKNlseqQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKL-- 1529
Cdd:TIGR02169 424 --DLNA----AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAea 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1530 RKQVSEETQKKRQAEEELKRKS--------EAEKEAAKQKQKALEDLEKLRMQA---EEAERQVKQAEIEKEKQI----- 1593
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASiqgvhgtvAQLGSVGERYATAIEVAAGNRLNNvvvEDDAVAKEAIELLKRRKAgratf 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1594 ----KVAHEAAQKSAAA-----------------------------------ELQSKHMSFAEKTSkLEESLKQEHGAV- 1633
Cdd:TIGR02169 578 lplnKMRDERRDLSILSedgvigfavdlvefdpkyepafkyvfgdtlvvediEAARRLMGKYRMVT-LEGELFEKSGAMt 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1634 -------------LQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRlqaeDEAHKKTlaqeeaekqkeeae 1700
Cdd:TIGR02169 657 ggsraprggilfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL----SDASRKI-------------- 718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1701 REAKKRAkaeESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQR 1780
Cdd:TIGR02169 719 GEIEKEI---EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPE 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1781 KQLE-DELAKVRSEMD-ILIQLKTKAEKETMSNT--EKSKQLLEAEAAKMKDlaEEASRLRAISEEAKHQRQIAEEEAAR 1856
Cdd:TIGR02169 796 IQAElSKLEEEVSRIEaRLREIEQKLNRLTLEKEylEKEIQELQEQRIDLKE--QIKSIEKEIENLNGKKEELEEELEEL 873
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1857 QRAEAERI--LKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASqhkqEIEEKIVQLKKSSEA 1934
Cdd:TIGR02169 874 EAALRDLEsrLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEE 949
|
890 900
....*....|....*....|....*.
gi 1988774676 1935 EMerqkaIVDDTLKQRRVVEEEIRIL 1960
Cdd:TIGR02169 950 EL-----SLEDVQAELQRVEEEIRAL 970
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1248-1924 |
2.16e-14 |
|
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: 80.54 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1248 WLIRWIADAKQRQEKIQ---AVPITDSKTLKE-QLAQEK---KLLEEIEQNKDKVDE----------CQKYAKAYIDTIK 1310
Cdd:pfam05483 93 WKVSIEAELKQKENKLQenrKIIEAQRKAIQElQFENEKvslKLEEEIQENKDLIKEnnatrhlcnlLKETCARSAEKTK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1311 DYELQ-------LVAYKAQVEPLVSPLKKTKLdSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRL--------- 1374
Cdd:pfam05483 173 KYEYEreetrqvYMDLNNNIEKMILAFEELRV-QAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVsllliqite 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1375 -DDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQ 1453
Cdd:pfam05483 252 kENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1454 ELKNLSEQQIKDKSQQ---VDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLR 1530
Cdd:pfam05483 332 EKEAQMEELNKAKAAHsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1531 KQVSEETQ---KKRQAE---EELKRKSEAEKEAAKQKQKALEDLEkLRMQAEEAERQVKQAEIEKEKqikvaheaaqksa 1604
Cdd:pfam05483 412 KILAEDEKlldEKKQFEkiaEELKGKEQELIFLLQAREKEIHDLE-IQLTAIKTSEEHYLKEVEDLK------------- 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1605 aAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRlqAEDEAHK 1684
Cdd:pfam05483 478 -TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR--DELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1685 KTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMA--EEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLL 1762
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1763 EDELYRLKNEVAAAQQQRKQLEDELAKVrsemdilIQLKTKAEKETMSNTEKSKQLLEaEAAKM-----KDLAEEASRLR 1837
Cdd:pfam05483 635 EIKVNKLELELASAKQKFEEIIDNYQKE-------IEDKKISEEKLLEEVEKAKAIAD-EAVKLqkeidKRCQHKIAEMV 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1838 AISEEAKHQRQIAEEEaarqRAEAERILKEKLaaiSEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQH 1917
Cdd:pfam05483 707 ALMEKHKHQYDKIIEE----RDSELGLYKNKE---QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKEN 779
|
....*..
gi 1988774676 1918 KQEIEEK 1924
Cdd:pfam05483 780 TAILKDK 786
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
189-286 |
2.64e-14 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 71.64 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 189 TAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLGVTRLLD 267
Cdd:cd21230 1 TPKQRLLGWIQ---NKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1988774676 268 PEDVDVPHPDEKSIITYVS 286
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2287-2599 |
2.81e-14 |
|
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: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2287 LAEEAENmrklAEDAARLSVEAQEA-ARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQ 2365
Cdd:COG1196 205 LERQAEK----AERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2366 KLLEDKQLMQQRLEEETEEYHKSLEVERKR-------QLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRL 2438
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERrreleerLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2439 HETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMT 2518
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2519 EKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELE 2598
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
.
gi 1988774676 2599 R 2599
Cdd:COG1196 521 G 521
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1923-2606 |
3.92e-14 |
|
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: 79.38 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1923 EKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASsgkLDLELELNKLKNIADETQQSKIRAEEEAEKL 2002
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVS---LKLEEEIQENKDLIKENNATRHLCNLLKETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2003 RKLAlEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELerlRKKAEEARKQKDEADKEAEKQIVVAQQAAQK-CSAAEQ 2081
Cdd:pfam05483 165 ARSA-EKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL---RVQAENARLEMHFKLKEDHEKIQHLEEEYKKeINDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2082 QVQSVLAQQIEDSITQKKLkeeyekakklakeaeaakekaereAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRK 2161
Cdd:pfam05483 241 QVSLLLIQITEKENKMKDL------------------------TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2162 EaeFEAAKRAQAEAAALMQKQQADTEMAKhKKLAEQTLKQKFQVEqELTKVK----LKLDETDKQKSVLDEELQRLKDEV 2237
Cdd:pfam05483 297 E--LEDIKMSLQRSMSTQKALEEDLQIAT-KTICQLTEEKEAQME-ELNKAKaahsFVVTEFEATTCSLEELLRTEQQRL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2238 DDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLiKKDKDSTQKLLaEEAENMRKLAEDaarLSVEAQEAARLRQI 2317
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEEL-KKILAEDEKLL-DEKKQFEKIAEE---LKGKEQELIFLLQA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2318 AEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQ-KQKDLAQEQAQKLLEDKQLMQQR--LEEETEEYHKSLEVERK 2394
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTAHCDKLLLENKELTQEAsdMTLELKKHQEDIINCKK 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2395 RQLEIMAEAERLRLQVSQLseaQARAEEEAKKFKKQADKVATRLHETE-------IATQEKMTVVERLEFERLNTSKEAD 2467
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNL---RDELESVREEFIQKGDEVKCKLDKSEenarsieYEVLKKEKQMKILENKCNNLKKQIE 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2468 DLRKAIADLENEKARLKKEAEElQNKSKEMADAQQKKIEHEKTVLQQTFmteKEMLLKKEKLIEDeKKRLESQFEEEVKK 2547
Cdd:pfam05483 605 NKNKNIEELHQENKALKKKGSA-ENKQLNAYEIKVNKLELELASAKQKF---EEIIDNYQKEIED-KKISEEKLLEEVEK 679
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774676 2548 AKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRlEQER 2606
Cdd:pfam05483 680 AKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNK-EQEQ 737
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
189-289 |
4.78e-14 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 71.64 E-value: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 189 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 268
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1988774676 269 ED-VDVPHPDEKSIITYVSSLY 289
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
648-837 |
5.85e-14 |
|
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: 74.02 E-value: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 648 LHAFVSAATKELMWLNDKEEEEVNFDWSDRNTNMTAKKDNYSGLMRELELREKKVNDIQALGDRLVRDGHPGKKTVESFT 727
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 728 AALQTQWSWILQLCCCIEAHLKENTAYYQFFADVKEAQDKMKKMQENMKkkySCDRSTTATRLEDLLQDAAEEKEQLNEF 807
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|
gi 1988774676 808 KTVVAGLNKRSRSIIQLKPRNPTTSIKGKL 837
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1348-1992 |
5.94e-14 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 79.03 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1348 TLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDkqkqlaeahakAIAKAEKEAQELKLKM 1427
Cdd:pfam07111 52 SLELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELD-----------ALAVAEKAGQAEAEGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1428 QEEVSKREIAAVDAEKQKtniQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTekqkytaeselkq 1507
Cdd:pfam07111 121 RAALAGAEMVRKNLEEGS---QRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETK------------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1508 lrdRAAEAEKLrKLAQDEAEKLRKQVSeETQKKRQAEEELkrkseaekeaakqkqkaLEDLEKLRMQAEEAERQVKQAEI 1587
Cdd:pfam07111 185 ---RAGEAKQL-AEAQKEAELLRKQLS-KTQEELEAQVTL-----------------VESLRKYVGEQVPPEVHSQTWEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1588 EKEKQIKVAHEAaqKSAAAELQSkhmsfaekTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSR--EEAEKELEKWR 1665
Cdd:pfam07111 243 ERQELLDTMQHL--QEDRADLQA--------TVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEfpKKCRSLLNRWR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1666 QKANeALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERqrkIAESTAQQKLTAEQEL 1745
Cdd:pfam07111 313 EKVF-ALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVER---MSAKGLQMELSRAQEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1746 -IRLRADFDNAEQQRSL-----------LEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAE--KETMSN 1811
Cdd:pfam07111 389 rRRQQQQTASAEEQLKFvvnamsstqiwLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQlrQESCPP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1812 TEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQiAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEA 1891
Cdd:pfam07111 469 PPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQ-QEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1892 ENERLRRQ--AEDEAYQRKALEDQASQHKQEIEEKIVQL------------KKSSEAEMERQKAIVDDTLKQRRVVEE-- 1955
Cdd:pfam07111 548 EVARQGQQesTEEAASLRQELTQQQEIYGQALQEKVAEVetrlreqlsdtkRRLNEARREQAKAVVSLRQIQHRATQEke 627
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1988774676 1956 ---EIRILKLNFEKASSGKLDLEL-ELNKLKNIADETQQSK 1992
Cdd:pfam07111 628 rnqELRRLQDEARKEEGQRLARRVqELERDKNLMLATLQQE 668
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1302-1928 |
6.05e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.19 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1302 AKAYIDTIKDYELQLVAYKAQVEPLvSPLKKTKldsasdniiQEYVTLRTRYSELMTLtsqyikfitDTQRRLDDEEKAA 1381
Cdd:COG4913 230 LVEHFDDLERAHEALEDAREQIELL-EPIRELA---------ERYAAARERLAELEYL---------RAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1382 EKLKAEERkkmaEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQE------EVSKREIAavDAEKQKTNIQLELQEL 1455
Cdd:COG4913 291 ELLEAELE----ELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrlEQLEREIE--RLERELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1456 KNL----------SEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQkytAESELKQLRDRAAEAEKLRKLAQDE 1525
Cdd:COG4913 365 EALlaalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIASLERRKSNIPAR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1526 AEKLRKQVSEETQKKrqaEEELK--------RKSEAEKEAA----------------KQKQKALEDLE----KLRMQAEE 1577
Cdd:COG4913 442 LLALRDALAEALGLD---EAELPfvgelievRPEEERWRGAiervlggfaltllvppEHYAAALRWVNrlhlRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1578 AERQVKQAEIEKEK------QIKVAHEAAQKSAAAELQsKHMSFAEKTSklEESLKQEHGAVL---QLQQEAERLKKQQE 1648
Cdd:COG4913 519 VRTGLPDPERPRLDpdslagKLDFKPHPFRAWLEAELG-RRFDYVCVDS--PEELRRHPRAITragQVKGNGTRHEKDDR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1649 DAENSR----EEAEKELEKWRQKANEalrlrLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEEL 1724
Cdd:COG4913 596 RRIRSRyvlgFDNRAKLAALEAELAE-----LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1725 ERqrkiaestaqqkltAEQELIRLRADFDNAEQqrslLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKA 1804
Cdd:COG4913 671 AE--------------LEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1805 EKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKE--------------KLA 1870
Cdd:COG4913 733 QDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldaDLE 812
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774676 1871 AISE-ATRLKTEAEIALKEKEAENERLRRQAEDEayQRKALEDQASQHKQEIEEKIVQL 1928
Cdd:COG4913 813 SLPEyLALLDRLEEDGLPEYEERFKELLNENSIE--FVADLLSKLRRAIREIKERIDPL 869
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3749-3787 |
8.09e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 68.12 E-value: 8.09e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1988774676 3749 LLEAQAATGFIVDPLKNETLTVDEAVRKGVVGPEIHDKL 3787
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3416-3454 |
1.30e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 67.35 E-value: 1.30e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1988774676 3416 LLEAQAASGFIVDPVRNQCLSVDEAVKSGVVGPELHEKL 3454
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1451-1930 |
1.61e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.65 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1451 ELQELKNLsEQQIKDKSQQVD-----EALHSR-TKIEEEIRLIRIQLETTekQKYTAESELKQLRDRAAEAEKLRKLAQD 1524
Cdd:COG4913 233 HFDDLERA-HEALEDAREQIEllepiRELAERyAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1525 EAEKLRKQVSEETQKKRQAEEEL-----KRKSEAEKEAAkQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEA 1599
Cdd:COG4913 310 ELERLEARLDALREELDELEAQIrgnggDRLEQLEREIE-RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1600 AQkSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQ----EDAENSREEAEKEL-------------- 1661
Cdd:COG4913 389 AA-ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEALgldeaelpfvgeli 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1662 ------EKWRQKANEAL---RLRLQAEDEAHKK-------TLAQEEAEKQKEEAEREAKKRAKAEESALKQK-------- 1717
Cdd:COG4913 468 evrpeeERWRGAIERVLggfALTLLVPPEHYAAalrwvnrLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKldfkphpf 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1718 -EMAEEELERQRKIA--ESTAQQK-----LTAE------------QELIRLRAD----FDNAEQqRSLLEDELYRLKNEV 1773
Cdd:COG4913 548 rAWLEAELGRRFDYVcvDSPEELRrhpraITRAgqvkgngtrhekDDRRRIRSRyvlgFDNRAK-LAALEAELAELEEEL 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1774 AAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKE--------TMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKH 1845
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEidvasaerEIAELEAELERLDASSDDLAALEEQLEELEAELEELEE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1846 QRQIAEEEAARQRAEAERI------LKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAY-QRKALEDQASQHK 1918
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAeeeldeLQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEeRIDALRARLNRAE 786
|
570
....*....|..
gi 1988774676 1919 QEIEEKIVQLKK 1930
Cdd:COG4913 787 EELERAMRAFNR 798
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2370-2629 |
1.88e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.28 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2370 DKQLmqQRLEEE---TEEYHKSLEVERKRQLEIMA-EAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIAT 2445
Cdd:COG1196 199 ERQL--EPLERQaekAERYRELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2446 QEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLK 2525
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2526 KEKLIEDEKKRLESqfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQE 2605
Cdd:COG1196 357 EAELAEAEEALLEA--EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260
....*....|....*....|....
gi 1988774676 2606 RILAEENQKLREKLQQLEDAQKDQ 2629
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEE 458
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
189-289 |
2.47e-13 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 69.29 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 189 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 268
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1988774676 269 ED-VDVPHPDEKSIITYVSSLY 289
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
63-169 |
2.68e-13 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 69.23 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 63 ADERDrvqKKTFTKWVNKHLIKAQRHvtDLYEDLRDGhnlISLLEVL--------SGETLPREKGRMRFHKLQNVQIALD 134
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDPLIN--NLYEDLRDG---LVLLQVLdkiqpgcvNWKKVNKPKPLNKFKKVENCNYAVD 72
|
90 100 110
....*....|....*....|....*....|....*
gi 1988774676 135 FLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 169
Cdd:cd21219 73 LAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1702-1934 |
3.50e-13 |
|
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: 74.80 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1702 EAKKRAKAEESALKQK-EMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQR 1780
Cdd:COG4942 20 DAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1781 KQLEDELAKVRSEMdiliqlktkaekETMSNTEKSKQLLEAEaakmkDLAEEASRLRAISEEAKHQRQIAEE------EA 1854
Cdd:COG4942 100 EAQKEELAELLRAL------------YRLGRQPPLALLLSPE-----DFLDAVRRLQYLKYLAPARREQAEElradlaEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1855 ARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEA 1934
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1421-1980 |
3.83e-13 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 75.84 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1421 QELKlKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQ-QIKDKSQQVDEAlHSRTKIE-EEIRLIRIQLETTEKQK 1498
Cdd:pfam05701 42 LELE-KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEElKLNLERAQTEEA-QAKQDSElAKLRVEEMEQGIADEAS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1499 YTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQ----VSEETQKKRQAEEELKrkseaekeAAKQKQKALEDLEKLRMQ 1574
Cdd:pfam05701 120 VAAKAQLEVAKARHAAAVAELKSVKEELESLRKEyaslVSERDIAIKRAEEAVS--------ASKEIEKTVEELTIELIA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1575 AEEAERQVKQAEIEKEKqikvaheaaQKSAAAelqskhMSFAEKTSKLEESLKqehgavlQLQQEAERLKKQQedaeNSR 1654
Cdd:pfam05701 192 TKESLESAHAAHLEAEE---------HRIGAA------LAREQDKLNWEKELK-------QAEEELQRLNQQL----LSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1655 EEAEKELEkwrqkANEALRLRLQAEDEAHKktlaqeeaekqKEEAEREAKKRAKAEESALKQKEM---AEEELERQRKIA 1731
Cdd:pfam05701 246 KDLKSKLE-----TASALLLDLKAELAAYM-----------ESKLKEEADGEGNEKKTSTSIQAAlasAKKELEEVKANI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1732 EstaqqKLTAEQELIRLRAdfdnaeqqrSLLEDELYRLKNEVAAAQQQR-------KQLEDELAKVRSEMDiLIQLKTKA 1804
Cdd:pfam05701 310 E-----KAKDEVNCLRVAA---------ASLRSELEKEKAELASLRQREgmasiavSSLEAELNRTKSEIA-LVQAKEKE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1805 EKETMsnTEKSKQLLEA--EAAKMKDLAEEA-SRLRAISEEAKHQRqiAEEEAARQRAEAerILKEKLAAIsEATRLKTE 1881
Cdd:pfam05701 375 AREKM--VELPKQLQQAaqEAEEAKSLAQAArEELRKAKEEAEQAK--AAASTVESRLEA--VLKEIEAAK-ASEKLALA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1882 AEIALKEKEAENERLRRQA----------EDEAYQRKALEDQASQHKQeIEEKIVQLKKSSEAEMeRQKAIVDDTLKQRR 1951
Cdd:pfam05701 448 AIKALQESESSAESTNQEDsprgvtlsleEYYELSKRAHEAEELANKR-VAEAVSQIEEAKESEL-RSLEKLEEVNREME 525
|
570 580
....*....|....*....|....*....
gi 1988774676 1952 VVEEEIRILKLNFEKASSGKLDLELELNK 1980
Cdd:pfam05701 526 ERKEALKIALEKAEKAKEGKLAAEQELRK 554
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
88-167 |
4.50e-13 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 68.39 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 88 HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM----RFHKLQNVQIALDFLRHRQV----KLVNIRNDDIADGNPKLT 159
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1988774676 160 LGLIWTII 167
Cdd:cd21223 105 LALLWRII 112
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1150-1935 |
6.82e-13 |
|
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: 75.60 E-value: 6.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1150 SDVKEVETYRAKLKKMRTEAEdeqPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRwkavftqidlrq 1229
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHE---AMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ------------ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1230 reLEQLGRQLGYYRESydwlirwIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQnkdkvdECQKYAKAYiDTI 1309
Cdd:pfam01576 231 --IAELRAQLAKKEEE-------LQAALARLEEETAQKNNALKKIRELEAQISELQEDLES------ERAARNKAE-KQR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1310 KDYELQLVAYKAQVEplvsplkkTKLDSAsdNIIQEyvtlrtryselmtLTSQYIKFITDTQRRLDDEEKAAEKLKAEER 1389
Cdd:pfam01576 295 RDLGEELEALKTELE--------DTLDTT--AAQQE-------------LRSKREQEVTELKKALEEETRSHEAQLQEMR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1390 KKMA----EMQAELDKQKQLAEAHAKAIAKAEKEAQELklkmQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKD 1465
Cdd:pfam01576 352 QKHTqaleELTEQLEQAKRNKANLEKAKQALESENAEL----QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQ 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1466 KSQQVDEAlhsrTKIEEEIRLIRIQLETTEKQKYTAESELKQL---------------RDRAAEAEKLRKLaQDEAEKLR 1530
Cdd:pfam01576 428 RAELAEKL----SKLQSELESVSSLLNEAEGKNIKLSKDVSSLesqlqdtqellqeetRQKLNLSTRLRQL-EDERNSLQ 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1531 KQVSEETQKKRQAEE----------ELKRKSEAEKEAAKQ----KQKALEDLEKLRMQAEEAERQVKQAEIEKEkqiKVA 1596
Cdd:pfam01576 503 EQLEEEEEAKRNVERqlstlqaqlsDMKKKLEEDAGTLEAleegKKRLQRELEALTQQLEEKAAAYDKLEKTKN---RLQ 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1597 HEAAQKSAAAELQSKHMSFAEKTS-KLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALR-- 1673
Cdd:pfam01576 580 QELDDLLVDLDHQRQLVSNLEKKQkKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERtn 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1674 --LRLQAEDEAHKKtlaqeeaeKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTaqqKLTAEQELIRLRAD 1751
Cdd:pfam01576 660 kqLRAEMEDLVSSK--------DDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDA---KLRLEVNMQALKAQ 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1752 FDN--------AEQQRSLLEDELYRLKNEVAAAQQQRKQLEDelAKVRSEMDiLIQLKTKAEKETMSNTEKSKQLLEAEa 1823
Cdd:pfam01576 729 FERdlqardeqGEEKRRQLVKQVRELEAELEDERKQRAQAVA--AKKKLELD-LKELEAQIDAANKGREEAVKQLKKLQ- 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1824 AKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERiLKEKLAAiseatrlkteAEIALKEKEAENERLRRQAEDE 1903
Cdd:pfam01576 805 AQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQ-LQEDLAA----------SERARRQAQQERDELADEIASG 873
|
810 820 830
....*....|....*....|....*....|..
gi 1988774676 1904 AYQRKALEDQasqhKQEIEEKIVQLKKSSEAE 1935
Cdd:pfam01576 874 ASGKSALQDE----KRRLEARIAQLEEELEEE 901
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1615-2093 |
7.74e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.19 E-value: 7.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1615 FAEKTSKLEEsLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANealRLRLQAEDEAHKKTLAQEEAEK 1694
Cdd:COG4717 73 LKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ---LLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1695 qkeeaeREAKKRAKAEESALKQKEMAEEELER-QRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEV 1773
Cdd:COG4717 149 ------EELEERLEELRELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1774 AAAQQQRKQLEDELA------KVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKmkdLAEEASRLRAISEEAKHQR 1847
Cdd:COG4717 223 EELEEELEQLENELEaaaleeRLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF---LVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1848 QIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAyqrKALEDQASQhkQEIEEKIVQ 1927
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA---EELEEELQL--EELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1928 LKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLeLELNKLKNIADETQQSKIRAEEEAEKLRKLal 2007
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEELEEELEEL-- 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2008 eeekrrreaeekvkkiaAAEEEAARQRKAALE---ELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQ 2084
Cdd:COG4717 452 -----------------REELAELEAELEQLEedgELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
....*....
gi 1988774676 2085 SVLAQQIED 2093
Cdd:COG4717 515 PPVLERASE 523
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3085-3123 |
7.78e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.04 E-value: 7.78e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1988774676 3085 LLEAQAGTGYLVDPVHNQKYTVDEAVKAGVVGPELHEKL 3123
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2042-2637 |
8.75e-13 |
|
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: 75.39 E-value: 8.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2042 ERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQsVLAQQIEDSITQKKLKEEyEKAKKLAKEAEAAKEKA 2121
Cdd:pfam02463 145 EIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAE-LIIDLEELKLQELKLKEQ-AKKALEYYQLKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2122 EREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQ 2201
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE-KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2202 KFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKD 2281
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2282 STQKLLAEEAENmRKLAEDAARLSVEAQEAARLRQIAEDDL---NQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKD 2358
Cdd:pfam02463 382 ESERLSSAAKLK-EEELELKSEEEKEAQLLLELARQLEDLLkeeKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2359 LAQEQAQKLLEDKqlmQQRLEEETEEYHKSLEVERK-----RQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADK 2433
Cdd:pfam02463 461 LKDELELKKSEDL---LKETQLVKLQEQLELLLSRQkleerSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2434 VATRLHETEIATQEKMTVVERLEFERLN----TSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEK 2509
Cdd:pfam02463 538 VENYKVAISTAVIVEVSATADEVEERQKlvraLTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2510 TVLQQTFMTEKEMLLKKEKLIE-------------------DEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQ 2570
Cdd:pfam02463 618 DDKRAKVVEGILKDTELTKLKEsakakesglrkgvsleeglAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774676 2571 ATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKV 2637
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2036-2634 |
1.16e-12 |
|
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: 75.01 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2036 AALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQ------KCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKK 2109
Cdd:TIGR00618 170 MNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLctpcmpDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2110 LAKEAEAAkekaereaalLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAAlmQKQQADTEMA 2189
Cdd:TIGR00618 250 EAQEEQLK----------KQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQ--QAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2190 KHKKLAEQTLKQKFQVEQEltkvklklDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIE 2269
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQ--------QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2270 EENQRLikkdKDSTQKLLAEEAENMRKLAEDAARlSVEAQEAARLR---QIAEDDLNQQRALAEKMLKEKMQAIQEASR- 2345
Cdd:TIGR00618 390 TLTQKL----QSLCKELDILQREQATIDTRTSAF-RDLQGQLAHAKkqqELQQRYAELCAAAITCTAQCEKLEKIHLQEs 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2346 ---LKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQ-----VSQLSEAQ 2417
Cdd:TIGR00618 465 aqsLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQrgeqtYAQLETSE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2418 ARAEEEAKKFKKQA----DKVATRLHETEIATQEKMTVVERLEferlNTSKEADDLRKAIADLENEKARLKKEAEELQNK 2493
Cdd:TIGR00618 545 EDVYHQLTSERKQRaslkEQMQEIQQSFSILTQCDNRSKEDIP----NLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2494 SKEMADAQQKKIE----HEKTVLQQTFMTEKEMLLKKEK------LIEDEKKRLESQFEEEVKKAKALKDEQERQKQQME 2563
Cdd:TIGR00618 621 LQPEQDLQDVRLHlqqcSQELALKLTALHALQLTLTQERvrehalSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774676 2564 QEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRET 2634
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1941-2637 |
1.28e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.72 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1941 AIVDDTLKQRRVVEEEIRILKlnFEKASSGKLDLELELNKLKniadETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKV 2020
Cdd:PRK03918 139 AILESDESREKVVRQILGLDD--YENAYKNLGEVIKEIKRRI----ERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2021 KKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVqSVLAQQIEDSITQKKL 2100
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI-EELEEKVKELKELKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2101 KEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKE-AEFEAAKRAQaeaaalm 2179
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRlEELEERHELY------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2180 qkqqadtEMAKHKKLAEQTLKQKFQVEqELTKVKLKLDETDKQKSVLDEELQRLKDEvddavkqRGQVEEELFKVKVQME 2259
Cdd:PRK03918 365 -------EEAKAKKEELERLKKRLTGL-TPEKLEKELEELEKAKEEIEEEISKITAR-------IGELKKEIKELKKAIE 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2260 ELLKLKNKIEEENQRLIKKDKdstQKLLAEEAENMRKLAEDAARLsveaqeAARLRQIaeddlnqqralaEKMLKEKMQA 2339
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHR---KELLEEYTAELKRIEKELKEI------EEKERKL------------RKELRELEKV 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2340 IQEASRLKAEAEMLQKQKDLAQEQAQKLLEDkqlmqqrLEEETEEYHKSLEverkRQLEIMAEAERLRLQVSQLSEAQAR 2419
Cdd:PRK03918 489 LKKESELIKLKELAEQLKELEEKLKKYNLEE-------LEKKAEEYEKLKE----KLIKLKGEIKSLKKELEKLEELKKK 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2420 AEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMAD 2499
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAE 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2500 AQqKKIEhektvlqqtfMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQatmdaalsK 2579
Cdd:PRK03918 638 TE-KRLE----------ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE--------K 698
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774676 2580 QKEAEEEMLRKQKEMQELERQRleqerilaEENQKLREKLQQLEDAQKDQHTRETDKV 2637
Cdd:PRK03918 699 LKEELEEREKAKKELEKLEKAL--------ERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2193-2625 |
1.46e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.03 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2193 KLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEeelfkvkvQMEELLKLKNKIEEEN 2272
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP--------LYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2273 QRLikkdkdstqKLLAEEAENMRKLAEDAARLSVEAQEAarlrqiaeddlnqQRALAEKMLKEKMQAIQEASRLKAEAEM 2352
Cdd:COG4717 146 ERL---------EELEERLEELRELEEELEELEAELAEL-------------QEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2353 LQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEE---------- 2422
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2423 ------------EAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEEL 2490
Cdd:COG4717 284 gllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2491 QNKSKEmadaqqkkiEHEKTVLQQTFMTEKEMLLKKEKL------IEDEKKRLESQFEEEVKKAKALKDEQErqKQQMEQ 2564
Cdd:COG4717 364 QLEELE---------QEIAALLAEAGVEDEEELRAALEQaeeyqeLKEELEELEEQLEELLGELEELLEALD--EEELEE 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774676 2565 EKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQEriLAEENQKLREKLQQLEDA 2625
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE--LLQELEELKAELRELAEE 491
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1372-1911 |
2.28e-12 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 73.62 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1372 RRLDDEEKAAEKLK---AEERKKMAEMQAELDK-QKQLAEAHAKAiaKAEKEAQELKLKMQEEVSK----REIAAVDAEK 1443
Cdd:pfam05557 27 RARIELEKKASALKrqlDRESDRNQELQKRIRLlEKREAEAEEAL--REQAELNRLKKKYLEALNKklneKESQLADARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1444 QKTNIQLELQELKnlseQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKL-RKLA 1522
Cdd:pfam05557 105 VISCLKNELSELR----RQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELeFEIQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1523 Q--DEAEKLRKQVSE-------ETQKKRQAEE-----ELKRKSEAEKEAAKQKQKALEDLEKlrMQAEEAERQVKQAEIE 1588
Cdd:pfam05557 181 SqeQDSEIVKNSKSElaripelEKELERLREHnkhlnENIENKLLLKEEVEDLKRKLEREEK--YREEAATLELEKEKLE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1589 KEKQ--IKVAHEA--------AQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAE 1658
Cdd:pfam05557 259 QELQswVKLAQDTglnlrspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1659 KELEKWRQKAnealrLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTA--- 1735
Cdd:pfam05557 339 ALVRRLQRRV-----LLLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELggy 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1736 -QQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQlktkaeketMSNTEK 1814
Cdd:pfam05557 414 kQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQG---------DYDPKK 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1815 SK--QLLEAEAAKMKD-LAEEASRLRaiseeakhqrqiAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEA 1891
Cdd:pfam05557 485 TKvlHLSMNPAAEAYQqRKNQLEKLQ------------AEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKEL 552
|
570 580
....*....|....*....|
gi 1988774676 1892 ENERLRRQAEDEAYQRKALE 1911
Cdd:pfam05557 553 ESAELKNQRLKEVFQAKIQE 572
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1793-2567 |
2.47e-12 |
|
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: 73.85 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1793 EMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAI 1872
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1873 SEATRLKTEAEIALKEKEAENERLRRQaedeayqrkaleDQASQHKQEIEEKIVQlkkssEAEMERQKAIVDDTLKQRRV 1952
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQ------------QLLKQLRARIEELRAQ-----EAVLEETQERINRARKAAPL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1953 VEEEIRILKLNFeKASSGKLDLELELNKLkniADETQQSKIRAEEEAEKLRKLALeeEKRRREAEEKVKKIAAAEEEAAR 2032
Cdd:TIGR00618 296 AAHIKAVTQIEQ-QAQRIHTELQSKMRSR---AKLLMKRAAHVKQQSSIEEQRRL--LQTLHSQEIHIRDAHEVATSIRE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2033 QRKAALEELERLRKKAEEarKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAK 2112
Cdd:TIGR00618 370 ISCQQHTLTQHIHTLQQQ--KTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2113 EAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHK 2192
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLT 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2193 KLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELlklknkieeen 2272
Cdd:TIGR00618 528 RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL----------- 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2273 qrlikkdkdstQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKML-KEKMQAIQEASRLKAEAE 2351
Cdd:TIGR00618 597 -----------QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTaLHALQLTLTQERVREHAL 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2352 MLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKrQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQA 2431
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRE-LETHIEEYDREFNEIENASSSLGSDLAAREDALNQS 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2432 DKVATRLHETEIATQEkmtvverLEFERLNTSKEADDLRKA-IADLENEKARLKKEAEELQNKSKEMADAQQKKIEH--- 2507
Cdd:TIGR00618 745 LKELMHQARTVLKART-------EAHFNNNEEVTAALQTGAeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSded 817
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2508 EKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKK 2567
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4337-4375 |
2.69e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.50 E-value: 2.69e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1988774676 4337 LLEAQACTGGIIDPTSGEKYSIAEATEKGLVDKIMVDRL 4375
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1777-2627 |
2.74e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 73.71 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1777 QQQRKQLEDELAKVRSEMDiliQLKTKAEKETMSNTEKSKQ-------LLEAEAAKMK-------DLAEEASR-LRAISE 1841
Cdd:NF041483 7 QESHRADDDHLSRFEAEMD---RLKTEREKAVQHAEDLGYQvevlrakLHEARRSLASrpaydgaDIGYQAEQlLRNAQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1842 EAKHQRQIAEEEAARQRAEAERILKEKlaaISEATRLKTEAeialkEKEAeNERLRRQAEDEAYQRKALEDQ-------A 1914
Cdd:NF041483 84 QADQLRADAERELRDARAQTQRILQEH---AEHQARLQAEL-----HTEA-VQRRQQLDQELAERRQTVESHvnenvawA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1915 SQHKQEIEEKIVQLKKSSEAEMErqKAIVDDTLKQRRVVEEEIRILKLNFEKASSgkldlelelnklkniadETQQSKIR 1994
Cdd:NF041483 155 EQLRARTESQARRLLDESRAEAE--QALAAARAEAERLAEEARQRLGSEAESARA-----------------EAEAILRR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1995 AEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAAL---------EELERLRKKAEEARKQKDEADKEAEKQ 2065
Cdd:NF041483 216 ARKDAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELsraaeqrmqEAEEALREARAEAEKVVAEAKEAAAKQ 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2066 IVVAQQA-AQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAAL-------LRQQAEEAER 2137
Cdd:NF041483 296 LASAESAnEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAaedtaaqLAKAARTAEE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2138 QKTAAEE-EAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQA---DTE--MAKHKKLAEQTLKQKFQVEQeltk 2211
Cdd:NF041483 376 VLTKASEdAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAakdDTKeyRAKTVELQEEARRLRGEAEQ---- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2212 vkLKLDETDKQKSVLDEELQRLKDEVDDAVKqrgQVEEELFKVKVQMEElLKLKNKIEEENQRLIKKDKDSTQKLLAEEA 2291
Cdd:NF041483 452 --LRAEAVAEGERIRGEARREAVQQIEEAAR---TAEELLTKAKADADE-LRSTATAESERVRTEAIERATTLRRQAEET 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2292 enMRKLAEDAARLSVEAQE-AARLRQIAEDDLNQQRALAEK-MLKEKMQAIQEASRLKAEAEmlqkQKDLAQEQAqklLE 2369
Cdd:NF041483 526 --LERTRAEAERLRAEAEEqAEEVRAAAERAARELREETERaIAARQAEAAEELTRLHTEAE----ERLTAAEEA---LA 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2370 DKQLMQQRLEEETEEYHKSLEV---ERKRQLEIMAEAERLRLQVSQLSEAQARaeeeakkfKKQADKVATRLHETEIATQ 2446
Cdd:NF041483 597 DARAEAERIRREAAEETERLRTeaaERIRTLQAQAEQEAERLRTEAAADASAA--------RAEGENVAVRLRSEAAAEA 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2447 EKMTVVERLEFERLNTSKEADDLR------KAIADLENEKARLKKEAEELQNKSKEMADAQQKKI-EHEKTVLQQTFMTE 2519
Cdd:NF041483 669 ERLKSEAQESADRVRAEAAAAAERvgteaaEALAAAQEEAARRRREAEETLGSARAEADQERERArEQSEELLASARKRV 748
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2520 KEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMD-AALSKQKEAEEEMLRKQKEMQElE 2598
Cdd:NF041483 749 EEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEhAAERTRTEAQEEADRVRSDAYA-E 827
|
890 900
....*....|....*....|....*....
gi 1988774676 2599 RQRleqeriLAEENQKLREKLQQLEDAQK 2627
Cdd:NF041483 828 RER------ASEDANRLRREAQEETEAAK 850
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
72-166 |
2.74e-12 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 66.49 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 72 KTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVL-------SGETLPREKGRMRFHKLQNVQIALDFLRHRQVKLV 144
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|..
gi 1988774676 145 NIRNDDIADGNPKLTLGLIWTI 166
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQL 108
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1523-1782 |
2.91e-12 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 71.42 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1523 QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKA-LEDLEKL--RMQAEEAERQVKQAEIEKEKQIKVAHEA 1599
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAeQARQKELeqRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1600 AQKSAaaelqskhmsfAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRlRLQAE 1679
Cdd:TIGR02794 125 KAKQA-----------AEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEA-KAKAE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1680 DEAHKKtlaqeeaekqkeeaeREAKKRAKAEESALKQKE-MAEEELERQRKIAESTAQQKLTAEQELirlradfdNAEQQ 1758
Cdd:TIGR02794 193 EAKAKA---------------EAAKAKAAAEAAAKAEAEaAAAAAAEAERKADEAELGDIFGLASGS--------NAEKQ 249
|
250 260
....*....|....*....|....
gi 1988774676 1759 RSLLEDELYRLKNEVAAAQQQRKQ 1782
Cdd:TIGR02794 250 GGARGAAAGSEVDKYAAIIQQAIQ 273
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1511-1725 |
3.48e-12 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 71.76 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1511 RAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKaledleklrmQAEEAERQVKQAEIEKE 1590
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK----------QAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1591 KQIKVAHEAAQKSAAAElqskHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDA-ENSREEAEKELEKWRQKan 1669
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAE----AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAaAKAAAEAKKKAEAEAKK-- 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774676 1670 ealrlrlQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELE 1725
Cdd:PRK09510 210 -------KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1406-1660 |
5.21e-12 |
|
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: 70.95 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1406 AEAHAKAIAKAEKEAQELKLKMQEEVSKREiaavDAEKQKTNIQLELQELknlsEQQIKDKSQQVDEalhsrtkIEEEIR 1485
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELA----ALKKEEKALLKQLAAL----ERRIAALARRIRA-------LEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1486 LIRIQLETTEKQKYTAESELKQLRDRAAE-AEKLRKLAQDEAEKLRKQVSEETQKKRQAeEELKRKSEAEKEAAKQKQKA 1564
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLDAVRRL-QYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1565 LEDLEKLRmqaeeaerqvkqAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLK 1644
Cdd:COG4942 159 LAELAALR------------AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*.
gi 1988774676 1645 KQQEDAENSREEAEKE 1660
Cdd:COG4942 227 ALIARLEAEAAAAAER 242
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2758-2795 |
5.88e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.73 E-value: 5.88e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1988774676 2758 LLEAQAATGYMLDPIKNQKLSVNAAVKEGLIGPELHNK 2795
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1852-2489 |
6.43e-12 |
|
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: 72.45 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1852 EEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAL--EDQASQHKQEI--EEKIVQ 1927
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikENNATRHLCNLlkETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1928 LKKSSEAEMERQKAI-----VDDTLKQRRVVEEEIRIlklnfeKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKL 2002
Cdd:pfam05483 168 AEKTKKYEYEREETRqvymdLNNNIEKMILAFEELRV------QAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2003 RKLALEEEKRRREAEEKVKKIAAAEeeaaRQRKAALEELERLR-KKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQ 2081
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEES----RDKANQLEEKTKLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2082 QVQ---SVLAQQIEDSITQkkLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAER 2158
Cdd:pfam05483 318 DLQiatKTICQLTEEKEAQ--MEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2159 L-----RKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTL-----------------------------KQKFQ 2204
Cdd:pfam05483 396 MtkfknNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELifllqarekeihdleiqltaiktseehylKEVED 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2205 VEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLiKKDKDSTQ 2284
Cdd:pfam05483 476 LKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNL-RDELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2285 KLLAEEAENMR----KLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLA 2360
Cdd:pfam05483 555 EEFIQKGDEVKckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2361 QEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEE-----------AKKFKK 2429
Cdd:pfam05483 635 EIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRcqhkiaemvalMEKHKH 714
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774676 2430 QADKVA----TRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEE 2489
Cdd:pfam05483 715 QYDKIIeerdSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2182-2713 |
7.16e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.26 E-value: 7.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2182 QQADTEMAKHKKLAEQTlkQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQmeEL 2261
Cdd:COG4913 265 AAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD--RL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2262 LKLKNKIEEENQRLIKKDKDSTQklLAEEAENMR-KLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAI 2340
Cdd:COG4913 341 EQLEREIERLERELEERERRRAR--LEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2341 QEASRLKAEAEMLQKQK---DLAQEQAQKLLEDK------------QLMQQRLEEEteEYHKSLE-----------VERK 2394
Cdd:COG4913 419 RELRELEAEIASLERRKsniPARLLALRDALAEAlgldeaelpfvgELIEVRPEEE--RWRGAIErvlggfaltllVPPE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2395 RQLEIMA--EAERLRLQVSQLSEAQARAEEEAKKFKKQ--ADKVATRLH------ETEIATQEKMTVVERLE-FERLN-- 2461
Cdd:COG4913 497 HYAAALRwvNRLHLRGRLVYERVRTGLPDPERPRLDPDslAGKLDFKPHpfrawlEAELGRRFDYVCVDSPEeLRRHPra 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2462 -----------TSKEADDL-------------RKAIADLENEKARLKKEAEELQNKSKEMADAQQ--KKIEHEKTVLQQT 2515
Cdd:COG4913 577 itragqvkgngTRHEKDDRrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEY 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2516 FMTEKEMLLKKEKL--IEDEKKRLES------QFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEM 2587
Cdd:COG4913 657 SWDEIDVASAEREIaeLEAELERLDAssddlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2588 LRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKVlhkdiihlTTIETTKTVYNGQNVGDVVDGI 2667
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAE--------EELERAMRAFNREWPAETADLD 808
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1988774676 2668 DKKPDPLAFDGIRDKVPASRLHELgvlpKKEFDKLKNgETTVQELG 2713
Cdd:COG4913 809 ADLESLPEYLALLDRLEEDGLPEY----EERFKELLN-ENSIEFVA 849
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
191-290 |
9.91e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 64.28 E-value: 9.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 191 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN---LENLEQAFSVAEK-DLGVTRLL 266
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1988774676 267 DPEDVdVPHPDEKSIITYVSSLYD 290
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2834-2871 |
1.61e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 1.61e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1988774676 2834 VLEAQLATGGIIDPINSHRVPTETAYKQGHYDAEMNKI 2871
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
65-164 |
1.70e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 63.98 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 65 ERDRvQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLE-VLSGE-------TLPREKGRMRFHKLQNVQIALDFL 136
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDkVIPGSvnwkkvnKAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1988774676 137 RHRQVKLVNIRNDDIADGNPKLTLGLIW 164
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3826-3863 |
1.70e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 1.70e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1988774676 3826 LEAQTATGGIIDPEFQFHLPTDVAMQRGYINKETNEKL 3863
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1724-2605 |
1.74e-11 |
|
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: 71.23 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1724 LERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRslleDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTK 1803
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIR----DQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1804 AEK--ETMSNTEKSKQLLEAEAAKMKDLAEEAsrLRAISEEAK---HQRQIAEEEAARQRAEAERILKEKLAAISEATRL 1878
Cdd:TIGR00606 264 IMKldNEIKALKSRKKQMEKDNSELELKMEKV--FQGTDEQLNdlyHNHQRTVREKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1879 KTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQAS----QHKQEIEEKIVQLKKSSEAEMERQKAIV---------DD 1945
Cdd:TIGR00606 342 KTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfERGPFSERQIKNFHTLVIERQEDEAKTAaqlcadlqsKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1946 TLKQRRVVEEEIRILKLNfEKASSGKLDLELELNKLKNIADETQQ---SKIRAEEEAEKLRKLALEEEKRRREAEEKVKK 2022
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLG-RTIELKKEILEKKQEELKFVIKELQQlegSSDRILELDQELRKAERELSKAEKNSLTETLK 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2023 iaaaeeeaARQRKAALEELERLRKKAEEARKQKD-EADKEAEKQIvvaQQAAQKCSAAEQQVQSVLAQQIEDSITQ---- 2097
Cdd:TIGR00606 501 --------KEVKSLQNEKADLDRKLRKLDQEMEQlNHHTTTRTQM---EMLTKDKMDKDEQIRKIKSRHSDELTSLlgyf 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2098 ----------KKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQE---DAERLRKEAE 2164
Cdd:TIGR00606 570 pnkkqledwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDeesDLERLKEEIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2165 FEAAKRAQAEAAALMQKQQAdTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDET-----DKQKSvLDEELQRLKDEVDD 2239
Cdd:TIGR00606 650 KSSKQRAMLAGATAVYSQFI-TQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKlrlapDKLKS-TESELKKKEKRRDE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2240 AVkqrGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKD-STQKLLAEEAENMRKLAEDA-------ARLSVEAQEA 2311
Cdd:TIGR00606 728 ML---GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDiEEQETLLGTIMPEEESAKVCltdvtimERFQMELKDV 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2312 AR--LRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLledkqlmQQRLEE-ETEEYHKS 2388
Cdd:TIGR00606 805 ERkiAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL-------KSKTNElKSEKLQIG 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2389 LEVERKRQLE-----IMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERlefERLNTS 2463
Cdd:TIGR00606 878 TNLQRRQQFEeqlveLSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKE---KVKNIH 954
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2464 KEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEK--EMLLKKE---KLIEDEKKRLE 2538
Cdd:TIGR00606 955 GYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKiqERWLQDNltlRKRENELKEVE 1034
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2539 ---SQFEEEVKKAKALKDEQERQKqqMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQE 2605
Cdd:TIGR00606 1035 eelKQHLKEMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
191-291 |
1.83e-11 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 63.53 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 191 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 270
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 1988774676 271 VdVPHPDEKSIITYVSSLYDA 291
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1616-2061 |
2.06e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.84 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1616 AEKTSK-LEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLR-----LQ---AEDEAHKKT 1686
Cdd:PRK02224 197 EEKEEKdLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEaeiedLRetiAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1687 LAQEEAEKQKEEAEREAKKRAKAEESAL----------------KQKEMAEEELERQR-----------------KIAES 1733
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLddadaeavearreeleDRDEELRDRLEECRvaaqahneeaeslredaDDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1734 TAQQKL----TAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQ--LKTKAEKE 1807
Cdd:PRK02224 357 RAEELReeaaELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREreAELEATLR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1808 TMSNT-EKSKQLLEA--------------EAAKMKDLAEEASRLRAISEEAKHQRQIAEE--EAARQRAEAERILKEKLA 1870
Cdd:PRK02224 437 TARERvEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEErlERAEDLVEAEDRIERLEE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1871 AISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLkksseAEMERQKAIVDDTLKQR 1950
Cdd:PRK02224 517 RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV-----AELNSKLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1951 RVVEEEirilklnFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLAleeekrrreaeekvKKIAAAEEEA 2030
Cdd:PRK02224 592 ERIRTL-------LAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELE--------------AEFDEARIEE 650
|
490 500 510
....*....|....*....|....*....|..
gi 1988774676 2031 ARQRKAALEE-LERLRKKAEEARKQKDEADKE 2061
Cdd:PRK02224 651 AREDKERAEEyLEQVEEKLDELREERDDLQAE 682
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2215-2628 |
2.19e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2215 KLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEE--------ENQRLIKKDKDSTQKL 2286
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDlretiaetEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2287 LAEEAENMRKLAEDAARLSVEAQEAARLRQiaeDDLNQQRALAEKMLKEKMQAIQEAsrlKAEAEMLQKQKDLAQEQAQK 2366
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDADAEAVEARR---EELEDRDEELRDRLEECRVAAQAH---NEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2367 LLEDKQlmqqRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQ 2446
Cdd:PRK02224 361 LREEAA----ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2447 EKMTVVERLEfERLNTSK---------------EADDLRKAIADLENEKARLKKEAEELQNKSKEMADAqqKKIEHEKTV 2511
Cdd:PRK02224 437 TARERVEEAE-ALLEAGKcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL--VEAEDRIER 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2512 LQQTFMTEKEMLLKKEKLIEDEKKRLESQFEE--------EVKKAKALKDEQERQKQQ-----MEQEKKTLQATMDA--- 2575
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERaaeleaeaEEKREAAAEAEEEAEEAReevaeLNSKLAELKERIESler 593
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774676 2576 ---ALSKQKEAEEEMLR---KQKEMQELERQRLEQ-----ERI--LAEEN-----QKLREKLQQLEDAQKD 2628
Cdd:PRK02224 594 irtLLAAIADAEDEIERlreKREALAELNDERRERlaekrERKreLEAEFdeariEEAREDKERAEEYLEQ 664
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1373-1898 |
2.42e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1373 RLDDEEKAAEKLKaEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKlkmqEEVSKREIAAVDAEKQKTNIQLEL 1452
Cdd:PRK03918 156 GLDDYENAYKNLG-EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVL----REINEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1453 QELKNLSEQqIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKqkytaesELKQLRDRAAEAEKLRKLAqDEAEKLRKQ 1532
Cdd:PRK03918 231 KELEELKEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKK-------EIEELEEKVKELKELKEKA-EEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1533 VSEETQKKRQAEEELKRKSEAEKEAakqkQKALEDLEKLRMQAEEAERQVKqaEIEKEKqikvaheaaqksaaAELQSKH 1612
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGI----EERIKELEEKEERLEELKKKLK--ELEKRL--------------EELEERH 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1613 MSFAEKTSKLE--ESLKQEHGAvlqlqQEAERLKKQQEDAENSREEAEKELEKWRQK----ANEALRLRLQAE------- 1679
Cdd:PRK03918 362 ELYEEAKAKKEelERLKKRLTG-----LTPEKLEKELEELEKAKEEIEEEISKITARigelKKEIKELKKAIEelkkakg 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1680 ---------DEAHKKTLAQ---------EEAEKQKEEAEREAKKRAKAEESAL-------KQKEMAE------------- 1721
Cdd:PRK03918 437 kcpvcgrelTEEHRKELLEeytaelkriEKELKEIEEKERKLRKELRELEKVLkkeseliKLKELAEqlkeleeklkkyn 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1722 -EELERQRKIAESTAQQKLTAEQELIRLRADF-----------------DNAEQQRSLLEDELY---------------- 1767
Cdd:PRK03918 517 lEELEKKAEEYEKLKEKLIKLKGEIKSLKKELekleelkkklaelekklDELEEELAELLKELEelgfesveeleerlke 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1768 ---------RLKN---EVAAAQQQRKQLEDELAKVRSEMDiliQLKTKAEKETMSNTEKSKQLLEAEAAKMKD----LAE 1831
Cdd:PRK03918 597 lepfyneylELKDaekELEREEKELKKLEEELDKAFEELA---ETEKRLEELRKELEELEKKYSEEEYEELREeyleLSR 673
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774676 1832 EASRLRAISEEAKHQRQIAEEEAarqraeaeRILKEKLAAISEATRLKTEAEIALKEKEAENERLRR 1898
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTL--------EKLKEELEEREKAKKELEKLEKALERVEELREKVKK 732
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2227-2601 |
5.21e-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: 69.71 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2227 DEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKiEEENQRLIKKDKDSTQKLLAEEAENMRKLAE--DAARL 2304
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK-AERYQALLKEKREYEGYELLKEKEALERQKEaiERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2305 SVEAQEAARLRQIaeDDLNQQRALAEKMLKEKMQAIQEasrlKAEAEMLQKQKDLA-----QEQAQKLLEDKQLMQQRLE 2379
Cdd:TIGR02169 248 SLEEELEKLTEEI--SELEKRLEEIEQLLEELNKKIKD----LGEEEQLRVKEKIGeleaeIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2380 EETEEYhkslEVERKRQLEimaEAERLRLQVSQLseaqaraeeeakkfKKQADKVATRLHETEiatQEKMTVVERLEFEr 2459
Cdd:TIGR02169 322 ERLAKL----EAEIDKLLA---EIEELEREIEEE--------------RKRRDKLTEEYAELK---EELEDLRAELEEV- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2460 lntSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEhektvlqqtfmtEKEMLLKKEKLIEDEKKRLES 2539
Cdd:TIGR02169 377 ---DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE------------ELADLNAAIAGIEAKINELEE 441
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 2540 QFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMdaalSKQKEAEEEMLRKQKEMQELERQR 2601
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK----EEYDRVEKELSKLQRELAEAEAQA 499
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2472-2636 |
5.67e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2472 AIADLENEKARLKKEAEELQNKSKEmADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLEsQFEEEVKKAKAL 2551
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEE-LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2552 KDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHT 2631
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
....*
gi 1988774676 2632 RETDK 2636
Cdd:COG1196 391 ALRAA 395
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1541-1944 |
5.94e-11 |
|
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: 69.60 E-value: 5.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1541 RQAEEE---LKRKSEAEKE-AAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAeLQSKHMSFA 1616
Cdd:COG3096 275 RHANERrelSERALELRRElFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1617 EKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWrQKANEALRLR-------LQAEDEAhkKTLAQ 1689
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADY-QQALDVQQTRaiqyqqaVQALEKA--RALCG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1690 EEAEKQKEEAEREAKKRAKAEES-----ALKQK----EMA----EEELERQRKIA-ESTAQQKLTAEQELIRLRADFDNA 1755
Cdd:COG3096 431 LPDLTPENAEDYLAAFRAKEQQAteevlELEQKlsvaDAArrqfEKAYELVCKIAgEVERSQAWQTARELLRRYRSQQAL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1756 EQQRSLLEDELYRLKNEVAAAQQQRKQLEdELAKvrsemdiliqlktKAEKETMSNTEKSKQLLEAEAaKMKDLAEEASR 1835
Cdd:COG3096 511 AQRLQQLRAQLAELEQRLRQQQNAERLLE-EFCQ-------------RIGQQLDAAEELEELLAELEA-QLEELEEQAAE 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1836 LRAISEEAKHQRqiaeEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAyQRKALEDQAS 1915
Cdd:COG3096 576 AVEQRSELRQQL----EQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERER-EATVERDELA 650
|
410 420
....*....|....*....|....*....
gi 1988774676 1916 QHKQEIEEKIVQLKKSSEAEMERQKAIVD 1944
Cdd:COG3096 651 ARKQALESQIERLSQPGGAEDPRLLALAE 679
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1720-1941 |
5.99e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 67.93 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1720 AEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQ 1799
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1800 lktkAEKETMSNTEKSKQLLEAEaakmkDLAEEASRLRAISEEAKHQRQI------AEEEAARQRAEAERILKEKLAAIS 1873
Cdd:COG3883 94 ----ALYRSGGSVSYLDVLLGSE-----SFSDFLDRLSALSKIADADADLleelkaDKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774676 1874 EATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKA 1941
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3161-3199 |
6.13e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.65 E-value: 6.13e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1988774676 3161 LLDAQMTTGGIIDPVKSHRIPHDVACKRNYFDDEMKQAL 3199
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3492-3530 |
6.25e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.65 E-value: 6.25e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1988774676 3492 LLEAQIVSGGIIDPVKSHRVPTDVAYQKNILSRDIAKTL 3530
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1153-1646 |
7.49e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1153 KEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQREL 1232
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1233 EQLGRQLGYYRESY-DWLIRWIADAKQRQEKIQAvpitdsktLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKD 1311
Cdd:COG1196 361 AEAEEALLEAEAELaEAEEELEELAEELLEALRA--------AAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1312 YELQLVAYKAQVEplvsplkktKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKK 1391
Cdd:COG1196 433 LEEEEEEEEEALE---------EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1392 MAEMQAELDKQKQLA---------------EAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQ--KTNIQLELQE 1454
Cdd:COG1196 504 EGFLEGVKAALLLAGlrglagavavligveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgrATFLPLDKIR 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1455 LKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEK-----QKYTAESELKQLRDRAAEAEKLRKLAQDEAEKL 1529
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRtlvaaRLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1530 RKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQ 1609
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
490 500 510
....*....|....*....|....*....|....*..
gi 1988774676 1610 SKHMSFAEKTSKLEESLKQEhgavlQLQQEAERLKKQ 1646
Cdd:COG1196 744 EEELLEEEALEELPEPPDLE-----ELERELERLERE 775
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2202-2627 |
8.08e-11 |
|
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: 69.10 E-value: 8.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2202 KFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEE-LFKVKVQMEELLKLKNKIEEENQR---LIK 2277
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERlkaLTG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2278 KDKDSTQKLLAEEA----ENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQ-RALAEKMLKEKMQAIQEASRLKAEAEM 2352
Cdd:pfam12128 369 KHQDVTAKYNRRRSkikeQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeSELREQLEAGKLEFNEEEYRLKSRLGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2353 LQKQKDLAQeqaqklLEDKQLMQQRLEEEteeyhkslEVERKRQLEIMAEAERLRLQvsqlseaqaraeEEAKKFKKQAD 2432
Cdd:pfam12128 449 LKLRLNQAT------ATPELLLQLENFDE--------RIERAREEQEAANAEVERLQ------------SELRQARKRRD 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2433 KVATRLHETEIATQEKMTVVERLEFERLNTSKEADD-LRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHE--- 2508
Cdd:pfam12128 503 QASEALRQASRRLEERQSALDELELQLFPQAGTLLHfLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNlyg 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2509 -KTVLQQTFMTEKEMLlkkekliEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEM 2587
Cdd:pfam12128 583 vKLDLKRIDVPEWAAS-------EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDL 655
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1988774676 2588 LRKQKEMQELERQRleqERILAEENQKLREKLQQLEDAQK 2627
Cdd:pfam12128 656 RRLFDEKQSEKDKK---NKALAERKDSANERLNSLEAQLK 692
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1501-1738 |
8.60e-11 |
|
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: 67.48 E-value: 8.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1501 AESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVseetqkkRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAER 1580
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1581 QVKQAEIEKEKQIKVAHEAAQKSAAAELQSkhmsfAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKE 1660
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1661 LEKWRQ--KANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK 1738
Cdd:COG4942 173 RAELEAllAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1549-1962 |
9.29e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 9.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1549 RKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQ 1628
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1629 EHGAVLQLQQEAERLKKQQEDaensREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAK 1708
Cdd:COG4717 144 LPERLEELEERLEELRELEEE----LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1709 AE----ESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQR---------SLLEDELYRLKNEVAA 1775
Cdd:COG4717 220 EEleelEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1776 AQQQRKQLEDELAKVRSEMDILIQLKtkaeKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAE---- 1851
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELL----AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaal 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1852 --------EEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAEN--ERLRRQAEDEAYQRKALEDQASQHKQEI 1921
Cdd:COG4717 376 laeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1988774676 1922 EEKIVQLKK-SSEAEMERQKAIVDDTLKQRRVVEEEIRILKL 1962
Cdd:COG4717 456 AELEAELEQlEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
191-286 |
1.02e-10 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 61.63 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 191 KEKLLLWSQRMtdgYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLI-NMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPE 269
Cdd:cd21229 5 KKLMLAWLQAV---LPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1988774676 270 DVDVPHPDEKSIITYVS 286
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3987-4025 |
1.17e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.88 E-value: 1.17e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1988774676 3987 LLESQAATGYVIDPIKNLKLTVNEAVKMGIVGPEFKDKL 4025
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4335-4372 |
1.18e-10 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 59.03 E-value: 1.18e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1988774676 4335 QRLLEAQACTGGIIDPTSGEKYSIAEATEKGLVDKIMV 4372
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1381-1841 |
1.36e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 68.31 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1381 AEKLKAEERKKMAEMQAEldKQKQLAEAHAKA---IAKAEKEAQE-------LKLKMQEEVSK-REIAAVDAEKQKTNIQ 1449
Cdd:NF041483 737 SEELLASARKRVEEAQAE--AQRLVEEADRRAtelVSAAEQTAQQvrdsvagLQEQAEEEIAGlRSAAEHAAERTRTEAQ 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1450 LELQELKNlseqqikDKSQQVDEALHSRTKIEEEIRliriqlETTEKQKYTAEselKQLRDRAAEAEKLRKLAQDEAEKL 1529
Cdd:NF041483 815 EEADRVRS-------DAYAERERASEDANRLRREAQ------EETEAAKALAE---RTVSEAIAEAERLRSDASEYAQRV 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1530 RKQVSEetqkkrqaeeelkRKSEAEKEAAKQKQKALEDLEKLRMQA------------EEAERQVKQAEIEKEKQIKVAH 1597
Cdd:NF041483 879 RTEASD-------------TLASAEQDAARTRADAREDANRIRSDAaaqadrligeatSEAERLTAEARAEAERLRDEAR 945
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1598 EAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKqqeDAENSREEAEKELEKWRQKA-NEALRLRL 1676
Cdd:NF041483 946 AEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRT---EAERVKAEAAAEAERLRTEArEEADRTLD 1022
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1677 QAEDEAHKK-TLAQEEAEKQKEEAEREAKK-RAKAEESALKQKEMAEEEL---------ERQRKIAESTAQ--------- 1736
Cdd:NF041483 1023 EARKDANKRrSEAAEQADTLITEAAAEADQlTAKAQEEALRTTTEAEAQAdtmvgaarkEAERIVAEATVEgnslvekar 1102
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1737 -------------------------QKLTAEQELIRLRADFDNAEQQRSLLEdelyRLKNEVAAAQQQRKQLE------- 1784
Cdd:NF041483 1103 tdadellvgarrdataireraeelrDRITGEIEELHERARRESAEQMKSAGE----RCDALVKAAEEQLAEAEakakelv 1178
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1785 ----DELAKVR----SEMDILI---------------QLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISE 1841
Cdd:NF041483 1179 sdanSEASKVRiaavKKAEGLLkeaeqkkaelvreaeKIKAEAEAEAKRTVEEGKRELDVLVRRREDINAEISRVQDVLE 1258
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1371-1592 |
1.46e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 67.84 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1371 QRRLDDEEKAAEKLKAEERKK------MAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL----KLKMQEEVSKREIAAVD 1440
Cdd:pfam17380 340 ERMAMERERELERIRQEERKRelerirQEEIAMEISRMRELERLQMERQQKNERVRQELeaarKVKILEEERQRKIQQQK 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1441 AEKQKTNIQLE---LQELKNLSEQQIKDKSQQVDEALHSRTKIE------EEIRLIRIQLETTEKQKYTAESELKQLRDR 1511
Cdd:pfam17380 420 VEMEQIRAEQEearQREVRRLEEERAREMERVRLEEQERQQQVErlrqqeEERKRKKLELEKEKRDRKRAEEQRRKILEK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1512 AAEAeklRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQ------------KALEdlEKLRMQAEEAE 1579
Cdd:pfam17380 500 ELEE---RKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEmeerrriqeqmrKATE--ERSRLEAMERE 574
|
250
....*....|...
gi 1988774676 1580 RQVKQAEIEKEKQ 1592
Cdd:pfam17380 575 REMMRQIVESEKA 587
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
63-170 |
1.62e-10 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 61.45 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 63 ADERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLP----REKGRMRFHKLQNVQIALDFLRH 138
Cdd:cd21222 10 APEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELMED 89
|
90 100 110
....*....|....*....|....*....|..
gi 1988774676 139 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 170
Cdd:cd21222 90 AGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1862-2629 |
1.63e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.84 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1862 ERILKEKLAAISEATRLKTEAEiALKEKEAENER-----LRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEaEM 1936
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLNESN-ELHEKQKFYLRqsvidLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH-EL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1937 ERQKAIVDDTLKQ--------RRV------VEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAE-- 2000
Cdd:pfam15921 155 EAAKCLKEDMLEDsntqieqlRKMmlshegVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEis 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2001 --KLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALE---ELERLRKKAEEARKQKDEADKEAEkqiVVAQQAAQK 2075
Cdd:pfam15921 235 ylKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEhevEITGLTEKASSARSQANSIQSQLE---IIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2076 CSAAEQQVQsvlaqQIEDSITQkkLKEEYEKAKKlakeaeaakekaereaaLLRQQAEEAERQKTAAeeeaanqakaqeD 2155
Cdd:pfam15921 312 NSMYMRQLS-----DLESTVSQ--LRSELREAKR-----------------MYEDKIEELEKQLVLA------------N 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2156 AERLRKEAEFEAAKRAQAEAAALMQKQQADTemakHKKLAEQTLkqkfqvEQELTKvklKLDETDKQKSVLDEELQRlkd 2235
Cdd:pfam15921 356 SELTEARTERDQFSQESGNLDDQLQKLLADL----HKREKELSL------EKEQNK---RLWDRDTGNSITIDHLRR--- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2236 EVDDAVKQRGQVEEELFKVKV----QMEELLKlknKIEEENQRLIKKDKDSTQklLAEEAENMRKLAED--AARLSVEAQ 2309
Cdd:pfam15921 420 ELDDRNMEVQRLEALLKAMKSecqgQMERQMA---AIQGKNESLEKVSSLTAQ--LESTKEMLRKVVEEltAKKMTLESS 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2310 EaarlRQIAedDLNQQralaekmLKEKMQAIQEASrlkAEAEMLQKQKDLAQEQAQKL------LEDKQLMQQRLEEETE 2383
Cdd:pfam15921 495 E----RTVS--DLTAS-------LQEKERAIEATN---AEITKLRSRVDLKLQELQHLknegdhLRNVQTECEALKLQMA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2384 EYHKSLEVERKrQLEIMAE--------AERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQ----EKMTV 2451
Cdd:pfam15921 559 EKDKVIEILRQ-QIENMTQlvgqhgrtAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSdlelEKVKL 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2452 V----ERLEFERlNTSKEADDLRKAIADLENEKARLKKEAEELQ----NKSKEMADAQQK---KIEHEKTVLQQTFMTEK 2520
Cdd:pfam15921 638 VnagsERLRAVK-DIKQERDQLLNEVKTSRNELNSLSEDYEVLKrnfrNKSEEMETTTNKlkmQLKSAQSELEQTRNTLK 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2521 EM----------LLKKEKLIEDEKKRLES-----QFEEEV-----KKAKALKDEQERQKQQME---QEKKTLQATMDAAL 2577
Cdd:pfam15921 717 SMegsdghamkvAMGMQKQITAKRGQIDAlqskiQFLEEAmtnanKEKHFLKEEKNKLSQELStvaTEKNKMAGELEVLR 796
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 2578 SKQKEAEEEMLRKQKEMQELERQRLE-QERILAEENQKLREKLQQLEDAQKDQ 2629
Cdd:pfam15921 797 SQERRLKEKVANMEVALDKASLQFAEcQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1377-1610 |
1.71e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 66.37 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1377 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEahakaiakaekeAQELKlkmqeevskreiaavdaekqktniQLELQELK 1456
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAE------------QERLK------------------------QLEKERLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1457 nlSEQQIKDKSQQVDEALHSRTKIEEEirliriQLETTEKQKYTAESELKQLRDRAAEAE-KLRKLAQDEAEklrKQVSE 1535
Cdd:PRK09510 113 --AQEQKKQAEEAAKQAALKQKQAEEA------AAKAAAAAKAKAEAEAKRAAAAAKKAAaEAKKKAEAEAA---KKAAA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774676 1536 ETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQS 1610
Cdd:PRK09510 182 EAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
552-741 |
1.99e-10 |
|
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: 63.62 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 552 LRYVQDLLAWVEENQRRIDNAEWGSDLPSMESQLGSHRGLHQTVEDFKSKIERAKADETQL---SPVSKGTYREYLGKLD 628
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 629 LQYGKLLNSSKSRLRNLE---SLHAFVSAATKELMWLNDKEEEEVNFDWSDRNTNMTAKKDNYSGLMRELELREKKVNDI 705
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1988774676 706 QALGDRLVRDGHPGK-KTVESFTAALQTQWSWILQLC 741
Cdd:cd00176 166 NELAEELLEEGHPDAdEEIEEKLEELNERWEELLELA 202
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2362-2652 |
2.03e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2362 EQAQKLLEDKQLMQQRLE---EETEEYHKSLEVERK---RQLEIMAEAERLRLQVSQLSEAQARAEEeaKKFKKQADKVA 2435
Cdd:TIGR02168 175 KETERKLERTRENLDRLEdilNELERQLKSLERQAEkaeRYKELKAELRELELALLVLRLEELREEL--EELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2436 TRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKA-------IADLENEKARLKKEAEELQNKSKEMADAQQKKIEHe 2508
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESK- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2509 ktvlqqtfmteKEMLLKKEKLIEDEKKRLESQFEEEVKKAKalkdEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEML 2588
Cdd:TIGR02168 332 -----------LDELAEELAELEEKLEELKEELESLEAELE----ELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774676 2589 RKQKEMQELERQ--RLEQER-ILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDIIHLTTIETTK 2652
Cdd:TIGR02168 397 SLNNEIERLEARleRLEDRReRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1460-1659 |
2.87e-10 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 65.25 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1460 EQQIKDKSQQVDEAlhsRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKlaqdeAEKLRKQVSEetqk 1539
Cdd:TIGR02794 49 AQQANRIQQQKKPA---AKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEE---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1540 KRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAElqskhmsfAEKT 1619
Cdd:TIGR02794 117 KQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAE--------AEAK 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1988774676 1620 SKLEESLKQEHGAVLQLQQEAERlKKQQEDAENSREEAEK 1659
Cdd:TIGR02794 189 AKAEEAKAKAEAAKAKAAAEAAA-KAEAEAAAAAAAEAER 227
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1791-2512 |
3.14e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 67.17 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1791 RSEMDILIQLKTKAEKETMSNTEKSKQLL---EAEAAKMKDLAEEAS-------RLRAISEEAK-HQRQIAEEEAARQRA 1859
Cdd:pfam12128 205 ILEDDGVVPPKSRLNRQQVEHWIRDIQAIagiMKIRPEFTKLQQEFNtlesaelRLSHLHFGYKsDETLIASRQEERQET 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1860 EAEriLKEKLAA--------ISEATRLKTEAEIALKEKEAENERLRRQA----EDEAYQRKALEDQASQHKQEIEEKIVQ 1927
Cdd:pfam12128 285 SAE--LNQLLRTlddqwkekRDELNGELSAADAAVAKDRSELEALEDQHgaflDADIETAAADQEQLPSWQSELENLEER 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1928 LK------KSSEAEMERQKAIVDDTLKqrRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEK 2001
Cdd:pfam12128 363 LKaltgkhQDVTAKYNRRRSKIKEQNN--RDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEY 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2002 LRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKqivvAQQAAQKCSAAEQ 2081
Cdd:pfam12128 441 RLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQ----ASEALRQASRRLE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2082 QVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEaakekaereaalLRQQAEEAERQKTAAEEEAANQAKAQE------- 2154
Cdd:pfam12128 517 ERQSALDELELQLFPQAGTLLHFLRKEAPDWEQS------------IGKVISPELLHRTDLDPEVWDGSVGGElnlygvk 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2155 -DAERLRKEAEFEAAKRAQAEAAALmqKQQADTEMAKHKKLAEQTLKQKFQVEQ---ELTKVKLKLDETDKQKSVLDEEL 2230
Cdd:pfam12128 585 lDLKRIDVPEWAASEEELRERLDKA--EEALQSAREKQAAAEEQLVQANGELEKasrEETFARTALKNARLDLRRLFDEK 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2231 QRLKDEVDDAVKQR-GQVEEELFKVKVQMEELL-KLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAE-DAARLSVE 2307
Cdd:pfam12128 663 QSEKDKKNKALAERkDSANERLNSLEAQLKQLDkKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALlKAAIAARR 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2308 AQEAARLRQIAEDdlnQQRALAEKMLKEkmqaiQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHK 2387
Cdd:pfam12128 743 SGAKAELKALETW---YKRDLASLGVDP-----DVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLAT 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2388 SLEverkrqlEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLheteiatQEKMTVVeRLEFERLNTSKEAD 2467
Cdd:pfam12128 815 QLS-------NIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRL-------SENLRGL-RCEMSKLATLKEDA 879
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1988774676 2468 DlrkaIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVL 2512
Cdd:pfam12128 880 N----SEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVI 920
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1542-1945 |
4.25e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.52 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1542 QAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVkQAEIEKEKQIKVAHEAA----QKSAAAELQSKHM---- 1613
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMAREL-AELNEAESDLEQDYQAAsdhlNLVQTALRQQEKIeryq 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1614 -SFAEKTSKLEESLkqehgAVLQLQQEaerlkkQQEDAENSREEAEKELEKWR------QKANEALRLR-------LQAE 1679
Cdd:PRK04863 355 aDLEELEERLEEQN-----EVVEEADE------QQEENEARAEAAEEEVDELKsqladyQQALDVQQTRaiqyqqaVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1680 DEAhkKTLAQEEAEKQKEEAEREAKKRAKAEESALkqkemAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQ- 1758
Cdd:PRK04863 424 ERA--KQLCGLPDLTADNAEDWLEEFQAKEQEATE-----ELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWd 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1759 --RSLLED--ELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKeTMSNTEKSKQLLEAEAAKMKDLAEEAS 1834
Cdd:PRK04863 497 vaRELLRRlrEQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGK-NLDDEDELEQLQEELEARLESLSESVS 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1835 RLRAISEEAKHQRqiaeEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAlEDQA 1914
Cdd:PRK04863 576 EARERRMALRQQL----EQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVE-RDEL 650
|
410 420 430
....*....|....*....|....*....|.
gi 1988774676 1915 SQHKQEIEEKIVQLKKSSEAEMERQKAIVDD 1945
Cdd:PRK04863 651 AARKQALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1541-2089 |
6.04e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1541 RQAEEELKRKSEAEKEA--AKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKqikVAHEAAQKsAAAELQskhmsfaek 1618
Cdd:COG4913 228 DALVEHFDDLERAHEALedAREQIELLEPIRELAERYAAARERLAELEYLRAA---LRLWFAQR-RLELLE--------- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1619 tsKLEESLKQEHGavlQLQQEAERLKKQQEDAENSREEAEkelEKWRQKANEALRlRLQAEDEAHKKTLaqeeaekqkee 1698
Cdd:COG4913 295 --AELEELRAELA---RLEAELERLEARLDALREELDELE---AQIRGNGGDRLE-QLEREIERLEREL----------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1699 aeREAKKRAKAEESALKQKEMA----EEELERQRKIAESTAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVA 1774
Cdd:COG4913 355 --EERERRRARLEALLAALGLPlpasAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1775 AAQQQRKQLEDELAKVRSEMdiliqlktkaeketmsntekskqlleAEAakmkdLAEEASRLRAISEEAkhqrQIAEEEA 1854
Cdd:COG4913 430 SLERRKSNIPARLLALRDAL--------------------------AEA-----LGLDEAELPFVGELI----EVRPEEE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1855 ARQRAeAERIL----------KEKLAAISEAT-RLKTEAEI-ALKEKEAENERLRRQAEDEAYQRKaLEDQASQHKQEIE 1922
Cdd:COG4913 475 RWRGA-IERVLggfaltllvpPEHYAAALRWVnRLHLRGRLvYERVRTGLPDPERPRLDPDSLAGK-LDFKPHPFRAWLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1923 EKIVQ----LKKSSEAEMER-QKAIVDDTL---------KQRRVVEEEIRILKLNFEKassgKLD-LELELNKLKNIADE 1987
Cdd:COG4913 553 AELGRrfdyVCVDSPEELRRhPRAITRAGQvkgngtrheKDDRRRIRSRYVLGFDNRA----KLAaLEAELAELEEELAE 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1988 TQQSKIRAEEEAEKL--RKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALE---ELERLRKKAEEARKQKDEADKEA 2062
Cdd:COG4913 629 AEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEELEEEL 708
|
570 580
....*....|....*....|....*..
gi 1988774676 2063 EKQIVVAQQAAQKCSAAEQQVQSVLAQ 2089
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1152-1647 |
6.12e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 65.91 E-value: 6.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1152 VKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVrvhSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRE 1231
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL---TEARTERDQFSQESGNLDDQLQKLLADLHKREKE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1232 --LEQLGRQLGYYRE-----SYDWLIRWIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKA 1304
Cdd:pfam15921 393 lsLEKEQNKRLWDRDtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLES 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1305 YIDTIKDYELQLVAYKAQVEP---LVSPLKKT--KLDSASDNIIQEYVTLRTRYsELMTLTSQYIKFITDTQRRLDDEEK 1379
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTLESserTVSDLTASlqEKERAIEATNAEITKLRSRV-DLKLQELQHLKNEGDHLRNVQTECE 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1380 AAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAI-------AKAEKEAQELKLKMQE---EVSKREIAAVDAEKQKTNIQ 1449
Cdd:pfam15921 552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAgamqvekAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARVSDLE 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1450 LELQELKNLSEQQ---IKDKSQQVDEALH----SRTKIE---EEIRLIRI-------QLETT----EKQKYTAESELKQL 1508
Cdd:pfam15921 632 LEKVKLVNAGSERlraVKDIKQERDQLLNevktSRNELNslsEDYEVLKRnfrnkseEMETTtnklKMQLKSAQSELEQT 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1509 RDRAAEAEKLRKLAQDEAEKLRKQVS------EETQKKRQAEEELKRKSEAEKEAAKQKQKALEdlEKLRMQAEEAERQV 1582
Cdd:pfam15921 712 RNTLKSMEGSDGHAMKVAMGMQKQITakrgqiDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS--QELSTVATEKNKMA 789
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774676 1583 KQAEIEKEKQIKVAHEAAQKSAAaeLQSKHMSFAEKTSKLEeslKQEhgavlqlqQEAERLKKQQ 1647
Cdd:pfam15921 790 GELEVLRSQERRLKEKVANMEVA--LDKASLQFAECQDIIQ---RQE--------QESVRLKLQH 841
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1438-1633 |
6.15e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.83 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1438 AVDAEKQKTNIQL----ELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRiqlettEKQKYTAESELKQLRDRAA 1513
Cdd:PRK09510 74 AKRAEEQRKKKEQqqaeELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAA------LKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1514 EAEKLRKLAQDEAeklrKQVSEETQKKRQAEEELKRKSEAEKEA-AKQKQKALEDLEKlrmqAEEAERQVKQAEIEKEKQ 1592
Cdd:PRK09510 148 KAEAEAKRAAAAA----KKAAAEAKKKAEAEAAKKAAAEAKKKAeAEAAAKAAAEAKK----KAEAEAKKKAAAEAKKKA 219
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1988774676 1593 IKVAHEAAQKsAAAELQSKHMSFAEKTSKLEESLKQEHGAV 1633
Cdd:PRK09510 220 AAEAKAAAAK-AAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1538-1744 |
6.42e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.83 E-value: 6.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1538 QKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEE---AERQVKQAE----IEKEKQiKVAHEAAQKSAAAelqs 1610
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKErlaAQEQKKQAEeaakQAALKQ-KQAEEAAAKAAAA---- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1611 khmsfaektSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTlaqe 1690
Cdd:PRK09510 145 ---------AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKA---- 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1988774676 1691 eaekqkeeaEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQE 1744
Cdd:PRK09510 212 ---------AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1773-2099 |
6.74e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 65.53 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1773 VAAAQQQRKQLEDELAKVRSEmdiliqlktkaEKETMSNTEKSKQLLEAEAAKMKDLAEEAS----RLRAISEEAKHQRQ 1848
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQE-----------KEEKAREVERRRKLEEAEKARQAEMDRQAAiyaeQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1849 IAEEEAARqraEAERILKEKLAAisEATRLKtEAEIALKEKEAENERLRRQAEdEAYQRKALEDQASQHKQEIEEKIVQL 1928
Cdd:pfam17380 353 IRQEERKR---ELERIRQEEIAM--EISRMR-ELERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1929 KKSSEAEMERQkaivddtlkQRRVVEEEIRilklnfekassgkldlELELNKLKNIADETQQSKIRAEEEAEKLRKLALE 2008
Cdd:pfam17380 426 RAEQEEARQRE---------VRRLEEERAR----------------EMERVRLEEQERQQQVERLRQQEEERKRKKLELE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2009 EEKRRREAEEKV-KKIAAAEEEAARQ------------------RKAALEELERLRKKAEEARKQKD-EADKEAEKQIVV 2068
Cdd:pfam17380 481 KEKRDRKRAEEQrRKILEKELEERKQamieeerkrkllekemeeRQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRK 560
|
330 340 350
....*....|....*....|....*....|.
gi 1988774676 2069 AQQAAQKCSAAEQQVQsvLAQQIEDSITQKK 2099
Cdd:pfam17380 561 ATEERSRLEAMERERE--MMRQIVESEKARA 589
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2129-2409 |
6.91e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 65.53 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2129 RQQAEEAERQKTAAEEEAANQAKaqEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKL----AEQTLKQKFQ 2204
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKA--REVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELerirQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2205 VEQELTKVKL-KLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRlikkdkdST 2283
Cdd:pfam17380 365 IRQEEIAMEIsRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR-------EV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2284 QKLLAEEAENMRKLAEDAARlsvEAQEAARLRQIAEDdlNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQ-KQKDLAQE 2362
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQE---RQQQVERLRQQEEE--RKRKKLELEKEKRDRKRAEEQRRKILEKELEErKQAMIEEE 512
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1988774676 2363 QAQKLLEDKQLMQQRLEEETEEYHKSlEVERKRQLEImaeAERLRLQ 2409
Cdd:pfam17380 513 RKRKLLEKEMEERQKAIYEEERRREA-EEERRKQQEM---EERRRIQ 555
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2230-2628 |
7.69e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2230 LQRLKDEVDDAVKQRGQ-----------VEEELFKVKVQMEELLKLKNKIEEENQRL---------IKKDKDSTQKLLA- 2288
Cdd:COG4717 48 LERLEKEADELFKPQGRkpelnlkelkeLEEELKEAEEKEEEYAELQEELEELEEELeeleaeleeLREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2289 -----EEAENMRKLAEDAARL-SVEAQEAARLRQIAE-DDLNQ-----QRALAEKMLKEKMQAIQEASRLKAEAEMLQKQ 2356
Cdd:COG4717 128 lplyqELEALEAELAELPERLeELEERLEELRELEEElEELEAelaelQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2357 KDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEE-------------- 2422
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvlglla 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2423 --------EAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKS 2494
Cdd:COG4717 288 llflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2495 KEmadaqqkkiEHEKTVLQQTFMTEKEMLLKKEKL------IEDEKKRLESQFEEEVKKAKALKDEQErqKQQMEQEKKT 2568
Cdd:COG4717 368 LE---------QEIAALLAEAGVEDEEELRAALEQaeeyqeLKEELEELEEQLEELLGELEELLEALD--EEELEEELEE 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 2569 LQAtmdaalsKQKEAEEEMLRKQKEMQELERQ--RLEQERILAEENQKLREKLQQLEDAQKD 2628
Cdd:COG4717 437 LEE-------ELEELEEELEELREELAELEAEleQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1460-1662 |
9.98e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.06 E-value: 9.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1460 EQQIKDKSQQVDEALHSRTKIEEEIRLIriqlettEKQKYTAESELKQlrdrAAEAEKLRKLAQDEAEKLRKQVSEETQK 1539
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQL-------EKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1540 KrqAEEELKRKSEAEKEAAKQKQKaLEDLEKLRMQAEEAerqvkQAEIEKEKQIKVAHEAAQKsAAAELQSKHMSFAEKT 1619
Cdd:PRK09510 148 K--AEAEAKRAAAAAKKAAAEAKK-KAEAEAAKKAAAEA-----KKKAEAEAAAKAAAEAKKK-AEAEAKKKAAAEAKKK 218
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1988774676 1620 SKLEESLKQEHGAVlQLQQEAERLKKQQEDAENSREEAEKELE 1662
Cdd:PRK09510 219 AAAEAKAAAAKAAA-EAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1391-1732 |
1.14e-09 |
|
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: 63.40 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1391 KMAEMQAELDKQKqlaeAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLEL--QELKNLSEQQIKDKSQ 1468
Cdd:pfam13868 16 LAAKCNKERDAQI----AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyrQELEEQIEEREQKRQE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1469 QVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELK 1548
Cdd:pfam13868 92 EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1549 RKSEAEKEAAKQKqkaledlEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSkhmsfAEKTSKLEESLKQ 1628
Cdd:pfam13868 172 EAEREEIEEEKER-------EIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREE-----AEKKARQRQELQQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1629 EHgavlQLQQEAERLKKQQEdaensREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAK 1708
Cdd:pfam13868 240 AR----EEQIELKERRLAEE-----AEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAER 310
|
330 340 350
....*....|....*....|....*....|.
gi 1988774676 1709 AEESALKQKEMAEEEL-------ERQRKIAE 1732
Cdd:pfam13868 311 EEELEEGERLREEEAErrerieeERQKKLKE 341
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1542-1799 |
1.45e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 63.33 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1542 QAEEELKRKSEAEKEAAKQKQKALEDLEKlrmQAEEAERQvKQAEIEKEKQIKVAHEAAQKSAAAELQSKHmsfAEKTSK 1621
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQ---QAEEAEKQ-RAAEQARQKELEQRAAAEKAAKQAEQAAKQ---AEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1622 LEESLKQEHGAVLQLQQEAERLKKQQEDAENsreeaekelekwrqkanealrlrlQAEDEAHKKTLAQEEAEKQKEEAER 1701
Cdd:TIGR02794 120 QAEEAKAKQAAEAKAKAEAEAERKAKEEAAK------------------------QAEEEAKAKAAAEAKKKAEEAKKKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1702 EAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRK 1781
Cdd:TIGR02794 176 EAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGA 255
|
250
....*....|....*...
gi 1988774676 1782 QLEDELAKVRSEMDILIQ 1799
Cdd:TIGR02794 256 AAGSEVDKYAAIIQQAIQ 273
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1143-1670 |
1.62e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1143 REVHTVPSDVKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKasavSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVF 1222
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE----LEERIEELKKEIEELEEKVKELKELKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1223 TQIDLRQRELEQLGR---QLGYYRESYDWLIRWIADAKQRQEKIqavpitdsktlkeqlaqeKKLLEEIEQNKDKVDECQ 1299
Cdd:PRK03918 297 KLSEFYEEYLDELREiekRLSRLEEEINGIEERIKELEEKEERL------------------EELKKKLKELEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1300 KYAKAYiDTIKDYELQLVAYKAQVEPLvsplkktkldsASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEK 1379
Cdd:PRK03918 359 ERHELY-EEAKAKKEELERLKKRLTGL-----------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1380 AAEKLKAEERK-KMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQE-EVSKREIAAVDAEKQKTNIQLEL-QELK 1456
Cdd:PRK03918 427 AIEELKKAKGKcPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKlRKELRELEKVLKKESELIKLKELaEQLK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1457 NLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTE---KQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQV 1533
Cdd:PRK03918 507 ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1534 SEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAER--QVKQAEIEK-EKQIKVAHEAAQKSAAAELQS 1610
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEelAETEKRLEElRKELEELEKKYSEEEYEELRE 666
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1611 KHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKeLEKWRQKANE 1670
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEE 725
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1505-1924 |
1.66e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1505 LKQLRDRAAEAEKLR----KLAQDEAEKLRKQVSEETQKK---RQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEE 1577
Cdd:COG4717 48 LERLEKEADELFKPQgrkpELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1578 AERQVKQAEIEKEKQIK-------VAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQ----EHGAVLQLQQEAERLKKQ 1646
Cdd:COG4717 128 LPLYQELEALEAELAELperleelEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1647 QEDAENSREEAEKELEkwrQKANEALRLRLQAEDEAHKKTLAQEEAEKQ------------------------------- 1695
Cdd:COG4717 208 LAELEEELEEAQEELE---ELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1696 --KEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLED-ELYRLKNE 1772
Cdd:COG4717 285 llALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1773 VAAAQQQRKQLEDElAKVRSEMDILIQLKTKAEKEtmsntEKSKQLLEAEAAkMKDLAEEASRLRAISEEAKHQRQIAEE 1852
Cdd:COG4717 365 LEELEQEIAALLAE-AGVEDEEELRAALEQAEEYQ-----ELKEELEELEEQ-LEELLGELEELLEALDEEELEEELEEL 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774676 1853 EAARQRAEAERI-LKEKLAAISEATR-LKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQA-SQHKQEIEEK 1924
Cdd:COG4717 438 EEELEELEEELEeLREELAELEAELEqLEEDGELAELLQELEELKAELRELAEEWAALKLALELlEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2193-2412 |
1.97e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2193 KLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELfkvKVQMEELLKLKNKIEEEN 2272
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2273 QRLiKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAAR----LRQIAEDDLNQQRALAEKmLKEKMQAIQEASRLKA 2348
Cdd:COG4942 97 AEL-EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRrlqyLKYLAPARREQAEELRAD-LAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774676 2349 EAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQ 2412
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1343-1799 |
2.38e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.21 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1343 IQEYVTLRTRYSELMTLTSQYIKF----ITDTQRRLDDEEKAAEKLKAEERKKMA-------EMQAELDKQK-------- 1403
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYVAAdymrHANERRVHLEEALELRRELYTSRRQLAaeqyrlvEMARELAELNeaesdleq 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1404 ------------QLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAvdaekqktNIQLELQELKNLSEQQIKD-KSQQV 1470
Cdd:PRK04863 329 dyqaasdhlnlvQTALRQQEKIERYQADLEELEERLEEQNEVVEEAD--------EQQEENEARAEAAEEEVDElKSQLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1471 D--EALhsrtkIEEEIRLIRIQletTEKQKYTAESELKQLRDRAAEAeklrklAQDEAEKLRKQVSEETQKKRQAEEELk 1548
Cdd:PRK04863 401 DyqQAL-----DVQQTRAIQYQ---QAVQALERAKQLCGLPDLTADN------AEDWLEEFQAKEQEATEELLSLEQKL- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1549 rkSEAEkEAAKQKQKALEDLEKL--RMQAEEAERQVKQAEIEKEKQikvAHEAAQKSAaaeLQSKHmsfaektSKLEESL 1626
Cdd:PRK04863 466 --SVAQ-AAHSQFEQAYQLVRKIagEVSRSEAWDVARELLRRLREQ---RHLAEQLQQ---LRMRL-------SELEQRL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1627 KQehgavlqlQQEAERLKKQQEDAENSREEAEKELekwrqkanEALRLRLQAEDEAHKktlaqeeaekqkeeaerEAKKR 1706
Cdd:PRK04863 530 RQ--------QQRAERLLAEFCKRLGKNLDDEDEL--------EQLQEELEARLESLS-----------------ESVSE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1707 AKAEESALKQKemaEEELERQRKIAESTAQQKLTAEQELIRLR----ADFDNAEQQRSLLEDELYRLKnevaAAQQQRKQ 1782
Cdd:PRK04863 577 ARERRMALRQQ---LEQLQARIQRLAARAPAWLAAQDALARLReqsgEEFEDSQDVTEYMQQLLERER----ELTVERDE 649
|
490
....*....|....*..
gi 1988774676 1783 LEDELAKVRSEMDILIQ 1799
Cdd:PRK04863 650 LAARKQALDEEIERLSQ 666
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
71-167 |
2.61e-09 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 57.58 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 71 KKTFTKWVN---------KHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDFL 136
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1988774676 137 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 167
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2464-2634 |
3.06e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2464 KEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEE 2543
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2544 EVKKAKALKdEQERQKQQMEQEKKTLQATMDAAL-SKQKEAEEEMLRKQKEMQELERQRLEQERILA---EENQKLREKL 2619
Cdd:COG4717 151 LEERLEELR-ELEEELEELEAELAELQEELEELLeQLSLATEEELQDLAEELEELQQRLAELEEELEeaqEELEELEEEL 229
|
170
....*....|....*
gi 1988774676 2620 QQLEDAQKDQHTRET 2634
Cdd:COG4717 230 EQLENELEAAALEER 244
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1402-1609 |
3.28e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 62.17 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1402 QKQLAEAHAKAIAKAEKEAqelKLKMQEEVSKREIAAVDAEKQKtniQLELQELKNLSEQQIKDKSqqvdealhsrTKIE 1481
Cdd:TIGR02794 44 DPGAVAQQANRIQQQKKPA---AKKEQERQKKLEQQAEEAEKQR---AAEQARQKELEQRAAAEKA----------AKQA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1482 EEIRLiriqlETTEKQKYTAESELKQLRDRAAEAEKLRKlaQDEAEKLRKQVSEETQKKRQAE-----EELKRKSEAEKE 1556
Cdd:TIGR02794 108 EQAAK-----QAEEKQKQAEEAKAKQAAEAKAKAEAEAE--RKAKEEAAKQAEEEAKAKAAAEakkkaEEAKKKAEAEAK 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774676 1557 A---AKQKQKALEDLEKLRMQAEEAERQVKqAEIEKEKQIKVAHEAAQKSAAAELQ 1609
Cdd:TIGR02794 181 AkaeAEAKAKAEEAKAKAEAAKAKAAAEAA-AKAEAEAAAAAAAEAERKADEAELG 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1024-1598 |
3.53e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1024 LRIEDCE--AGTVARIRKPV--EKEPLKEYIQKTTEQKKVQGELdglKKDLDKVSVKTQEVlaspqpSASAPVLRSELDl 1099
Cdd:PRK03918 155 LGLDDYEnaYKNLGEVIKEIkrRIERLEKFIKRTENIEELIKEK---EKELEEVLREINEI------SSELPELREELE- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1100 tvqkmdhahMLSSVYLEKLKTVEMVirntqgaEGVLKQYEDCLREVHTVPSDVKEVETYRAKLKKMRTEAEDEQPVFDSL 1179
Cdd:PRK03918 225 ---------KLEKEVKELEELKEEI-------EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1180 EEELKKASAVS---DKMVRVHSERDVELDHFRQQLSSLQDRWKavftqidlrqrELEQLGRQLGYYRESYDWLIRWIADA 1256
Cdd:PRK03918 289 KEKAEEYIKLSefyEEYLDELREIEKRLSRLEEEINGIEERIK-----------ELEEKEERLEELKKKLKELEKRLEEL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1257 KQRQEKIQavpitDSKTLKEQLAQEKKLLEEIEqnKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKKT--K 1334
Cdd:PRK03918 358 EERHELYE-----EAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1335 LDSASDNII--------QEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEER-----KKMAEMQAELdk 1401
Cdd:PRK03918 431 LKKAKGKCPvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklKELAEQLKEL-- 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1402 QKQLAEAHAKAIAKAEKEAQELK-----LKMQEEVSKREIAAVDA-EKQKTNIQLELQEL-KNLSE--QQIKDKSQQVDE 1472
Cdd:PRK03918 509 EEKLKKYNLEELEKKAEEYEKLKeklikLKGEIKSLKKELEKLEElKKKLAELEKKLDELeEELAEllKELEELGFESVE 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1473 ALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEetQKKRQAEEELKRKSE 1552
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE--LEKKYSEEEYEELRE 666
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1988774676 1553 AEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHE 1598
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1819-2629 |
3.67e-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: 63.55 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1819 LEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEaaRQRAEAERILKEKLAAIsEATRLKTEAEIALKEK---EAENER 1895
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREY-EGYELLKEKEALERQKeaiERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1896 LRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLE 1975
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1976 LELNKLKniaDETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRkaalEELERLRKKAEEARKQK 2055
Cdd:TIGR02169 329 AEIDKLL---AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR----DELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2056 DEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEyekakklakeaeaakekaereaalLRQQAEEA 2135
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE------------------------IKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2136 ERQKTAAEEEAANQAKAQEDAERLRKEaefeaakraqaeaaaLMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLK 2215
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKE---------------LSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2216 LDETDKQKSVLDEELQ---------RLKDEV--DDAVKQRGQveEELFKVKVQMEELLKLkNKIEEENQRLIKKDKDSTQ 2284
Cdd:TIGR02169 523 VHGTVAQLGSVGERYAtaievaagnRLNNVVveDDAVAKEAI--ELLKRRKAGRATFLPL-NKMRDERRDLSILSEDGVI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2285 KLLAEEAENMRKLAEDAA-----RLSVEAQEAA-------RLRQIAEDDLNQQRALAEKMLKEKmQAIQEASRLKAEAEM 2352
Cdd:TIGR02169 600 GFAVDLVEFDPKYEPAFKyvfgdTLVVEDIEAArrlmgkyRMVTLEGELFEKSGAMTGGSRAPR-GGILFSRSEPAELQR 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2353 LQKQKdlaqEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLrlqvsqlseaqaraeeeakkfKKQAD 2432
Cdd:TIGR02169 679 LRERL----EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL---------------------EQEEE 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2433 KVATRLheteiatQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQnksKEMADAQQKKIEHEKTVL 2512
Cdd:TIGR02169 734 KLKERL-------EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHSRIPEIQAELSKL 803
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2513 qqtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVkkAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQK 2592
Cdd:TIGR02169 804 ------EEEVSRIEARLREIEQKLNRLTLEKEY--LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
810 820 830
....*....|....*....|....*....|....*..
gi 1988774676 2593 EMQELERQRLEqeriLAEENQKLREKLQQLEDAQKDQ 2629
Cdd:TIGR02169 876 ALRDLESRLGD----LKKERDELEAQLRELERKIEEL 908
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1136-1663 |
3.87e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 63.45 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1136 KQYEDCLREVHTVPSDVKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQ 1215
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1216 -------------DRWKAVFTQIDLRQRELEQLGRQLGYYRESYDWLIRWIAD--AKQRQEKIQAVPITD---SKTLKEQ 1277
Cdd:TIGR00618 380 hihtlqqqkttltQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQqeLQQRYAELCAAAITCtaqCEKLEKI 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1278 LAQE--KKLLEEIEQNKDKVDECQKYAKayIDTIKDYELQLVA-------------YKAQVEPLVSPLKKTKLDSASDNI 1342
Cdd:TIGR00618 460 HLQEsaQSLKEREQQLQTKEQIHLQETR--KKAVVLARLLELQeepcplcgscihpNPARQDIDNPGPLTRRMQRGEQTY 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1343 IQEYVTLRTRYSELMTLTSQyIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQE 1422
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHA 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1423 LKLKMQEEVSKREIAAVDAEKQKTNIQLEL---QELKNLSEQQIKDKSqqvdealhSRTKIEEEIRLIRIQLETTEkqky 1499
Cdd:TIGR00618 617 LLRKLQPEQDLQDVRLHLQQCSQELALKLTalhALQLTLTQERVREHA--------LSIRVLPKELLASRQLALQK---- 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1500 tAESELKQLRDRAAEAEKLRKLAQDEAEKLrKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAE 1579
Cdd:TIGR00618 685 -MQSEKEQLTYWKEMLAQCQTLLRELETHI-EEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1580 RQVKQAEI-------EKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAEN 1652
Cdd:TIGR00618 763 HFNNNEEVtaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSA 842
|
570
....*....|.
gi 1988774676 1653 SREEAEKELEK 1663
Cdd:TIGR00618 843 TLGEITHQLLK 853
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2401-2614 |
5.20e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2401 AEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIAtqekmtvVERLEFERLNTSKEADDLRKAIADLENEK 2480
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR-------IAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2481 ARLKKEAEELQNKSKEMADAQQKKIEHEKTVL----------------QQTFMTEKEMLLKKEKLIEDEKKRLESQFEEE 2544
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2545 VKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQK 2614
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4413-4451 |
5.24e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 54.26 E-value: 5.24e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1988774676 4413 FLEVQYLTGGLIEPDVEGRVSIDESIRKGTIDARTAQKL 4451
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1654-2413 |
5.61e-09 |
|
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: 62.83 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1654 REEAEKELEKWRQKANEaLRLRLQAEDEAHKK-------TLAQEEAEKQKEEAEREA-----KKRAKAEESALKQKEMAE 1721
Cdd:pfam15921 73 KEHIERVLEEYSHQVKD-LQRRLNESNELHEKqkfylrqSVIDLQTKLQEMQMERDAmadirRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1722 EELERQRKIAESTAQQKLT--------------AEQELIRLRADFDNAEQQRSLLEDELYRL--KNEVAAAQQQRKQLED 1785
Cdd:pfam15921 152 HELEAAKCLKEDMLEDSNTqieqlrkmmlshegVLQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1786 ELAKVRSEM----DILIQLKTKAEKET----MSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQ 1857
Cdd:pfam15921 232 EISYLKGRIfpveDQLEALKSESQNKIelllQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1858 RAEAERILKEKLAAISEatrLKTEAEIALKEKEAENERLRRQ---AEDEAYQRKALEDQASQHKQEIEEKIvqlkkssea 1934
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQ---LRSELREAKRMYEDKIEELEKQlvlANSELTEARTERDQFSQESGNLDDQL--------- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1935 emerQKAIVDdtLKQRrvvEEEirilklnfekassgkLDLELELNklKNIADETQQSKIRAEEEAEKLrklaleeekrrr 2014
Cdd:pfam15921 380 ----QKLLAD--LHKR---EKE---------------LSLEKEQN--KRLWDRDTGNSITIDHLRREL------------ 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2015 eaeekvkkiaaaeeeaaRQRKAALEELERLRKkaeearKQKDEADKEAEKQIVVAQ---QAAQKCSAAEQQVQSV--LAQ 2089
Cdd:pfam15921 422 -----------------DDRNMEVQRLEALLK------AMKSECQGQMERQMAAIQgknESLEKVSSLTAQLESTkeMLR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2090 QIEDSITQKKLKEEyekakKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRK-EAEFEAA 2168
Cdd:pfam15921 479 KVVEELTAKKMTLE-----SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvQTECEAL 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2169 KRAQAEAAALMQ--KQQADTEM---AKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDavkq 2243
Cdd:pfam15921 554 KLQMAEKDKVIEilRQQIENMTqlvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD---- 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2244 rgqVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKL--LAEEAENM-RKLAEDAARLSVEAQEAARLRQIAED 2320
Cdd:pfam15921 630 ---LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLkRNFRNKSEEMETTTNKLKMQLKSAQS 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2321 DLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLE---DKQLMQQRLEEETEEYHKSLEVERKRQL 2397
Cdd:pfam15921 707 ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEamtNANKEKHFLKEEKNKLSQELSTVATEKN 786
|
810
....*....|....*.
gi 1988774676 2398 EIMAEAERLRLQVSQL 2413
Cdd:pfam15921 787 KMAGELEVLRSQERRL 802
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
184-286 |
7.31e-09 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 56.71 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 184 QSEDMTAKEKLLLWSQ-RMTDgyqgIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLG 261
Cdd:cd21315 11 DGKGPTPKQRLLGWIQsKVPD----LPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDaVKNAKEAMDLAEDWLD 86
|
90 100
....*....|....*....|....*
gi 1988774676 262 VTRLLDPEDVDVPHPDEKSIITYVS 286
Cdd:cd21315 87 VPQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1450-1851 |
8.28e-09 |
|
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: 61.90 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1450 LELQELKNLSEQQIKDKSQQVDealhSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAqDEAEKL 1529
Cdd:COG5185 184 LTLGLLKGISELKKAEPSGTVN----SIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTS-DKLEKL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1530 RKQVSE-ETQKKRQAEEELKRKSEAEKEAAKQ----KQKALEDLEKLRMQA--EEAERQVKQAEIEKEKQIKVAH-EAAQ 1601
Cdd:COG5185 259 VEQNTDlRLEKLGENAESSKRLNENANNLIKQfentKEKIAEYTKSIDIKKatESLEEQLAAAEAEQELEESKREtETGI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1602 KSAAAELQSKHMSFAEKTSKLEESLKQEHGAVL--QLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAE 1679
Cdd:COG5185 339 QNLTAEIEQGQESLTENLEAIKEEIENIVGEVElsKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAA 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1680 DEAHKKtlaqeeaekqkeeAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELI--RLRADFDNAEQ 1757
Cdd:COG5185 419 DRQIEE-------------LQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEInrSVRSKKEDLNE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1758 QRSLLEDELYRLKNEVaaaQQQRKQLEDELAKVRSEMDILIQLKTKAEKETmsNTEKSKQLLEAEAAKMKDLAEEASRLR 1837
Cdd:COG5185 486 ELTQIESRVSTLKATL---EKLRAKLERQLEGVRSKLDQVAESLKDFMRAR--GYAHILALENLIPASELIQASNAKTDG 560
|
410
....*....|....
gi 1988774676 1838 AISEEAKHQRQIAE 1851
Cdd:COG5185 561 QAANLRTAVIDELT 574
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
72-166 |
8.51e-09 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 56.19 E-value: 8.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 72 KTFTKWVNKHLIKA--QRHVTDLYEDLRDGHNLISLLEVLSGETL------PREKGRMrfhkLQNVQIALDFLRHRQVKL 143
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1988774676 144 VNIRNDDIADGNPKLTLGLIWTI 166
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1509-1734 |
8.84e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 61.43 E-value: 8.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1509 RDRAAEAEKLRKLAQDEAEKLrKQVSEETQKKRQAEEELKRKSE------AEKEAAKQKQKALEDLEKLRMQAEeAERQV 1582
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERE-TEIAIAQANREAEEAELEQEREietariAEAEAELAKKKAEERREAETARAE-AEAAY 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1583 KQAEIEKEKQIKVAHEAAQKSAAAELQSKhmsfaektsKLEESLKQEHgAVLQLQQEAERLKKQQEdaensrEEAEKEle 1662
Cdd:COG2268 269 EIAEANAEREVQRQLEIAEREREIELQEK---------EAEREEAELE-ADVRKPAEAEKQAAEAE------AEAEAE-- 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 1663 kwrqkaneALRLRLQAEDEAHKKtlaqeeaekqKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAEST 1734
Cdd:COG2268 331 --------AIRAKGLAEAEGKRA----------LAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1448-1808 |
9.51e-09 |
|
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: 61.45 E-value: 9.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1448 IQLELQElknlSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETT----EKQKYTAESELKQLRDRAAEAEKLRKLAQ 1523
Cdd:pfam07888 32 LQNRLEE----CLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1524 DEAEKLRKqvsEETQKKRQAEEELKRKSEAEKEAAKQKQKALE---DLEKLRMQAEEAERQVKQAEIEKEK-QIKV-AHE 1598
Cdd:pfam07888 108 ASSEELSE---EKDALLAQRAAHEARIRELEEDIKTLTQRVLEretELERMKERAKKAGAQRKEEEAERKQlQAKLqQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1599 AAQKSAAAELQSKHMSFAEKTSKLEE------SLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAL 1672
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQlqdtitTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1673 RLRLQAEDEAHKKTLAQEEAEKQKEEAE---REAKKRAKAEESALKQKEMAE--------EELERQRKIAESTAQQKLTA 1741
Cdd:pfam07888 265 AQRDRTQAELHQARLQAAQLTLQLADASlalREGRARWAQERETLQQSAEADkdrieklsAELQRLEERLQEERMEREKL 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774676 1742 EQELIRLRadfDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVrseMDILIQLKTKAEKET 1808
Cdd:pfam07888 345 EVELGREK---DCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL---LEYIRQLEQRLETVA 405
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1622-1945 |
1.01e-08 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 60.85 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1622 LEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEahKKTLAQEEAEKQKEEAER 1701
Cdd:pfam19220 25 LKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGE--LEELVARLAKLEAALREA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1702 EAKKRAKAeeSALKQKEMAEEELERQRKIAestAQQKLTAEQELIRLRADFDNAEQQRSLLEDELyrlknevAAAQQQRK 1781
Cdd:pfam19220 103 EAAKEELR--IELRDKTAQAEALERQLAAE---TEQNRALEEENKALREEAQAAEKALQRAEGEL-------ATARERLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1782 QLEDELAKVRSEMDiliqlktKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLraISEEAKHQRQIAEEEAARQRAEA 1861
Cdd:pfam19220 171 LLEQENRRLQALSE-------EQAAELAELTRRLAELETQLDATRARLRALEGQL--AAEQAERERAEAQLEEAVEAHRA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1862 ERI-LKEKLAAIS---EAT-RLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKksseaEM 1936
Cdd:pfam19220 242 ERAsLRMKLEALTaraAATeQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQ-----EM 316
|
....*....
gi 1988774676 1937 ERQKAIVDD 1945
Cdd:pfam19220 317 QRARAELEE 325
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2278-2617 |
1.16e-08 |
|
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: 60.32 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2278 KDKDSTQKLLAEEAENMRKLAEdAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQK 2357
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMME-EERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2358 DLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQvsqlseaqaraeeeakKFKKQADKVATR 2437
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE----------------YLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2438 LHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADL---ENEKARLKKEAEELQNKSKEMADAQQkkiehektVLQQ 2514
Cdd:pfam13868 172 EAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLyqeEQERKERQKEREEAEKKARQRQELQQ--------AREE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2515 TFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKAlkdEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEM 2594
Cdd:pfam13868 244 QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQE---EAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERL 320
|
330 340
....*....|....*....|...
gi 1988774676 2595 QELERQRleQERILAEENQKLRE 2617
Cdd:pfam13868 321 REEEAER--RERIEEERQKKLKE 341
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1389-1559 |
1.17e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 61.33 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1389 RKKMAEMQAELDKQKQLAEAHAKAIAK-----AEKEAQELKLKMQEEVSKREiaavdaekqktniqLELQELknlsEQQI 1463
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKealleAKEEIHKLRNEFEKELRERR--------------NELQKL----EKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1464 KDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRA-AEAEKLRKLAQDEA-EKLRKQVSEETQKKR 1541
Cdd:PRK12704 92 LQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQlQELERISGLTAEEAkEILLEKVEEEARHEA 171
|
170 180
....*....|....*....|.
gi 1988774676 1542 QA---EEELKRKSEAEKEAAK 1559
Cdd:PRK12704 172 AVlikEIEEEAKEEADKKAKE 192
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2274-2640 |
1.21e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2274 RLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRqiaeDDLNQQRALAEKMLKEKmqaiQEASRLKAEAEML 2353
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEIS----SELPELREELEKLEKEV----KELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2354 QKQKDLAQEQAQKLLEDKQLMQQRLEEeTEEYHKSLEVERKRQLEIMAEAERLRlqvsqlseaqaraeeEAKKFKKQADK 2433
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEE-LKKEIEELEEKVKELKELKEKAEEYI---------------KLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2434 VATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAE----------ELQNKSKEMADAQQK 2503
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHElyeeakakkeELERLKKRLTGLTPE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2504 KIEHEKTVLQqtfmTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQER----QKQQMEQEKKTLQATMDAALSK 2579
Cdd:PRK03918 388 KLEKELEELE----KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEYTAELKR 463
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2580 ----QKEAEEEMLRKQKEMQELERQRLEQERI-----LAEENQKLREKLQQLEDAQKDQHTRETDKVLHK 2640
Cdd:PRK03918 464 iekeLKEIEEKERKLRKELRELEKVLKKESELiklkeLAEQLKELEEKLKKYNLEELEKKAEEYEKLKEK 533
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2130-2586 |
1.22e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2130 QQAEEAERQKTAAEEEAANQAKAQEDAERLRKE-AEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQE 2208
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEElEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2209 LTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRG-QVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLl 2287
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2288 aEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQ--EQAQ 2365
Cdd:COG4717 230 -EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKeaEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2366 KLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSeaqaraeeeakKFKKQADKVATRLHETEIAT 2445
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE-----------ELEEELQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2446 QEKMTVVERLEfERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEmaDAQQKKIEHEKTVLQQTfMTEKEMLLK 2525
Cdd:COG4717 378 EAGVEDEEELR-AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEEL-EEELEELRE 453
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774676 2526 KEKLIEDEKKRLESqfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEE 2586
Cdd:COG4717 454 ELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1481-1950 |
1.29e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.89 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1481 EEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAeklrKLAQDEAEKLRKQVS---EET--QKKRQAEEELKRKSEAEK 1555
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQL----KEQLQLLNKLLPQANllaDETlaDRLEELREELDAAQEAQA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1556 EAAkQKQKALEDLEK----LR---MQAEEAERQVKQAEiEKEKQIKvaheaAQKSAAAEL--QSKHMSFAEKTSKLEESl 1626
Cdd:COG3096 911 FIQ-QHGKALAQLEPlvavLQsdpEQFEQLQADYLQAK-EQQRRLK-----QQIFALSEVvqRRPHFSYEDAVGLLGEN- 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1627 kqehgavlqlQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRlRLQAEDEAHkktlaqeeaekqkeeaereakkR 1706
Cdd:COG3096 983 ----------SDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQ-VLASLKSSR----------------------D 1029
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1707 AKAEESALKQKEMAEeelerqrkiaestaqqkltaeqelIRLRADfDNAEQQRSLLEDELYrlkNEVAAAQQQRKQLEDE 1786
Cdd:COG3096 1030 AKQQTLQELEQELEE------------------------LGVQAD-AEAEERARIRRDELH---EELSQNRSRRSQLEKQ 1081
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1787 LAKVRSEMDILIQLKTKAEKETMSNTEkskqllEAEAAKmkdlaEEASRLRAISEEAKHQRQIAEEEAARQRAeaerilk 1866
Cdd:COG3096 1082 LTRCEAEMDSLQKRLRKAERDYKQERE------QVVQAK-----AGWCAVLRLARDNDVERRLHRRELAYLSA------- 1143
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1867 EKLAAISEatrlktEAEIALKEKEAENERLR---RQAEDEAY-QRK-ALEDQASQHKQE-IEEKIVQLKKSSEA--EMER 1938
Cdd:COG3096 1144 DELRSMSD------KALGALRLAVADNEHLRdalRLSEDPRRpERKvQFYIAVYQHLRErIRQDIIRTDDPVEAieQMEI 1217
|
490
....*....|..
gi 1988774676 1939 QKAIVDDTLKQR 1950
Cdd:COG3096 1218 ELARLTEELTSR 1229
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1538-1807 |
1.34e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.51 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1538 QKKRQAEEELKRKSEAE---KEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEK-EKQIKVAHEAAQKSAaaelqsKHM 1613
Cdd:PRK04863 844 RRRVELERALADHESQEqqqRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEiREQLDEAEEAKRFVQ------QHG 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1614 SFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAEN---------------SREEAEKELEKwRQKANEALRLRL-Q 1677
Cdd:PRK04863 918 NALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafaltevvqrrahfSYEDAAEMLAK-NSDLNEKLRQRLeQ 996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1678 AEDEAhkktlaqeeaekqkeeaeREAKKRAKAEESALKQKEMAEEELerqrKIAESTAQQKLT-AEQEL--IRLRADFdN 1754
Cdd:PRK04863 997 AEQER------------------TRAREQLRQAQAQLAQYNQVLASL----KSSYDAKRQMLQeLKQELqdLGVPADS-G 1053
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 1755 AEQQRSLLEDELYrlkNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKE 1807
Cdd:PRK04863 1054 AEERARARRDELH---ARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1535-1982 |
1.65e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 61.22 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1535 EETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEklrmqaeeaERQVKQAEIEKEKQI-----KVAHEAAQKSAAAELQ 1609
Cdd:PRK10929 24 DEKQITQELEQAKAAKTPAQAEIVEALQSALNWLE---------ERKGSLERAKQYQQVidnfpKLSAELRQQLNNERDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1610 SKHMSFAEKTSKLEESLKQEHGAVL----QLQQEAER----------LKKQQEDAENSREEAEKELE---KWRQKANEAL 1672
Cdd:PRK10929 95 PRSVPPNMSTDALEQEILQVSSQLLeksrQAQQEQDRareisdslsqLPQQQTEARRQLNEIERRLQtlgTPNTPLAQAQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1673 RLRLQAEDEAHKKTLaqeeaekqkeeaereakkrakaeesalkqkemaeEELErqrkiaesTAQQKLTAEQELIRLRAdf 1752
Cdd:PRK10929 175 LTALQAESAALKALV----------------------------------DELE--------LAQLSANNRQELARLRS-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1753 dnaeqqrslledELYrlknevaaaQQQRKQLEDELAKVRSemdiliQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEE 1832
Cdd:PRK10929 211 ------------ELA---------KKRSQQLDAYLQALRN------QLNSQRQREAERALESTELLAEQSGDLPKSIVAQ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1833 ASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAaiseatrLKTEAEIA--LKEKEAENERLRRQAEDEAYQRKAl 1910
Cdd:PRK10929 264 FKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQA-------LNTLREQSqwLGVSNALGEALRAQVARLPEMPKP- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1911 edqasqhkQEIEEKIVQLKKSS---EAEMERQ----KAIVDD----TLKQRRVVEEEIRILKLNFEKASSGKLDLELELN 1979
Cdd:PRK10929 336 --------QQLDTEMAQLRVQRlryEDLLNKQpqlrQIRQADgqplTAEQNRILDAQLRTQRELLNSLLSGGDTLILELT 407
|
...
gi 1988774676 1980 KLK 1982
Cdd:PRK10929 408 KLK 410
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
70-169 |
1.92e-08 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 55.20 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 70 QKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKG-----RMRFHKLQNVQIALDFLRHRQVKLV 144
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 1988774676 145 NIRNDDIADGNPKLTLGLIWTIILH 169
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
189-291 |
2.67e-08 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 55.08 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 189 TAKEKLLLWSQRMTdgyQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLGVTRLLD 267
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQpVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 1988774676 268 PEDVDVPHPDEKSIITYVSSLYDA 291
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1881-2517 |
2.80e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.44 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1881 EAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQH---KQEIEEKIVQLKKSSE--AEMERQKAIVDDTLKQRRVVEE 1955
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHeerREELETLEAEIEDLREtiAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1956 EIR------ILKLNFEKASSGKL-----DLELELNKLKNIADETQQSKIRAEEEAEKLRklaleeekrrreaeekvkkia 2024
Cdd:PRK02224 290 ELEeerddlLAEAGLDDADAEAVearreELEDRDEELRDRLEECRVAAQAHNEEAESLR--------------------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2025 aaeeeaarqrkaalEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSvLAQQIEDSITQKKLKEEY 2104
Cdd:PRK02224 349 --------------EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE-LRERFGDAPVDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2105 ekakklakeaeaakekaereAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRaqaeaaalmqkqqa 2184
Cdd:PRK02224 414 --------------------LEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQ-------------- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2185 DTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDEtdkqksvLDEELQRLKdevdDAVKQRGQVEEELFKVKVQMEELLKL 2264
Cdd:PRK02224 460 PVEGSPHVETIEEDRERVEELEAELEDLEEEVEE-------VEERLERAE----DLVEAEDRIERLEERREDLEELIAER 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2265 KNKIEEENQRLIKKDKDSTQklLAEEAENMRKLAEDAARLSVEAQEAArlrqiaeDDLNQQRAlaekMLKEKMQAIQEAS 2344
Cdd:PRK02224 529 RETIEEKRERAEELRERAAE--LEAEAEEKREAAAEAEEEAEEAREEV-------AELNSKLA----ELKERIESLERIR 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2345 RLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETeeyhkslevERKRQLEIMAEAERLrlqvsqlsEAQARAEEEA 2424
Cdd:PRK02224 596 TLLAAIADAEDEIERLREKREALAELNDERRERLAEKR---------ERKRELEAEFDEARI--------EEAREDKERA 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2425 KKFKKQADKVATRLHETEIATQEKMTVVERlEFERLntskeaDDLRKAIADLENEKARLK---KEAEELQNKSKEM-ADA 2500
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDLQAEIGAVEN-ELEEL------EELRERREALENRVEALEalyDEAEELESMYGDLrAEL 731
|
650
....*....|....*..
gi 1988774676 2501 QQKKIEHEKTVLQQTFM 2517
Cdd:PRK02224 732 RQRNVETLERMLNETFD 748
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1038-1940 |
2.95e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 60.45 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1038 RKPVEKEPLKEYIQKTTEQKKVQGELDGLKKDLDKVSVKTQEvlaspqpsasapvLRSELDLTVQKMDHAHMlssvylEK 1117
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEK-------------DNSELELKMEKVFQGTD------EQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1118 LKTVEmvirNTQGAEGVLKQYE--DCLREVHTVPSDVKEvetyrakLKKMRTEAEDEQPVFdSLEEELKKASAVSDKMVR 1195
Cdd:TIGR00606 303 LNDLY----HNHQRTVREKERElvDCQRELEKLNKERRL-------LNQEKTELLVEQGRL-QLQADRHQEHIRARDSLI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1196 VHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQLGRQLGYYRESYDWLIRWIADAKQRQEKIQAVPITDSKTLK 1275
Cdd:TIGR00606 371 QSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1276 EQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDyeLQLVAYKAQVEPLVSPLKKTKLDSAsdNIIQEYVTLRTRYSE 1355
Cdd:TIGR00606 451 KKQEELKFVIKELQQLEGSSDRILELDQELRKAERE--LSKAEKNSLTETLKKEVKSLQNEKA--DLDRKLRKLDQEMEQ 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1356 LMTLTSQYIKFITDTQRRLDDEEKaAEKLKAEERKKMAEMQAELDKQKQLAEAHAKaIAKAEKEAQELKLKMQEEVSKRE 1435
Cdd:TIGR00606 527 LNHHTTTRTQMEMLTKDKMDKDEQ-IRKIKSRHSDELTSLLGYFPNKKQLEDWLHS-KSKEINQTRDRLAKLNKELASLE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1436 IAAVDAEKQKTniQLELQELKnLSEQQIKDKSQQVDEALHSRTKieEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEA 1515
Cdd:TIGR00606 605 QNKNHINNELE--SKEEQLSS-YEDKLFDVCGSQDEESDLERLK--EEIEKSSKQRAMLAGATAVYSQFITQLTDENQSC 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1516 EKL-RKLAQDEAEkLRKQVSEETQKKRQAEEELKrksEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIK 1594
Cdd:TIGR00606 680 CPVcQRVFQTEAE-LQEFISDLQSKLRLAPDKLK---STESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1595 VAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQ--QEDAENSREEAEKELEKWRQKANEal 1672
Cdd:TIGR00606 756 VNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKiaQQAAKLQGSDLDRTVQQVNQEKQE-- 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1673 rlrlqaEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADF 1752
Cdd:TIGR00606 834 ------KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1753 DNAEQ-QRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMK-DLA 1830
Cdd:TIGR00606 908 KEQDSpLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNaQLE 987
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1831 EEASRLRAISEEAKHQRQIAEEEAARqraeaERILKEKLaaiseaTRLKTEAEIalkekeAENERLRRQAEDEAYQRKAL 1910
Cdd:TIGR00606 988 ECEKHQEKINEDMRLMRQDIDTQKIQ-----ERWLQDNL------TLRKRENEL------KEVEEELKQHLKEMGQMQVL 1050
|
890 900 910
....*....|....*....|....*....|
gi 1988774676 1911 edQASQHKQEIEEKIVQLKKSSEAEMERQK 1940
Cdd:TIGR00606 1051 --QMKQEHQKLEENIDLIKRNHVLALGRQK 1078
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1372-1739 |
3.04e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1372 RRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQ---------ELKLKMQEEVSK-REIAAVDA 1441
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElaelperleELEERLEELRELeEELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1442 EKQKTNIQLE--LQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQ--KYTAESELKQLRDRAAEAE- 1516
Cdd:COG4717 171 ELAELQEELEelLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEleQLENELEAAALEERLKEARl 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1517 --------------------------------------------KLRKLAQDEAEKLRKQVSEETQKKRQAEEELKR--- 1549
Cdd:COG4717 251 llliaaallallglggsllsliltiagvlflvlgllallflllaREKASLGKEAEELQALPALEELEEEELEELLAAlgl 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1550 KSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQK----SAAAELQSKHMSFAEKTSKLEES 1625
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDeeelRAALEQAEEYQELKEELEELEEQ 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1626 LKQEHGAVLQL--QQEAERLKKQQEDAENSREEAEKELEKWRQKanealrlrlQAEDEAHKKTLAQEEAEKQKEEAEREA 1703
Cdd:COG4717 411 LEELLGELEELleALDEEELEEELEELEEELEELEEELEELREE---------LAELEAELEQLEEDGELAELLQELEEL 481
|
410 420 430
....*....|....*....|....*....|....*.
gi 1988774676 1704 KKRAKAEESALKQKEMAEEELERQRKIAESTAQQKL 1739
Cdd:COG4717 482 KAELRELAEEWAALKLALELLEEAREEYREERLPPV 517
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1784-2407 |
3.05e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1784 EDELAKVRSEmdilIQLKTKAEKETMSNTEKSKQLLEAeaaKMKDLAEEASRLRAISEEakhqrqiaEEEAARQRAEAER 1863
Cdd:PRK03918 164 YKNLGEVIKE----IKRRIERLEKFIKRTENIEELIKE---KEKELEEVLREINEISSE--------LPELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1864 ILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEdqasqhkqEIEEKIVQLK--KSSEAEMERQKA 1941
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE--------ELEEKVKELKelKEKAEEYIKLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1942 IVDDTLKQRRVVE-------EEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRR 2014
Cdd:PRK03918 301 FYEEYLDELREIEkrlsrleEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2015 EAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKdeadKEAEKQIVVAQQAAQKCsaaeqqvqSVLAQQIEDS 2094
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI----KELKKAIEELKKAKGKC--------PVCGRELTEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2095 iTQKKLKEEYEKAKKLAKEAEaakekaereaallrQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAE 2174
Cdd:PRK03918 449 -HRKELLEEYTAELKRIEKEL--------------KEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2175 AAALMQKQQADTEMAKHKKLA----------EQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQR 2244
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLiklkgeikslKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2245 GQVEEELFKvkvqmeELLKLKNkieeenqrlIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQ 2324
Cdd:PRK03918 594 LKELEPFYN------EYLELKD---------AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2325 QRalAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKqlmqqrleEETEEYHKSLEVERKrqleIMAEAE 2404
Cdd:PRK03918 659 EE--YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL--------EEREKAKKELEKLEK----ALERVE 724
|
...
gi 1988774676 2405 RLR 2407
Cdd:PRK03918 725 ELR 727
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1391-1570 |
3.08e-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: 57.63 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1391 KMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELklkmQEEVSKREIAAVDAEKQKTNIQLELQELknlsEQQIKDKSQQV 1470
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAAL----EARLEAAKTELEDLEKEIKRLELEIEEV----EARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1471 DEALHSRtkieeEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRK 1550
Cdd:COG1579 83 GNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170 180
....*....|....*....|
gi 1988774676 1551 seaEKEAAKQKQKALEDLEK 1570
Cdd:COG1579 158 ---LEELEAEREELAAKIPP 174
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1377-1589 |
3.14e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 59.09 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1377 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAvdAEKQKtniqleLQELK 1456
Cdd:TIGR02794 78 EEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAE--AERKA------KEEAA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1457 NLSEQQIKDKSQQvdealhsrtkieeeirliriqlettEKQKYTAESELKQLRDRAAEAEKLRKLAQDE----AEKLRKQ 1532
Cdd:TIGR02794 150 KQAEEEAKAKAAA-------------------------EAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakakAEAAKAK 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774676 1533 VSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDL--EKLRMQAEEAERQVKQAEIEK 1589
Cdd:TIGR02794 205 AAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLasGSNAEKQGGARGAAAGSEVDK 263
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1378-1610 |
3.43e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 59.09 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1378 EKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREiaavdAEKQKTNIQLELQELKN 1457
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1458 LSEQQIKDKSQQvDEALHSRTKIEEEIRliriQLETTEKQKYTAESELKqlrdrAAEAEKlrklaQDEAEKLRKqvsEET 1537
Cdd:TIGR02794 124 AKAKQAAEAKAK-AEAEAERKAKEEAAK----QAEEEAKAKAAAEAKKK-----AEEAKK-----KAEAEAKAK---AEA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774676 1538 QKKRQAeEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEI------EKEKQIKVAHEAAQKSAAAELQS 1610
Cdd:TIGR02794 186 EAKAKA-EEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELgdifglASGSNAEKQGGARGAAAGSEVDK 263
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2227-2631 |
4.73e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 59.45 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2227 DEELQRLKDEVDDAVKqrgqveeELFKVKVQMEELlklKNKIEEENQRLIKKDkDSTQKLLAeeaenMRKLAEDAARLSV 2306
Cdd:pfam10174 115 EENFRRLQSEHERQAK-------ELFLLRKTLEEM---ELRIETQKQTLGARD-ESIKKLLE-----MLQSKGLPKKSGE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2307 EAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRlkaeaeMLQKQKDLAQEQA-QKLLEDKQLMQQRLEEETEEY 2385
Cdd:pfam10174 179 EDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHR------RNQLQPDPAKTKAlQTVIEMKDTKISSLERNIRDL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2386 HKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLH--ETEIATQEKMTVVERLEFERLNTS 2463
Cdd:pfam10174 253 EDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLalQTKLETLTNQNSDCKQHIEVLKES 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2464 KEADDLRKAIADLENEKARLKKEAEE--LQNKSKEMADAQQkkiehEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQF 2541
Cdd:pfam10174 333 LTAKEQRAAILQTEVDALRLRLEEKEsfLNKKTKQLQDLTE-----EKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2542 EEEVKKAKALKDEQERQK--QQMEQEKKTLQATMDAALSkQKEAEEEMLRKQKEmqELERQRLEQERILAEENQKLREKL 2619
Cdd:pfam10174 408 EQLRDKDKQLAGLKERVKslQTDSSNTDTALTTLEEALS-EKERIIERLKEQRE--REDRERLEELESLKKENKDLKEKV 484
|
410
....*....|..
gi 1988774676 2620 QQLEDAQKDQHT 2631
Cdd:pfam10174 485 SALQPELTEKES 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2362-2635 |
5.34e-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: 59.70 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2362 EQAQKLLEDKQLMQQRLEEETEEYHKSLEVERK----RQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATR 2437
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEkreyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2438 LHETEIATQEKMTVVERL-EFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEmADAQQKKIEHEKTVLQQTF 2516
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-LEAEIDKLLAEIEELEREI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2517 MTEKEMLLK-KEKLIEDEKKR--LESQFEEEVKKAKALKDEQERQKQQMEQ----------EKKTLQATMDAALSKQKEA 2583
Cdd:TIGR02169 346 EEERKRRDKlTEEYAELKEELedLRAELEEVDKEFAETRDELKDYREKLEKlkreinelkrELDRLQEELQRLSEELADL 425
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 2584 EEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETD 2635
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2266-2503 |
6.21e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2266 NKIEEENQRL--IKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEA 2343
Cdd:COG4942 20 DAAAEAEAELeqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2344 SRLKAE-AEMLQKQKDLAQEQAQKLL---EDKQLMQQRLEeeteeYHKSLEVERKRQleimaeAERLRLQVSQLSEAQAR 2419
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALLlspEDFLDAVRRLQ-----YLKYLAPARREQ------AEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2420 AEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMAD 2499
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
....
gi 1988774676 2500 AQQK 2503
Cdd:COG4942 249 AALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2452-2629 |
7.10e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2452 VERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQ-------QTFMTEKEMLl 2524
Cdd:COG3883 46 LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgsesfSDFLDRLSAL- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2525 kkEKLIEDEKKRLESQfeeevkkaKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQ 2604
Cdd:COG3883 125 --SKIADADADLLEEL--------KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
170 180
....*....|....*....|....*
gi 1988774676 2605 ERILAEENQKLREKLQQLEDAQKDQ 2629
Cdd:COG3883 195 EAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
184-291 |
7.36e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 53.56 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 184 QSEDMTAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQ-QTNLENLEQAFSVAEKDLGV 262
Cdd:cd21313 3 DAKKQTPKQRLLGWIQ---NKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDpQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1988774676 263 TRLLDPEDVDVPHPDEKSIITYVSSLYDA 291
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4061-4097 |
7.50e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.94 E-value: 7.50e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1988774676 4061 IRLLEAQIATGGIIDPEESHRLPVEVAYNRGFFDEEM 4097
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1559-1741 |
7.99e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 58.35 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1559 KQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAhEAAQKSAAAELQSKhmsfaektskleeslkQEHGAVLQLQQ 1638
Cdd:COG2268 180 EDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIA-QANREAEEAELEQE----------------REIETARIAEA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1639 EAERLKKQQE---DAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALK 1715
Cdd:COG2268 243 EAELAKKKAEerrEAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAE 322
|
170 180
....*....|....*....|....*.
gi 1988774676 1716 QKEMAEEELERQRKIAESTAQQKLTA 1741
Cdd:COG2268 323 AEAEAEAEAIRAKGLAEAEGKRALAE 348
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2368-2629 |
9.34e-08 |
|
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: 57.62 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2368 LEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLheteiatqe 2447
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ--------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2448 kmtvvERLEFERLNTSKEADDLRKAIADLENEKARLK--KEAEELQNKSKEMaDAQQKKIEHEKTVLQQTFMTEKEMLLK 2525
Cdd:pfam13868 99 -----EREQMDEIVERIQEEDQAEAEEKLEKQRQLREeiDEFNEEQAEWKEL-EKEEEREEDERILEYLKEKAEREEERE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2526 KEKL-IEDEKKRLESQFEEEVKKAKALKDEQE---------------RQKQQMEQEKK-TLQATMDAALSKQKEAEEEML 2588
Cdd:pfam13868 173 AEREeIEEEKEREIARLRAQQEKAQDEKAERDelraklyqeeqerkeRQKEREEAEKKaRQRQELQQAREEQIELKERRL 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1988774676 2589 RKQKEMQELERQRL-----EQERILAEENQKLREKLQQLEDAQKDQ 2629
Cdd:pfam13868 253 AEEAEREEEEFERMlrkqaEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1450-1608 |
9.35e-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: 56.09 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1450 LELQEL---KNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQD-- 1524
Cdd:COG1579 10 LDLQELdseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1525 EAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKL--RMQAEEAERQVKQAEIEKE-KQIKVAHEAAQ 1601
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELeaELEEKKAELDEELAELEAElEELEAEREELA 169
|
....*..
gi 1988774676 1602 KSAAAEL 1608
Cdd:COG1579 170 AKIPPEL 176
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2180-2554 |
9.38e-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: 58.49 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2180 QKQQADTEMAKHKKLAEQTLKQKF-----QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKV 2254
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEQDWNKELkselkNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2255 KVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKlaedaarlsveaqeaarlrqiaedDLNQQRALAEKMLK 2334
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK------------------------DEQIKKLQQEKELL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2335 EKmqaiqEASRLKAEAEMLQKQ-KDLAQEQAQKLLEDKQLMQQR--LEEETEEYHKSLEVER------KRQLEI-MAEAE 2404
Cdd:TIGR04523 425 EK-----EIERLKETIIKNNSEiKDLTNQDSVKELIIKNLDNTResLETQLKVLSRSINKIKqnleqkQKELKSkEKELK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2405 RLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFE--RLNTSKEADDLRKAIADLENEKAR 2482
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKS 579
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774676 2483 LKKEAEELQNKSKEMADAQQ---KKIEhEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDE 2554
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKdliKEIE-EKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1371-1568 |
1.15e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.51 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1371 QRRLDDEEKaaEKLKAEERKKMAEMQA--ELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKreiAAVDAEKQktni 1448
Cdd:PRK09510 100 QERLKQLEK--ERLAAQEQKKQAEEAAkqAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK---AAAEAKKK---- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1449 qlELQELKNLSEQQIKDKsqqvdealhsrtkieeeirliriqLETTEKQKYTAESELKQLRDRAAEAEKLRKlAQDEAEK 1528
Cdd:PRK09510 171 --AEAEAAKKAAAEAKKK------------------------AEAEAAAKAAAEAKKKAEAEAKKKAAAEAK-KKAAAEA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1988774676 1529 LRKQVSEETQKKRQAEEELKRKSeAEKEAAKQKQKALEDL 1568
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKA-AEKAAAAKAAAEVDDL 262
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1377-1737 |
1.21e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 58.04 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1377 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQL--ELQE 1454
Cdd:pfam15709 172 ERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERNLEVaaELSG 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1455 LKNLSEQQIKDKSQQVDEALHSRT-------KIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAE 1527
Cdd:pfam15709 252 PDVINSKETEDASERGAFSSDSVVedpwlssKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1528 K-LRKQVSEETQKKRQAEEELKRKSEAEKEaaKQKQKALEDLEKLRMQAEEaERQVKQAEIEKEKQiKVAHEAAQKSAAA 1606
Cdd:pfam15709 332 KaSRDRLRAERAEMRRLEVERKRREQEEQR--RLQQEQLERAEKMREELEL-EQQRRFEEIRLRKQ-RLEEERQRQEEEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1607 ELQSKHMSFAEKTSKLEEslKQEHGAVLQLQQeaerlKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEahkkt 1686
Cdd:pfam15709 408 RKQRLQLQAAQERARQQQ--EEFRRKLQELQR-----KKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEE----- 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1988774676 1687 laqeEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQ 1737
Cdd:pfam15709 476 ----RLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2227-2412 |
1.22e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2227 DEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLiKKDKDSTQKLLAEEAENMRKLAEDAARLSV 2306
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2307 EAQEAARLRQIAE--------DDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRL 2378
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190
....*....|....*....|....*....|....
gi 1988774676 2379 EEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQ 2412
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1368-1659 |
1.40e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 57.57 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1368 TDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHA---KAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQ 1444
Cdd:pfam02029 52 PSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIAdekESVAERKENNEEEENSSWEKEEKRDSRLGRYKEE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1445 KTNIQlelqeLKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQD 1524
Cdd:pfam02029 132 ETEIR-----EKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1525 EAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQvkqaEIEKEKQikvaheaAQKSA 1604
Cdd:pfam02029 207 VKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESE----EFEKLRQ-------KQQEA 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774676 1605 AAELQSKHMSFAEKTSKLEESLKQEHgavlqlQQEAERLKKQQEDAENSREEAEK 1659
Cdd:pfam02029 276 ELELEELKKKREERRKLLEEEEQRRK------QEEAERKLREEEEKRRMKEEIER 324
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1449-1785 |
1.47e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.22 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1449 QLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKlrklaqdEAEK 1528
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE-------ELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1529 LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAEL 1608
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1609 QSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLA 1688
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1689 QEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYR 1768
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330
....*....|....*..
gi 1988774676 1769 LKNEVAAAQQQRKQLED 1785
Cdd:COG4372 325 AKKLELALAILLAELAD 341
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2297-2639 |
1.83e-07 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 57.42 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2297 LAEDAARLSVEAQEAARLRQIAEDDLNQQRA-------LAEKMLKEKMQAIQEA-----------SRLKAEAEMLQKQKD 2358
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAkfkelylAKEEDLKRQNAVLQEAqveldalqnqlALARAEMENIKAVAT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2359 LAQEQAQKLLED------------KQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAER----LRLQVSQlSEAQARAEE 2422
Cdd:pfam03528 86 VSENTKQEAIDEvksqwqeevaslQAIMKETVREYEVQFHRRLEQERAQWNQYRESAEReiadLRRRLSE-GQEEENLED 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2423 EAKKFKKQADKVATRL--HETEIAT--------QEKMTVVERLEFERLNTSKEAD-----DLRKAIADLENEKARLKKEA 2487
Cdd:pfam03528 165 EMKKAQEDAEKLRSVVmpMEKEIAAlkaklteaEDKIKELEASKMKELNHYLEAEkscrtDLEMYVAVLNTQKSVLQEDA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2488 EELQNKSKEMADA-QQKKIEHekTVLQQTFMTEKEMLLKKEKLIEDEKKRLESqfeeevkkakALKDEQERQKQQmeqek 2566
Cdd:pfam03528 245 EKLRKELHEVCHLlEQERQQH--NQLKHTWQKANDQFLESQRLLMRDMQRMES----------VLTSEQLRQVEE----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2567 ktlqatmdaaLSKQKEAEEEMLRKQKEMQELERQRLEQERILA-------EENQKLREKLQQLEDAQKDQHTRETDKVLH 2639
Cdd:pfam03528 308 ----------IKKKDQEEHKRARTHKEKETLKSDREHTVSIHAvfspagvETSAPLSNVEEQINSAHGSVHSLDTDVVLG 377
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2183-2385 |
1.84e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2183 QADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELL 2262
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2263 K-----------------------------LKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEdaarLSVEAQEAAR 2313
Cdd:COG3883 93 RalyrsggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 2314 LRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEY 2385
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1460-1774 |
1.91e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.83 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1460 EQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQK 1539
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1540 KRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKT 1619
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1620 SKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEA 1699
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774676 1700 EREAKKRAKAEESALKQKEMAEEELERQRKIaesTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVA 1774
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALE---DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDV 355
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
65-170 |
1.95e-07 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 53.08 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 65 ERDRVQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 135
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnkvNKPPYPKLGANMK--KLENCNYAVEL 93
|
90 100 110
....*....|....*....|....*....|....*.
gi 1988774676 136 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 170
Cdd:cd21331 94 GKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRY 129
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2260-2623 |
2.01e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2260 ELLKLKNKIEEENQRLIkkdkdSTQKLLAEEAENMRKLAED----AARLSVeAQEAARLR-QI--AEDDLNqqrALAEKm 2332
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLV-----EMARELAELNEAESDLEQDyqaaSDHLNL-VQTALRQQeKIerYQADLE---ELEER- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2333 LKEKMQAIQEASRlkaEAEMLQKQKDLAQEQAQKLleDKQL--MQQRLEEETE---EYHKSLE-VERKRQLeimaeaerl 2406
Cdd:PRK04863 364 LEEQNEVVEEADE---QQEENEARAEAAEEEVDEL--KSQLadYQQALDVQQTraiQYQQAVQaLERAKQL--------- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2407 rLQVSQLSeaqaraeeeakkfkkqADKVATRLHEteIATQEKMTVVERLEFE-RLNTSKEADD--------LRKAIADLE 2477
Cdd:PRK04863 430 -CGLPDLT----------------ADNAEDWLEE--FQAKEQEATEELLSLEqKLSVAQAAHSqfeqayqlVRKIAGEVS 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2478 NEKA------------RLKKEAEELQNKSKEMADAQQKKIEHEKTV-LQQTFMTEKEMLLKKEKLIEDEKKRLESQFE-- 2542
Cdd:PRK04863 491 RSEAwdvarellrrlrEQRHLAEQLQQLRMRLSELEQRLRQQQRAErLLAEFCKRLGKNLDDEDELEQLQEELEARLEsl 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2543 -EEVKKAKALKDEQERQKQQMEQEKKTLQA------TMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKL 2615
Cdd:PRK04863 571 sESVSEARERRMALRQQLEQLQARIQRLAArapawlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDEL 650
|
....*...
gi 1988774676 2616 REKLQQLE 2623
Cdd:PRK04863 651 AARKQALD 658
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1502-1941 |
2.12e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 57.44 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1502 ESELKQLRDRAAEAEKLRKLAQDEAEK----LRKQVSEETQKKRQAEEELK--RKSEAEKEAAKQKQKaleDLEKLRMQA 1575
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKkasaLKRQLDRESDRNQELQKRIRllEKREAEAEEALREQA---ELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1576 EEAERQVKQaeiEKEKQIKVAHE--AAQKSAAAEL----QSKHMSFAEKTSKLEEsLKQEHGAVLQLQQEAERLKKQQED 1649
Cdd:pfam05557 85 LEALNKKLN---EKESQLADAREviSCLKNELSELrrqiQRAELELQSTNSELEE-LQERLDLLKAKASEAEQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1650 AENSREEAE---KELEKWRQKAN-----------EALRL-RLQAEDEAHK------------KTLAQEEAEKQKEEAERE 1702
Cdd:pfam05557 161 QQSSLAEAEqriKELEFEIQSQEqdseivknsksELARIpELEKELERLRehnkhlnenienKLLLKEEVEDLKRKLERE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1703 AKKRAKAEESALKqKEMAEEELERQRKIAESTA-----------------QQKLTAEQELIRLRADFDNAEQQRSLLEDE 1765
Cdd:pfam05557 241 EKYREEAATLELE-KEKLEQELQSWVKLAQDTGlnlrspedlsrrieqlqQREIVLKEENSSLTSSARQLEKARRELEQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1766 LYRLKNEVAAAQQQRKQ-------LEDELAKVRSEMDILIQLKTKAEKEtMSNTEKSKQLLEaeaaKMKDLAEEASRLRA 1838
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRhkalvrrLQRRVLLLTKERDGYRAILESYDKE-LTMSNYSPQLLE----RIEEAEDMTQKMQA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1839 ISEEAKHQRQIAEEEAARQRAEA---ERILK-----EKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQrkaL 1910
Cdd:pfam05557 395 HNEEMEAQLSVAEEELGGYKQQAqtlERELQalrqqESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEME---L 471
|
490 500 510
....*....|....*....|....*....|..
gi 1988774676 1911 EDQASQHKQEIEE-KIVQLKKSSEAEMERQKA 1941
Cdd:pfam05557 472 ERRCLQGDYDPKKtKVLHLSMNPAAEAYQQRK 503
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1502-1890 |
2.21e-07 |
|
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: 56.83 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1502 ESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQkqkALEDLEKLRMQAEEAERQ 1581
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ---SREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1582 vkQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKtskleeslkqehgaVLQLQQEAERLKKQQEDAENSREEAEKEl 1661
Cdd:pfam07888 110 --SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQR--------------VLERETELERMKERAKKAGAQRKEEEAE- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1662 ekwrqkaNEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEeelerQRKIAESTAqqkltA 1741
Cdd:pfam07888 173 -------RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA-----HRKEAENEA-----L 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1742 EQELIRLRADFDNAEQQRSLLEDELyrlknEVAAAQQQRKQLEDELAKVRS-EMDILIQLKTKAEKETMSNTEKSKQLL- 1819
Cdd:pfam07888 236 LEELRSLQERLNASERKVEGLGEEL-----SSMAAQRDRTQAELHQARLQAaQLTLQLADASLALREGRARWAQERETLq 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774676 1820 ---EAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEklaAISEATRLKTEAEIALKEKE 1890
Cdd:pfam07888 311 qsaEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSE---SRRELQELKASLRVAQKEKE 381
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1462-1743 |
2.34e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 57.27 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1462 QIKDKSQQVDEAlhsrtKIEEEIRLIRIQlettekqkytaeselkqlRDRAAEAEKLRKLAQDEAEKLRKQVSE--ETQK 1539
Cdd:PRK05035 440 AIEQEKKKAEEA-----KARFEARQARLE------------------REKAAREARHKKAAEARAAKDKDAVAAalARVK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1540 KRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAElqskhmsfAEKT 1619
Cdd:PRK05035 497 AKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQ--------QAAN 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1620 SKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKwRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEA 1699
Cdd:PRK05035 569 AEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDP-KKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA 647
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1988774676 1700 EREAKKRAKAEESALKQKEMAEEELERQRKIAESTA----QQKLTAEQ 1743
Cdd:PRK05035 648 VAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAiaraKAKKAAQQ 695
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1017-1579 |
2.52e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1017 SELKDLRLRIEDCEAG-TVARIRKPVEKEPLKEYIQKTTEQKKVQGELDGLKKDL-----------DKVSVKTQEVLAsp 1084
Cdd:PRK02224 213 SELAELDEEIERYEEQrEQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaeterereelaEEVRDLRERLEE-- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1085 qpsasapvLRSELDltvqkmdhaHMLSSVYLEKL--KTVEMVIRNTQGAEgvlKQYEDCLREVHTVPSDV-KEVETYRAK 1161
Cdd:PRK02224 291 --------LEEERD---------DLLAEAGLDDAdaEAVEARREELEDRD---EELRDRLEECRVAAQAHnEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1162 LKKMRTEAEDEQPVFDSLEEELKKASAVSDkmvrvhsERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQLgrqlgy 1241
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVE-------DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL------ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1242 yRESYDwlirwiaDAKQRQEKIQAvpitDSKTLKEQLAQEKKLLEEieqnkDKVDECQKYAK--AYIDTIKDYELQ---L 1316
Cdd:PRK02224 418 -REERD-------ELREREAELEA----TLRTARERVEEAEALLEA-----GKCPECGQPVEgsPHVETIEEDRERveeL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1317 VAYKAQVEPLVSPLKKtKLDSASDniiqeYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLkaeeRKKMAEMQ 1396
Cdd:PRK02224 481 EAELEDLEEEVEEVEE-RLERAED-----LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL----RERAAELE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1397 AEldkqkqlAEAHAKAIAKAEKEAQElklkmqeevsKREIAAvDAEKQKTNIQLELQELKNLSEQQ--IKDKSQQVDEAL 1474
Cdd:PRK02224 551 AE-------AEEKREAAAEAEEEAEE----------AREEVA-ELNSKLAELKERIESLERIRTLLaaIADAEDEIERLR 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1475 HSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKlrklaqDEAEKLRKQVSEETQKKRQAEEELK------ 1548
Cdd:PRK02224 613 EKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDK------ERAEEYLEQVEEKLDELREERDDLQaeigav 686
|
570 580 590
....*....|....*....|....*....|....*
gi 1988774676 1549 RKSEAEKEAAKQKQKALED----LEKLRMQAEEAE 1579
Cdd:PRK02224 687 ENELEELEELRERREALENrveaLEALYDEAEELE 721
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1714-1947 |
2.57e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.35 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1714 LKQKEMAEEELERQRKIAESTAQQKLTAEQElirlradfdnAEQQRsLLEDELYRLknevaAAQQQRKQLEDelakvrse 1793
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQA----------AEQER-LKQLEKERL-----AAQEQKKQAEE-------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1794 mdiliQLKTKAEKETMSNTEKSKQlleAEAAKMKdLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILK-EKLAAI 1872
Cdd:PRK09510 123 -----AAKQAALKQKQAEEAAAKA---AAAAKAK-AEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKaEAEAAA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774676 1873 SEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDqasqhKQEIEEKIVQLKKSSEAEMERQKAIVDDTL 1947
Cdd:PRK09510 194 KAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAE-----AKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2032-2384 |
2.61e-07 |
|
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: 56.83 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2032 RQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKcsaAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLA 2111
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ---SREKHEELEEKYKELSASSEELSEEKDALLAQR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2112 KEAEAAKEKAEREAALLRQQAEEAERQktaaeeeAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKH 2191
Cdd:pfam07888 125 AAHEARIRELEEDIKTLTQRVLERETE-------LERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2192 KKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQR-----------------LKDEVDDAVKQRGQVEEELFKV 2254
Cdd:pfam07888 198 RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrslqerlnaserkvegLGEELSSMAAQRDRTQAELHQA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2255 KVQMEEL---LKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEK 2331
Cdd:pfam07888 278 RLQAAQLtlqLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRV 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 2332 MLKEKMQAIQEasrLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEE 2384
Cdd:pfam07888 358 QLSESRRELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADA 407
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1441-1623 |
2.64e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.01 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1441 AEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETtEKQKYTAESELKQLRDRAAEAEKLRk 1520
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAA-EKAAKQAEQAAKQAEEKQKQAEEAK- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1521 lAQDEAEKLRKqvsEETQKKRQAEEELKRKSEAE---KEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKvah 1597
Cdd:TIGR02794 126 -AKQAAEAKAK---AEAEAERKAKEEAAKQAEEEakaKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKA--- 198
|
170 180
....*....|....*....|....*.
gi 1988774676 1598 EAAQKSAAAELQSKHMSFAEKTSKLE 1623
Cdd:TIGR02794 199 EAAKAKAAAEAAAKAEAEAAAAAAAE 224
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2200-2621 |
2.72e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2200 KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQM----EELLKLKNKIEEENQRL 2275
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVedrrEEIEELEEEIEELRERF 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2276 --IKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAE---------------------DDLNQQRALAEKM 2332
Cdd:PRK02224 401 gdAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpvegsphvETIEEDRERVEEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2333 LKEKMQAIQEASRLKAEAEMLQKQKDLAQEqAQKLLEDKQLMQQRLEEETEEyhksleVERKRQleimaEAERLRLQVSQ 2412
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLVEAEDR-IERLEERREDLEELIAERRET------IEEKRE-----RAEELRERAAE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2413 LSEAQARAEEEAKKFKKQADKVATRLHETEiatQEKMTVVERLefERLNTSKEADDlrkAIADLENEKARLKKEAEELQN 2492
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELN---SKLAELKERI--ESLERIRTLLA---AIADAEDEIERLREKREALAE 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2493 KSKEmadaqqkkiehektvlqqtfmtekemllKKEKLIE--DEKKRLESQFEEE-VKKAKALKDEQERQKQQME------ 2563
Cdd:PRK02224 621 LNDE----------------------------RRERLAEkrERKRELEAEFDEArIEEAREDKERAEEYLEQVEekldel 672
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 2564 -QEKKTLQATMDAALSKQKEAEEemLRKQKEMQELERQRLEQERILAEENQ----KLREKLQQ 2621
Cdd:PRK02224 673 rEERDDLQAEIGAVENELEELEE--LRERREALENRVEALEALYDEAEELEsmygDLRAELRQ 733
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1153-1586 |
2.72e-07 |
|
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: 57.36 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1153 KEVETYRAKLKKMRTEAEDEQpvfDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQREL 1232
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKL---KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1233 EQLGRQLGyyresydwlirwIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTI-KD 1311
Cdd:TIGR00606 768 EEQETLLG------------TIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQeKQ 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1312 YELQLVAYKAQVeplvsplkKTKLDSASDNIIQEYvtlrtrYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKaeerkK 1391
Cdd:TIGR00606 836 HELDTVVSKIEL--------NRKLIQDQQEQIQHL------KSKTNELKSEKLQIGTNLQRRQQFEEQLVELST-----E 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1392 MAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNL----SEQQIKDKS 1467
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgKDDYLKQKE 976
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1468 Q-------QVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKK 1540
Cdd:TIGR00606 977 TelntvnaQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEH 1056
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1988774676 1541 RQAEEELKRKSEAEKEAAKQkQKALEDlEKLRMQAEEAERQVKQAE 1586
Cdd:TIGR00606 1057 QKLEENIDLIKRNHVLALGR-QKGYEK-EIKHFKKELREPQFRDAE 1100
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1620-1944 |
3.09e-07 |
|
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: 56.44 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1620 SKLEESLkQEHGAVLQLQQEAERlkkqqeDAENSREEAEKELEKWRQKANEaLRLRLQAEDEAHKKTLAQEEAEKQKEEA 1699
Cdd:pfam07888 34 NRLEECL-QERAELLQAQEAANR------QREKEKERYKRDREQWERQRRE-LESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1700 EREAKKRAKAEESAL-KQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 1778
Cdd:pfam07888 106 LSASSEELSEEKDALlAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1779 QRKQLEDELAKVRSEMD----ILIQLKTKAEKETMSNTEKSKQLLEAEAAKmKDLAEEASRLrAISEEAKH--QRQIAEE 1852
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALL-EELRSLQERL-NASERKVEglGEELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1853 EAARQRAEAEriLKEKLAAISEATRLKTEAEIALKEkeaenERLRRQAEDEAYQRKALEDQasQHKQEIEEKIVQLKKS- 1931
Cdd:pfam07888 264 AAQRDRTQAE--LHQARLQAAQLTLQLADASLALRE-----GRARWAQERETLQQSAEADK--DRIEKLSAELQRLEERl 334
|
330
....*....|...
gi 1988774676 1932 SEAEMERQKAIVD 1944
Cdd:pfam07888 335 QEERMEREKLEVE 347
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1464-1883 |
3.22e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1464 KDKSQQVDEALHSR--------TKIEEEIRLIRIQ--LETTEKQKYTAESELKQLRDRAAeaeklrkLAQdeaEKLRKQv 1533
Cdd:PRK04863 279 NERRVHLEEALELRrelytsrrQLAAEQYRLVEMAreLAELNEAESDLEQDYQAASDHLN-------LVQ---TALRQQ- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1534 seetQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVK----------QAEIEKEKQIKVAHEAAQKS 1603
Cdd:PRK04863 348 ----EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDelksqladyqQALDVQQTRAIQYQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1604 AAAELQSKHMSFAEKtsKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAlrLRLQAEDEAh 1683
Cdd:PRK04863 424 ERAKQLCGLPDLTAD--NAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEV--SRSEAWDVA- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1684 kktlaqeeaekqkeeaeREAKKRAKaeesalKQKEMAEEELERQRKIAEstAQQKLTAEQELIRLRADF----------- 1752
Cdd:PRK04863 499 -----------------RELLRRLR------EQRHLAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFckrlgknldde 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1753 DNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELakvrSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEE 1832
Cdd:PRK04863 554 DELEQLQEELEARLESLSESVSEARERRMALRQQL----EQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDV 629
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1988774676 1833 ASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAE 1883
Cdd:PRK04863 630 TEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1711-2343 |
3.69e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1711 ESALKQKEMAEEELERQRKIAESTAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKV 1790
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARERL---AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1791 RSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEE-ASRLRAISEEAKHQRQIAEE---EAARQRAEAERILK 1866
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARlEALLAALGLPLPASAEEFAAlraEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1867 EKLAAISEATRLKTEAEIALKEKEAENERLRRQAE--DEAYQ--RKALEDQASQHKQEI----EEkiVQLKkssEAEMER 1938
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLERRKSniPARLLalRDALAEALGLDEAELpfvgEL--IEVR---PEEERW 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1939 QKAI------------VDDTLKQ--RRVVEEEIRILKLNFEKASSGKLDLELE-------LNKLkniadETQQSKIRAEE 1997
Cdd:COG4913 477 RGAIervlggfaltllVPPEHYAaaLRWVNRLHLRGRLVYERVRTGLPDPERPrldpdslAGKL-----DFKPHPFRAWL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1998 EAEKLRKLALEeekrrreaeekvkkiaaaeeeaarqRKAALEELERLRK--------KAEEARKQKDEADKEAEKQiVVA 2069
Cdd:COG4913 552 EAELGRRFDYV-------------------------CVDSPEELRRHPRaitragqvKGNGTRHEKDDRRRIRSRY-VLG 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2070 QQAAQKCSAAEQQvqsvlAQQIEDSITQkklkeeyekakklakeaeaakekaereaalLRQQAEEAERQKtaaeeeaanq 2149
Cdd:COG4913 606 FDNRAKLAALEAE-----LAELEEELAE------------------------------AEERLEALEAEL---------- 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2150 AKAQEDAERLRKEAEFeaakraqaeaaalmQKQQADTEMAkHKKLAEqtlkqkfqVEQELTKvklkLDETDKQKSVLDEE 2229
Cdd:COG4913 641 DALQERREALQRLAEY--------------SWDEIDVASA-EREIAE--------LEAELER----LDASSDDLAALEEQ 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2230 LQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLknkIEEENQRLIKKDKDSTQKLLAEeaenmrkLAEDAARLSVEAQ 2309
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEE---LDELQDRLEAAEDLARLELRAL-------LEERFAAALGDAV 763
|
650 660 670
....*....|....*....|....*....|....*.
gi 1988774676 2310 EAARLRQIAE--DDLNQQRALAEKMLKEKMQAIQEA 2343
Cdd:COG4913 764 ERELRENLEEriDALRARLNRAEEELERAMRAFNRE 799
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1369-1606 |
3.74e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1369 DTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELklkmqeevsKREIAAVDAEKQKTNI 1448
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL---------QAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1449 QLElqelKNLSEQQIKDKSQQVDEALHSRTKIEEEIRliriQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEK 1528
Cdd:COG3883 87 ELG----ERARALYRSGGSVSYLDVLLGSESFSDFLD----RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774676 1529 LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAA 1606
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1396-1858 |
4.19e-07 |
|
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: 56.30 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1396 QAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQktniqleLQELKNLSEQQIKDKSQQVDEA-L 1474
Cdd:pfam09731 81 EPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKA-------LEEVLKEAISKAESATAVAKEAkD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1475 HSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAE--AEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKrKSE 1552
Cdd:pfam09731 154 DAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEklKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLD-NVE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1553 AEKEAAKQKQKALEDLEKLrmqaEEAERQVKQAEIEKekqikvaheaAQKSAAAELQSKHMSFAEKTSKLEESLKQEhga 1632
Cdd:pfam09731 233 EKVEKAQSLAKLVDQYKEL----VASERIVFQQELVS----------IFPDIIPVLKEDNLLSNDDLNSLIAHAHRE--- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1633 VLQLQQEAERLKKQ-QEDAENSREEAEKELEKwrqkANEALRLRLQAEDEAHKKTLaqeeaekqkeeaerEAKKRAKAEE 1711
Cdd:pfam09731 296 IDQLSKKLAELKKReEKHIERALEKQKEELDK----LAEELSARLEEVRAADEAQL--------------RLEFEREREE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1712 SALKQKEMAEEELERQRKIAESTAQQKL-TAEQEL-IRLRADFDNA-EQQRSLLE---DELYRLKNEVAAAQQQRKQLED 1785
Cdd:pfam09731 358 IRESYEEKLRTELERQAEAHEEHLKDVLvEQEIELqREFLQDIKEKvEEERAGRLlklNELLANLKGLEKATSSHSEVED 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774676 1786 ELAKVRSemdilIQLKTKAEKETM--SNTEKSKQLLEAEAAKMKDLAEE----ASRLRAISEEAKhQRQIAEEEAARQR 1858
Cdd:pfam09731 438 ENRKAQQ-----LWLAVEALRSTLedGSADSRPRPLVRELKALKELASDdevvKAALASLPEEAY-QRGVYTEAALRER 510
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1407-1764 |
4.46e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 56.03 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1407 EAHAKAIAKA-EKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSeqqikDKSQQVDEALHSRTKIEEEIR 1485
Cdd:pfam02029 1 IEDEEEAARErRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG-----QGGLDEEEAFLDRTAKREERR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1486 LIRIQlETTEKQKytaESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKE-----AAKQ 1560
Cdd:pfam02029 76 QKRLQ-EALERQK---EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQEnkwstEVRQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1561 KQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKhmSFAEKTSKLEESLKQEHGAVLQLQQEA 1640
Cdd:pfam02029 152 AEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKR--GHPEVKSQNGEEEVTKLKVTTKRRQGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1641 ERLKKQQEDAENSREEAEKELEKWRQKANEALRlrlqAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEEsalkQKEMA 1720
Cdd:pfam02029 230 LSQSQEREEEAEVFLEAEQKLEELRRRRQEKES----EEFEKLRQKQQEAELELEELKKKREERRKLLEEE----EQRRK 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1988774676 1721 EEELERQRKIAESTAQQKltaeQELIRLRAdfDNAEQQRSLLED 1764
Cdd:pfam02029 302 QEEAERKLREEEEKRRMK----EEIERRRA--EAAEKRQKLPED 339
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1701-2138 |
4.73e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 56.07 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1701 REAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQR 1780
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1781 KQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAE 1860
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1861 AERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQK 1940
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1941 AIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKV 2020
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2021 KKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKL 2100
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430
....*....|....*....|....*....|....*...
gi 1988774676 2101 KEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQ 2138
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAA 519
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1258-1680 |
6.28e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 55.90 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1258 QRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAY---KAQVEPLVSPLKK-T 1333
Cdd:pfam05557 121 QRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQeqdSEIVKNSKSELARiP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1334 KLDSASDNIIQEYVTLRTRYSELMTLTSQyikfITDTQRRLDDEEKAAEKLKAEERKKmAEMQAELDKQKQLAEAHAKAI 1413
Cdd:pfam05557 201 ELEKELERLREHNKHLNENIENKLLLKEE----VEDLKRKLEREEKYREEAATLELEK-EKLEQELQSWVKLAQDTGLNL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1414 AKAEKEAQELKLKMQEE-VSKREIAAVDAE-KQKTNIQLELQE-----LKNLSEQQIKDKSQqvdEALHSRTK-----IE 1481
Cdd:pfam05557 276 RSPEDLSRRIEQLQQREiVLKEENSSLTSSaRQLEKARRELEQelaqyLKKIEDLNKKLKRH---KALVRRLQrrvllLT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1482 EEIRLIRIQLETTEKQKYTAESELKQLRdRAAEAEKLRKLAQDEAEKLRKQVS----EETQKKRQA-----EEELKRKSE 1552
Cdd:pfam05557 353 KERDGYRAILESYDKELTMSNYSPQLLE-RIEEAEDMTQKMQAHNEEMEAQLSvaeeELGGYKQQAqtlerELQALRQQE 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1553 AEKEAAKQKQKALE---DLEKLRMQAEEAERQVKQAEIEKEKqikvaHEAAQKSAAAELQSKHMSfAEKTSKLEESLKQE 1629
Cdd:pfam05557 432 SLADPSYSKEEVDSlrrKLETLELERQRLREQKNELEMELER-----RCLQGDYDPKKTKVLHLS-MNPAAEAYQQRKNQ 505
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 1630 HGavlQLQQEAERLKKQQEDAENSREEAEKELEKWRQKAN-EALRLRLQAED 1680
Cdd:pfam05557 506 LE---KLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFkEVLDLRKELES 554
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1500-1736 |
6.66e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1500 TAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKrkseaekeaakQKQKALEDLEKlrmQAEEAE 1579
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-----------ALQAEIDKLQA---EIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1580 RQVKQAEIEKEKQIKVAHEAAQKSAAAE--LQSKHMS-FAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREE 1656
Cdd:COG3883 79 AEIEERREELGERARALYRSGGSVSYLDvlLGSESFSdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1657 AEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQ 1736
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4164-4192 |
7.07e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.48 E-value: 7.07e-07
10 20
....*....|....*....|....*....
gi 1988774676 4164 IVDPETGKEMTVYEAYRKGLIDHQTYLEL 4192
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1480-1789 |
7.40e-07 |
|
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: 54.54 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1480 IEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDE-AEKLRKQVsEETQKKRQAEEELKRKseaEKEAA 1558
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyRQELEEQI-EEREQKRQEEYEEKLQ---EREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1559 KQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAV-LQLQ 1637
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIeEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1638 QEAERLKKQQEDAENSREEAEKELEKWRQKANEAlRLRLQAEDEAHKKtlaqeeaeKQKEEAEREAKKRAKAEESALKQK 1717
Cdd:pfam13868 184 REIARLRAQQEKAQDEKAERDELRAKLYQEEQER-KERQKEREEAEKK--------ARQRQELQQAREEQIELKERRLAE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 1718 EMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAK 1789
Cdd:pfam13868 255 EAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAE 326
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1293-1554 |
8.20e-07 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 55.01 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1293 DKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKKTKLD--------SASDNIIQEYVTLRTRYSELMTLTSQYI 1364
Cdd:pfam05262 79 DHILNLRRILAGYLMAAYGYERSDAETIAKFITIYNAVYRGDLDyfkefykeVVTKSLTKENAGLARRYDQWPGKTQIVI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1365 KF--------ITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREI 1436
Cdd:pfam05262 159 PLkknilsgnVSDVDTDSISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADF 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1437 AAVDAEKQKTNIQLELQELKNlSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTaESELKQLRDRAAEAE 1516
Cdd:pfam05262 239 AQDNADKQRDEVRQKQQEAKN-LPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAK-DHKAFDLKQESKASE 316
|
250 260 270
....*....|....*....|....*....|....*...
gi 1988774676 1517 KLRKLAQDEAEKLRKQVSEETQKKRQAEEElKRKSEAE 1554
Cdd:pfam05262 317 KEAEDKELEAQKKREPVAEDLQKTKPQVEA-QPTSLNE 353
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1887-2325 |
8.24e-07 |
|
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: 55.51 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1887 KEKEAENERLRRQAEDEAyqrkaledqasqHKQEIEEKIVQLKKSSEAEMERQKAIVDDtlkQRRVVEEEIRilklnfek 1966
Cdd:pfam17380 292 KFEKMEQERLRQEKEEKA------------REVERRRKLEEAEKARQAEMDRQAAIYAE---QERMAMERER-------- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1967 assgkldlelELNKLKNIADETQQSKIRAEE---EAEKLRKLaleeekrrreaeekvkkiaaAEEEAARQRKAaleelER 2043
Cdd:pfam17380 349 ----------ELERIRQEERKRELERIRQEEiamEISRMREL--------------------ERLQMERQQKN-----ER 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2044 LRKKAEEARKQKDEadkEAEKQIVVAQQAAQKCSAAEQQVQsvlAQQIEdsitQKKLKEEyekakklakeaeaakekaeR 2123
Cdd:pfam17380 394 VRQELEAARKVKIL---EEERQRKIQQQKVEMEQIRAEQEE---ARQRE----VRRLEEE-------------------R 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2124 EAALLRQQAEEAERQKtaaeeeaANQAKAQEDAERLRKEAEfeaakraqaeaaalMQKQQADtemakhKKLAEQtlKQKF 2203
Cdd:pfam17380 445 AREMERVRLEEQERQQ-------QVERLRQQEEERKRKKLE--------------LEKEKRD------RKRAEE--QRRK 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2204 QVEQELTKVKLKLDETDKQKSVLDEElqrlkdevddavkqrgqveeelfkvkvqMEEllkLKNKIEEENQRLIKKDKDST 2283
Cdd:pfam17380 496 ILEKELEERKQAMIEEERKRKLLEKE----------------------------MEE---RQKAIYEEERRREAEEERRK 544
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1988774676 2284 QKLLAEE---AENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQ 2325
Cdd:pfam17380 545 QQEMEERrriQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1375-1620 |
8.28e-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: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1375 DDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEevSKREIAAVDAEKQKTNIQLElqe 1454
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK--LQAEIAEAEAEIEERREELG--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1455 lKNLSEQQIKDKSQQVDEALHSRTKIEEEIRliRIQLettekqkytaeseLKQLRDRAAEAEKLRKLAQDEAEKLRKQVS 1534
Cdd:COG3883 90 -ERARALYRSGGSVSYLDVLLGSESFSDFLD--RLSA-------------LSKIADADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1535 EETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMS 1614
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
....*.
gi 1988774676 1615 FAEKTS 1620
Cdd:COG3883 234 AAAAAA 239
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2349-2627 |
8.41e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2349 EAEMLQKQKDLAQE---QAQKLLED-KQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRlqvsQLSEAQARAEEEA 2424
Cdd:PTZ00121 1078 DFDFDAKEDNRADEateEAFGKAEEaKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR----KAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2425 KKFKKQADKvATRLHETEIATQEKMTVVER--LEFERLNTSKEADDLRKAIADLENEKARLKKE---------------A 2487
Cdd:PTZ00121 1154 VEIARKAED-ARKAEEARKAEDAKKAEAARkaEEVRKAEELRKAEDARKAEAARKAEEERKAEEarkaedakkaeavkkA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2488 EELQNKSKEMADAQQKKIEHEKTVLQQTFM---TEKEMLLKKE--------KLIEDEKKRLESQFEEEVKKAKALKDEQE 2556
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMahfARRQAAIKAEearkadelKKAEEKKKADEAKKAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2557 RQKQQMEQEKKTLQATMDAALSKQK---------------EAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQ 2621
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKaeeakkaaeaakaeaEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
|
....*.
gi 1988774676 2622 LEDAQK 2627
Cdd:PTZ00121 1393 ADEAKK 1398
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2182-2635 |
8.50e-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: 55.50 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2182 QQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEE- 2260
Cdd:pfam05483 102 KQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREEt 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2261 ---LLKLKNKIEE------------ENQRL-----IKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAarlrqiaED 2320
Cdd:pfam05483 182 rqvYMDLNNNIEKmilafeelrvqaENARLemhfkLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEK-------EN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2321 DLNQQRALAEKMlKEKMQAIQEASRLKAE--AEMLQKQKDLAQEqaqklLEDKQLMQQR-------LEEETEEYHKS--- 2388
Cdd:pfam05483 255 KMKDLTFLLEES-RDKANQLEEKTKLQDEnlKELIEKKDHLTKE-----LEDIKMSLQRsmstqkaLEEDLQIATKTicq 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2389 LEVERKRQLEIMAEAERLR-LQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEAD 2467
Cdd:pfam05483 329 LTEEKEAQMEELNKAKAAHsFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2468 DLRKAIAD---LENEKARLKKEAEELQNKSKEMADA-QQKKIEHEKTVLQQTFMTEKEMLLKKEklIEDEKKRLESQfee 2543
Cdd:pfam05483 409 ELKKILAEdekLLDEKKQFEKIAEELKGKEQELIFLlQAREKEIHDLEIQLTAIKTSEEHYLKE--VEDLKTELEKE--- 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2544 evkKAKALKDEQERQKQQMEQEKKTLQAT-MDAALSKQKE-------AEEEMLRKQKEMQELERQ-RLEQERILAEENQK 2614
Cdd:pfam05483 484 ---KLKNIELTAHCDKLLLENKELTQEASdMTLELKKHQEdiinckkQEERMLKQIENLEEKEMNlRDELESVREEFIQK 560
|
490 500
....*....|....*....|.
gi 1988774676 2615 LREKLQQLEDAQKDQHTRETD 2635
Cdd:pfam05483 561 GDEVKCKLDKSEENARSIEYE 581
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2505-2703 |
9.03e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 55.60 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2505 IEHEKTVLQqtfmTEKEMLlkkEKLIED-EKKRLESqfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEA 2583
Cdd:PRK00409 504 IEEAKKLIG----EDKEKL---NELIASlEELEREL--EQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2584 EEEMLRKQKEMQEL---ERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDIIHLTtiETTKTVYNGQNv 2660
Cdd:PRK00409 575 AQQAIKEAKKEADEiikELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVG--DEVKYLSLGQK- 651
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1988774676 2661 GDVVDGIDKKPDPLAFDGIRDKVPASRLHELGVLPKKEFDKLK 2703
Cdd:PRK00409 652 GEVLSIPDDKEAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPK 694
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1702-1958 |
9.66e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.47 E-value: 9.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1702 EAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRadfdnaeQQRSLLEDELYRLKNEVAAAQQQRK 1781
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQK-------ELEQRAAAEKAAKQAEQAAKQAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1782 QLEDELAKVRSEMDILIQLKTKAEKETMSNTEKskqllEAEAAKMKDLAEEASRlraiseEAKHQRQIAEEEAaRQRAEA 1861
Cdd:TIGR02794 118 QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK-----QAEEEAKAKAAAEAKK------KAEEAKKKAEAEA-KAKAEA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1862 ERILK-EKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQK 1940
Cdd:TIGR02794 186 EAKAKaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYA 265
|
250
....*....|....*...
gi 1988774676 1941 AIVDDTLKQRRVVEEEIR 1958
Cdd:TIGR02794 266 AIIQQAIQQNLYDDPSFR 283
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1753-2001 |
9.66e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.47 E-value: 9.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1753 DNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLE-AEAAKMKDLAE 1831
Cdd:TIGR02794 29 PEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQrAAAEKAAKQAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1832 EASRL-RAISEEAKHQRQIAEEEAARQR-AEAERILKEKLAAISEATRLKTEAEIALKEKEAEnerlRRQAEDEAyqrKA 1909
Cdd:TIGR02794 109 QAAKQaEEKQKQAEEAKAKQAAEAKAKAeAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEA----KKKAEAEA---KA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1910 ledqasqhKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRvvEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQ 1989
Cdd:TIGR02794 182 --------KAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEA--EAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGG 251
|
250
....*....|..
gi 1988774676 1990 QSKIRAEEEAEK 2001
Cdd:TIGR02794 252 ARGAAAGSEVDK 263
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2198-2605 |
9.77e-07 |
|
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: 54.90 E-value: 9.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2198 TLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIK 2277
Cdd:pfam07888 8 TLEEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2278 KDKDSTQKLlaEEAENMRKLAEDA---------ARLSVEAQEAARLRQIAEDdlnqQRALAEKMLKEKMqaiqEASRLKA 2348
Cdd:pfam07888 88 ELRQSREKH--EELEEKYKELSASseelseekdALLAQRAAHEARIRELEED----IKTLTQRVLERET----ELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2349 EAEMLQKQKdlAQEQAQKllEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLseaqaraeeeakkfK 2428
Cdd:pfam07888 158 RAKKAGAQR--KEEEAER--KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTL--------------T 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2429 KQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIE-- 2506
Cdd:pfam07888 220 QKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREgr 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2507 ----HEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKE 2582
Cdd:pfam07888 300 arwaQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKE 379
|
410 420
....*....|....*....|....*
gi 1988774676 2583 AEEEMLRKQKEMQELER--QRLEQE 2605
Cdd:pfam07888 380 KEQLQAEKQELLEYIRQleQRLETV 404
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1363-1944 |
1.12e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.29 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1363 YIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKqlaeaHAKAIAKAEKEAQELKLKMQEEVSKreiaavdAE 1442
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYN-----NLKSALNELSSLEDMKNRYESEIKT-------AE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1443 KQKTNIQLELQELKNLSEQQIKDKSqqvDEALHSRTKIEEEIRLIRiQLETTEKQKYTAESELKQLRDraaeaeKLRKLA 1522
Cdd:PRK01156 263 SDLSMELEKNNYYKELEERHMKIIN---DPVYKNRNYINDYFKYKN-DIENKKQILSNIDAEINKYHA------IIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1523 QDEAEKlrkqvsEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQ--AEIEKEKQIKVAHEAA 1600
Cdd:PRK01156 333 VLQKDY------NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERmsAFISEILKIQEIDPDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1601 QKSAAAELQSKHMSFAEKTSKLEESLK---------QEHGAVLQLQ------------QEAERLKKQQEDAENSREEAEK 1659
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRalrenldelSRNMEMLNGQsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1660 ELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEEL-ERQRKIAESTAQQK 1738
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIkNRYKSLKLEDLDSK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1739 ltaeqelirlRADFDNAEQQRSLLE-DELYRLKNEVaaaQQQRKQLEDELAKVRSEMDiliqlktkaekETMSNTEKSKQ 1817
Cdd:PRK01156 567 ----------RTSWLNALAVISLIDiETNRSRSNEI---KKQLNDLESRLQEIEIGFP-----------DDKSYIDKSIR 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1818 LLEAEAAKMKDLAEEASRLRAISEEAKhqrqiaeeeaarqraEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLR 1897
Cdd:PRK01156 623 EIENEANNLNNKYNEIQENKILIEKLR---------------GKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSR 687
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1898 RQAED---EAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVD 1944
Cdd:PRK01156 688 KALDDakaNRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGD 737
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1639-2072 |
1.20e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 55.02 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1639 EAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQK- 1717
Cdd:NF033838 56 QKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQFKKDTl 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1718 EMAEEELERQRKIAEstAQQKLTAEQElirlradfdnaEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVrsemdil 1797
Cdd:NF033838 136 EPGKKVAEATKKVEE--AEKKAKDQKE-----------EDRRNYPTNTYKTLELEIAESDVEVKKAELELVKE------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1798 iqlktkaEKETMSNTEKSKQlleaEAAKMKDLAEEASRLraisEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATR 1877
Cdd:NF033838 196 -------EAKEPRDEEKIKQ----AKAKVESKKAEATRL----EKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1878 LKTEAEIALKEKEAENERLRRQAE--DEAYQRKALEDQASQHKQ---EIEEKIVQLKKSSEAEMERQKaivddtlkqRRV 1952
Cdd:NF033838 261 PKRRAKRGVLGEPATPDKKENDAKssDSSVGEETLPSPSLKPEKkvaEAEKKVEEAKKKAKDQKEEDR---------RNY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1953 VEEEIRILKLNFEKASSGKLDLELELNK--LKNIADETQQSKIRAEEEAEKlrklaleeekrrreaeekvkkiaaaeeea 2030
Cdd:NF033838 332 PTNTYKTLELEIAESDVKVKEAELELVKeeAKEPRNEEKIKQAKAKVESKK----------------------------- 382
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1988774676 2031 arQRKAALEELERLRKKAEEARKQK-DEADKEAEKQIVVAQQA 2072
Cdd:NF033838 383 --AEATRLEKIKTDRKKAEEEAKRKaAEEDKVKEKPAEQPQPA 423
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1502-1741 |
1.24e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 54.60 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1502 ESELKQLRDRAAEAEKlrKLAQDE-AEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQK--QKALEDLEKLRMQAEEA 1578
Cdd:PRK07735 4 EKDLEDLKKEAARRAK--EEARKRlVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRaaAAAKAKAAALAKQKREG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1579 ERQVKQAEIEKEKqiKVAHEAAQKSAAAELQSKHMSFAEKTSklEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAE 1658
Cdd:PRK07735 82 TEEVTEEEKAKAK--AKAAAAAKAKAAALAKQKREGTEEVTE--EEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1659 KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKK-----RAKAEESAL-KQKEM-----AEEELERQ 1727
Cdd:PRK07735 158 EETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKakaaaAAKAKAAALaKQKASqgngdSGDEDAKA 237
|
250
....*....|....
gi 1988774676 1728 RKIAESTAQQKLTA 1741
Cdd:PRK07735 238 KAIAAAKAKAAAAA 251
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1371-1628 |
1.33e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 54.95 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1371 QRRLDDEekaaeKLKAEERKKMAEmqAELDKQKQLAEAHAKAIAKAEKEAQElklkmqeevskREIAAVDAEKQKTNIQL 1450
Cdd:PRK05035 459 QARLERE-----KAAREARHKKAA--EARAAKDKDAVAAALARVKAKKAAAT-----------QPIVIKAGARPDNSAVI 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1451 ELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRliRIQLETTEKQKYTAESELKQLRDRAAEAEklrKLAQDEAEKLR 1530
Cdd:PRK05035 521 AAREARKAQARARQAEKQAAAAADPKKAAVAAAIA--RAKAKKAAQQAANAEAEEEVDPKKAAVAA---AIARAKAKKAA 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1531 KQVSEETQKKRQAEEELKrKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVK-QAEIEKEKQIKVAHEAAQKSAAAELQ 1609
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPK-KAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAvAAAIARAKARKAAQQQANAEPEEAED 674
|
250
....*....|....*....
gi 1988774676 1610 SKHMSFAEKTSKLEESLKQ 1628
Cdd:PRK05035 675 PKKAAVAAAIARAKAKKAA 693
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1502-1602 |
1.44e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 54.83 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1502 ESELKQLRDRAAEAEKLRKlaqdEAEKLRKQVSEetQKKRQAEEELKRKSEAEKEAAKQ----KQKALEDLEKLR-MQAE 1576
Cdd:PRK00409 526 EELERELEQKAEEAEALLK----EAEKLKEELEE--KKEKLQEEEDKLLEEAEKEAQQAikeaKKEADEIIKELRqLQKG 599
|
90 100
....*....|....*....|....*.
gi 1988774676 1577 EAERQVKQAEIEKEKQIKVAHEAAQK 1602
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEKKEK 625
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1400-1685 |
1.50e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 54.22 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1400 DKQKQLAEAHAKAIAKAEKEAQELKLKMQEEvskrEIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTK 1479
Cdd:PRK07735 2 DPEKDLEDLKKEAARRAKEEARKRLVAKHGA----EISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1480 IEEEIRliriqlETTEKQKYTAESelkqlrdRAAEAEKLRklaqdeAEKLRKQVSEETQkkrQAEEELKRKSEAeKEAAK 1559
Cdd:PRK07735 78 KREGTE------EVTEEEKAKAKA-------KAAAAAKAK------AAALAKQKREGTE---EVTEEEKAAAKA-KAAAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1560 QKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQE 1639
Cdd:PRK07735 135 AKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAK 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1988774676 1640 AERLKKQQEdaenSREEAEKELEKWRQKANEALRLRLQAEDEAHKK 1685
Cdd:PRK07735 215 AAALAKQKA----SQGNGDSGDEDAKAKAIAAAKAKAAAAARAKTK 256
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1755-1925 |
1.51e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.62 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1755 AEQQRSLLEdeLYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtMSNTEKSKQLLEAEAAKMKDLAEEA- 1833
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLELEIEEVEARIKKYe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1834 SRLRAIS--EEAKH-QRQIaeEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAL 1910
Cdd:COG1579 80 EQLGNVRnnKEYEAlQKEI--ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|....*
gi 1988774676 1911 EDQASQHKQEIEEKI 1925
Cdd:COG1579 158 LEELEAEREELAAKI 172
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1249-1949 |
1.55e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 55.06 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1249 LIRWIADAKQRQEKIQAVPITDSKTLKEQLAQE---------KKLLEEIEQNKDKVDECQKYAKAY--IDTIKDYELQlv 1317
Cdd:TIGR01612 1031 IEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEigkniellnKEILEEAEINITNFNEIKEKLKHYnfDDFGKEENIK-- 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1318 aYKAQVEPLVSPLKKtkLDSASDNIIQEYVTLRTRySElmtltsqyiKFITDTQRRLDDEEKAAEKLKAEE-----RKKM 1392
Cdd:TIGR01612 1109 -YADEINKIKDDIKN--LDQKIDHHIKALEEIKKK-SE---------NYIDEIKAQINDLEDVADKAISNDdpeeiEKKI 1175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1393 AEMQAELDKQKQLAEAHAK---AIAKAEK------EAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQE--LKNLSEq 1461
Cdd:TIGR01612 1176 ENIVTKIDKKKNIYDEIKKllnEIAEIEKdktsleEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEayIEDLDE- 1254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1462 qIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRaaeAEKLRKLAQDEAEK---------LRKQ 1532
Cdd:TIGR01612 1255 -IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDI---REKSLKIIEDFSEEsdindikkeLQKN 1330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1533 VSEETQKKRQAEEELKRKSEAEKEAAKQK-QKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEaaqksaaaelqsk 1611
Cdd:TIGR01612 1331 LLDAQKHNSDINLYLNEIANIYNILKLNKiKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD------------- 1397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1612 HMSFAEKTSKLEESL--KQEHGAVLQLQQEAERLKKQQEDA----ENSREEAE------KELEKWRQKANEALRLRLQAE 1679
Cdd:TIGR01612 1398 DINLEECKSKIESTLddKDIDECIKKIKELKNHILSEESNIdtyfKNADENNEnvlllfKNIEMADNKSQHILKIKKDNA 1477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1680 DEAHKKTLAQEEAEKQKEEAER-EAKKRAKAEEsalKQKEMAEeelerQRKIAESTAQQKLTAeqelIRLRADFDNAEQQ 1758
Cdd:TIGR01612 1478 TNDHDFNINELKEHIDKSKGCKdEADKNAKAIE---KNKELFE-----QYKKDVTELLNKYSA----LAIKNKFAKTKKD 1545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1759 RSLLEDELYRLKN----EVAAAQQQRKQLEDElaKVRSEMDIliqLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEAS 1834
Cdd:TIGR01612 1546 SEIIIKEIKDAHKkfilEAEKSEQKIKEIKKE--KFRIEDDA---AKNDKSNKAAIDIQLSLENFENKFLKISDIKKKIN 1620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1835 rlRAISEEAKHQRQIAEEEAARQRAEaeriLKEKLAAISEatrLKTEAEiALKEKEAENERLRRQAEDEAYQRKALEDQA 1914
Cdd:TIGR01612 1621 --DCLKETESIEKKISSFSIDSQDTE----LKENGDNLNS---LQEFLE-SLKDQKKNIEDKKKELDELDSEIEKIEIDV 1690
|
730 740 750
....*....|....*....|....*....|....*....
gi 1988774676 1915 SQHKQEIE----EKIVQLKKSSEAEMERQKAIVDDTLKQ 1949
Cdd:TIGR01612 1691 DQHKKNYEigiiEKIKEIAIANKEEIESIKELIEPTIEN 1729
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1377-1674 |
1.67e-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: 54.09 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1377 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELK 1456
Cdd:pfam06160 87 ALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1457 NLSEQQIKDKSQQVDEALHSRTkIEEEIRLIRI-----QLETT---------------EKQKYT-----AESELKQLRDR 1511
Cdd:pfam06160 167 ELTESGDYLEAREVLEKLEEET-DALEELMEDIpplyeELKTElpdqleelkegyremEEEGYAlehlnVDKEIQQLEEQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1512 AAEAEK-LRKLAQDEAEKLRKQVSEETQK-----------KRQAEEELKRKSEAEKEAAKQKQKALEDLEKL----RMQA 1575
Cdd:pfam06160 246 LEENLAlLENLELDEAEEALEEIEERIDQlydllekevdaKKYVEKNLPEIEDYLEHAEEQNKELKEELERVqqsyTLNE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1576 EEAERqvkQAEIEKE-KQIKVAHEAAQKsaaaELQSKHMSFAEKTSKLEESLKQehgaVLQLQQEAERLKKQQEDAENSR 1654
Cdd:pfam06160 326 NELER---VRGLEKQlEELEKRYDEIVE----RLEEKEVAYSELQEELEEILEQ----LEEIEEEQEEFKESLQSLRKDE 394
|
330 340
....*....|....*....|
gi 1988774676 1655 EEAEKELEKWRQKANEALRL 1674
Cdd:pfam06160 395 LEAREKLDEFKLELREIKRL 414
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1345-1801 |
1.72e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 54.44 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1345 EYVTLRTRyseLMTLTSQYikfiTDTQRRLddeEKAAEKLKAEErKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL- 1423
Cdd:pfam10174 304 ELLALQTK---LETLTNQN----SDCKQHI---EVLKESLTAKE-QRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLt 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1424 --KLKMQEEVSKREiAAVDAEKQKTNIqleLQE-LKNLSEQqIKDKSQQVDEalhsrtkieeeirlIRIQLETTEKQKYT 1500
Cdd:pfam10174 373 eeKSTLAGEIRDLK-DMLDVKERKINV---LQKkIENLQEQ-LRDKDKQLAG--------------LKERVKSLQTDSSN 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1501 AESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEK----LRMQAE 1576
Cdd:pfam10174 434 TDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEhassLASSGL 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1577 EAERQVKQAEIEKEK----------QIKVAHEAAQKSAAAElqskhmSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQ 1646
Cdd:pfam10174 514 KKDSKLKSLEIAVEQkkeecsklenQLKKAHNAEEAVRTNP------EINDRIRLLEQEVARYKEESGKAQAEVERLLGI 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1647 QEDAENSREEAEKELEKWRQKAneALRLRLQAEDEAHKKTLAQEEAEKQKEEAErEAKKRAKAEESALKQKEMAE--EEL 1724
Cdd:pfam10174 588 LREVENEKNDKDKKIAELESLT--LRQMKEQNKKVANIKHGQQEMKKKGAQLLE-EARRREDNLADNSQQLQLEElmGAL 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1725 ERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAA---------------QQQRKQLEDELAK 1789
Cdd:pfam10174 665 EKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAaisekdaniallelsSSKKKKTQEEVMA 744
|
490
....*....|...
gi 1988774676 1790 VRSEMDILI-QLK 1801
Cdd:pfam10174 745 LKREKDRLVhQLK 757
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
193-288 |
1.81e-06 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 50.38 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 193 KLLL-WSQRMTDGYqGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNL-----------------------EN 248
Cdd:cd21224 3 SLLLkWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 249 LEQAFSVAEK-----------DLG-VTRLLDPEDVDVPHPDEKSIITYVSSL 288
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1386-1841 |
2.02e-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: 54.57 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1386 AEERKKMAEMQAEL-----DKQKQLAEAHAKAIAKAEkeaqELklkmqEEVSKREiAAVDAEKQKTNIQLELqeLKNLSE 1460
Cdd:COG3096 277 ANERRELSERALELrrelfGARRQLAEEQYRLVEMAR----EL-----EELSARE-SDLEQDYQAASDHLNL--VQTALR 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1461 QQIKDKSQQVD-EALHSRTKIEEEIRliriqlettekqkytaeselKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEetqk 1539
Cdd:COG3096 345 QQEKIERYQEDlEELTERLEEQEEVV--------------------EEAAEQLAEAEARLEAAEEEVDSLKSQLAD---- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1540 KRQAEEELKRKseaekeaAKQKQKALEDLEKLRMQAEEAERQVKQAEiekekqikvAHEAAQKSAAAELQSKHMSFAEKT 1619
Cdd:COG3096 401 YQQALDVQQTR-------AIQYQQAVQALEKARALCGLPDLTPENAE---------DYLAAFRAKEQQATEEVLELEQKL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1620 SkLEESLKQEHGAVLQLQQEAerlkkqqeDAENSREEAekelekWrQKANEALR----LRLQAEDEAHKKTlaqeEAEKQ 1695
Cdd:COG3096 465 S-VADAARRQFEKAYELVCKI--------AGEVERSQA------W-QTARELLRryrsQQALAQRLQQLRA----QLAEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1696 KEEAEREAKKRAKAEESALKQK------EMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRL 1769
Cdd:COG3096 525 EQRLRQQQNAERLLEEFCQRIGqqldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAW 604
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774676 1770 KNEVAAAQQQRKQLEDELAKVRSEMDILIQLktkAEKETMSNTEKS-----KQLLEAEAAKMKDLA-EEASRLRAISE 1841
Cdd:COG3096 605 LAAQDALERLREQSGEALADSQEVTAAMQQL---LEREREATVERDelaarKQALESQIERLSQPGgAEDPRLLALAE 679
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2478-2623 |
2.12e-06 |
|
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: 53.06 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2478 NEKARLKKEAEELQNKSKEMADAQQKKIEhEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLEsqfeEEVKKAKALKDEQER 2557
Cdd:pfam02841 155 EERDKLEAKYNQVPRKGVKAEEVLQEFLQ-SKEAVEEAILQTDQALTAKEKAIEAERAKAE----AAEAEQELLREKQKE 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2558 QKQQMEQEKKTLQATMdAALSKQKEAEEEMLRKQKEMQeLERQRLEQERILAE----ENQKLREKLQQLE 2623
Cdd:pfam02841 230 EEQMMEAQERSYQEHV-KQLIEKMEAEREQLLAEQERM-LEHKLQEQEELLKEgfktEAESLQKEIQDLK 297
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1877-2370 |
2.15e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1877 RLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKivqlkKSSEAEMERQKAIVDDTLKQRRVVEEE 1956
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL-----EELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1957 IRILKLNFEKASsgkldLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKA 2036
Cdd:COG4717 125 LQLLPLYQELEA-----LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2037 ALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSIT--QKKLKEEYEKAKKLAKEA 2114
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLalLGLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2115 EAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKL 2194
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2195 AEQTLKQKFQVEQE--LTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELfKVKVQMEELLKLKNKIEEEN 2272
Cdd:COG4717 360 EEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL-EELLEALDEEELEEELEELE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2273 QRlikkdkdstqklLAEEAENMRKLAEDAARLSveaqeaARLRQIAEDDLNQQRALAEKMLKEKMQ-AIQEASRLKAEAE 2351
Cdd:COG4717 439 EE------------LEELEEELEELREELAELE------AELEQLEEDGELAELLQELEELKAELReLAEEWAALKLALE 500
|
490 500
....*....|....*....|
gi 1988774676 2352 MLQK-QKDLAQEQAQKLLED 2370
Cdd:COG4717 501 LLEEaREEYREERLPPVLER 520
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1367-1852 |
2.17e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 54.42 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1367 ITDTQRRLDDEEKAAEKLKAEErkkMAEMQAELDKQK----QLAEAHAKAIAKAEKEAQelklkMQEEvskreIAAVDAE 1442
Cdd:PRK10246 389 LTHAEQKLNALPAITLTLTADE---VAAALAQHAEQRplrqRLVALHGQIVPQQKRLAQ-----LQVA-----IQNVTQE 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1443 KQKTNIQLELQElknlseQQIKDKSQQVDEAlhsRTKIEEEIRL-----IRIQLE---------TTEK---QKYTAeSEL 1505
Cdd:PRK10246 456 QTQRNAALNEMR------QRYKEKTQQLADV---KTICEQEARIkdleaQRAQLQagqpcplcgSTSHpavEAYQA-LEP 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1506 KQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQA 1585
Cdd:PRK10246 526 GVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQ 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1586 EiEKEKQIKvaheaaQKSAAAELQSKHMSFAEKTSKLEESLKQEHgAVLQLQQEAERLKKQQEDAENS-REEAEKELEKW 1664
Cdd:PRK10246 606 E-EHERQLR------LLSQRHELQGQIAAHNQQIIQYQQQIEQRQ-QQLLTALAGYALTLPQEDEEASwLATRQQEAQSW 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1665 RQKANEALRLRLQ-AEDEAHKKTLAQEEAEKQKEEAE-----REAKKRAKAEESALkQKEMAEEELERQRkIAESTAQ-- 1736
Cdd:PRK10246 678 QQRQNELTALQNRiQQLTPLLETLPQSDDLPHSEETValdnwRQVHEQCLSLHSQL-QTLQQQDVLEAQR-LQKAQAQfd 755
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1737 QKLTA---EQELIRLRADFDNA-----EQQRSLLEDELYRLK-------NEVAAAQQQRKQLEDELAKVRSEMDILIQLK 1801
Cdd:PRK10246 756 TALQAsvfDDQQAFLAALLDEEtltqlEQLKQNLENQRQQAQtlvtqtaQALAQHQQHRPDGLDLTVTVEQIQQELAQLA 835
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1988774676 1802 TKAEKETMSNTEKSKQLleaeaakmKDLAEEASRLRAISEEAKHQRQIAEE 1852
Cdd:PRK10246 836 QQLRENTTRQGEIRQQL--------KQDADNRQQQQALMQQIAQATQQVED 878
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3948-3984 |
2.36e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.71 E-value: 2.36e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1988774676 3948 RYLQGTGCIAGVFLESTKERLSIYQAMKKNMIRPGTA 3984
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1395-1577 |
2.36e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1395 MQAELDKQKQLAEAHAKaIAKAEKEAQELklkmQEEVSKREIAAVDAEKQKTNIQLELQELknlsEQQIKDKSQQVDEAL 1474
Cdd:COG1579 2 MPEDLRALLDLQELDSE-LDRLEHRLKEL----PAELAELEDELAALEARLEAAKTELEDL----EKEIKRLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1475 HSRTKIEEEIRLIRiqletTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAE 1554
Cdd:COG1579 73 ARIKKYEEQLGNVR-----NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
170 180
....*....|....*....|...
gi 1988774676 1555 KEAAKQKQKALEDLEKLRMQAEE 1577
Cdd:COG1579 148 DEELAELEAELEELEAEREELAA 170
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1514-1871 |
2.54e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 53.80 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1514 EAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQI 1593
Cdd:pfam15709 164 TPASISHAERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERNL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1594 KVAHEAAQK----SAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQ---------EDAENSREEAEKE 1660
Cdd:pfam15709 244 EVAAELSGPdvinSKETEDASERGAFSSDSVVEDPWLSSKYDAEESQVSIDGRSSPTQtfvvtgnmeSEEERSEEDPSKA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1661 LEKWRQKANEAlRLRLQAEdEAHKKTLAQeeaekqkeeaerEAKKRAKAEESALKQkemaeEELERQRKIAE--STAQQK 1738
Cdd:pfam15709 324 LLEKREQEKAS-RDRLRAE-RAEMRRLEV------------ERKRREQEEQRRLQQ-----EQLERAEKMREelELEQQR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1739 LTAEqelIRLRADFDNAEQQRSllEDELYRLKNEVAAAQQQRKQLEDELAKVrsemdiLIQLKTKAEKETMSNTEKSKQL 1818
Cdd:pfam15709 385 RFEE---IRLRKQRLEEERQRQ--EEEERKQRLQLQAAQERARQQQEEFRRK------LQELQRKKQQEEAERAEAEKQR 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774676 1819 LEAEAAKmkdLAEEASRLRAISEEAK--HQRQIAEEEAARQRAEAERILKEKLAA 1871
Cdd:pfam15709 454 QKELEMQ---LAEEQKRLMEMAEEERleYQRQKQEAEEKARLEAEERRQKEEEAA 505
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1499-1945 |
2.60e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.88 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1499 YTAESELKQLRDRAAEaeklrKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEA----EKEAAKQKQKALEDLEKLRMQ 1574
Cdd:pfam05667 91 YPNEPDIRKILMFLVE-----KLPRESSEAADQPVGKSAVLQRAIAAAIRSQLAApwlpPECKPHQRRQGSRALRPFHTQ 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1575 A-EEAERQVKQAEIEKEkqikvaheaaqksaAAELQSKHMSFAE----KTSKLEESLKQEHGAVLQLQQEAERLKKQQED 1649
Cdd:pfam05667 166 TlVLPGRKGKTLKNSKE--------------LKEFYSEYLPPVTaqpsSRASVVPSLLERNAAELAAAQEWEEEWNSQGL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1650 AENSREEAEK--ELEKWRQKANEALRLRLQAEDEAHkktlaqeeaekqkeeaeREAKKRAKAEESALKQKEMAEEELERQ 1727
Cdd:pfam05667 232 ASRLTPEEYRkrKRTKLLKRIAEQLRSAALAGTEAT-----------------SGASRSAQDLAELLSSFSGSSTTDTGL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1728 RKIAESTAQQKLTAEQELIRLRADFDNAEQQrslLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILI----QLKTK 1803
Cdd:pfam05667 295 TKGSRFTHTEKLQFTNEAPAATSSPPTKVET---EEELQQQREEELEELQEQLEDLESSIQELEKEIKKLEssikQVEEE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1804 AEKETMSNTEKSKQ----------LLEAEA--AKMKDLAEEAS-RLRAISEE-AKHQRQIAEE------EAARQRAEAER 1863
Cdd:pfam05667 372 LEELKEQNEELEKQykvkkktldlLPDAEEniAKLQALVDASAqRLVELAGQwEKHRVPLIEEyralkeAKSNKEDESQR 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1864 I------LKEKLAAISEATRLKTEaeiALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIE-EKIVQLKKSSEAEM 1936
Cdd:pfam05667 452 KleeikeLREKIKEVAEEAKQKEE---LYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEiTKILSDTKSLQKEI 528
|
490
....*....|....*.
gi 1988774676 1937 -------ERQKAIVDD 1945
Cdd:pfam05667 529 nsltgklDRTFTVTDE 544
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2495-2627 |
2.79e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.63 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2495 KEMADAQQKKIEHE-KTVLQQTfmtEKEM-LLKKEKLIE--DEKKRLESQFEEEVKKAKalkDEQERQKQQMEQEKKTLQ 2570
Cdd:PRK12704 26 KKIAEAKIKEAEEEaKRILEEA---KKEAeAIKKEALLEakEEIHKLRNEFEKELRERR---NELQKLEKRLLQKEENLD 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774676 2571 ATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLrEKLQQL--EDAQK 2627
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLtaEEAKE 157
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
2452-2622 |
3.08e-06 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 53.30 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2452 VERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKsKEMADAQQKKIEHEKTVLQQTFMTEKEmllKKEKLIE 2531
Cdd:pfam15066 372 VEELIEDKYNVILEKNDINKTLQNLQEILANTQKHLQESRKE-KETLQLELKKIKVNYVHLQERYITEMQ---QKNKSVS 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2532 D--EKKRLESQFEEEVKKAKALKDEQERqkqqmeqekktlqATMDA--ALSKQKEA-EEEMLRKQKEMQELERQRLeqer 2606
Cdd:pfam15066 448 QclEMDKTLSKKEEEVERLQQLKGELEK-------------ATTSAldLLKREKETrEQEFLSLQEEFQKHEKENL---- 510
|
170
....*....|....*.
gi 1988774676 2607 ilaEENQKLREKLQQL 2622
Cdd:pfam15066 511 ---EERQKLKSRLEKL 523
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1712-1916 |
3.34e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1712 SALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAK-- 1789
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1790 --------VRSEMDILIQLK---------------TKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKH- 1845
Cdd:COG3883 93 ralyrsggSVSYLDVLLGSEsfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAe 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 1846 -QRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQ 1916
Cdd:COG3883 173 lEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1144-1752 |
3.35e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1144 EVHTVPSDVKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAvsdkmvrvHSERDVELDHFRQQLSSLqDRWKAvFT 1223
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAER--------YAAARERLAELEYLRAAL-RLWFA-QR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1224 QIDLRQRELEQLgrqlgyyRESYDWLIRWIADAKQRQEKIQAvpitDSKTLKEQLAQ-----EKKLLEEIEQNKDKVDEC 1298
Cdd:COG4913 289 RLELLEAELEEL-------RAELARLEAELERLEARLDALRE----ELDELEAQIRGnggdrLEQLEREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1299 QKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLK--KTKLDSASDNIIQEYVTLRTRYSELmtltsqyikfiTDTQRRLDD 1376
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAalLEALEEELEALEEALAEAEAALRDL-----------RRELRELEA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1377 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIA-----KAEKEA-----------QELKLKMQEEVSKREIAAVD 1440
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGelievRPEEERwrgaiervlggFALTLLVPPEHYAAALRWVN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1441 AEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTK-----IEEEI--RLIRIQLETTEkqkytaesELKQLRdRAA 1513
Cdd:COG4913 507 RLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHpfrawLEAELgrRFDYVCVDSPE--------ELRRHP-RAI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1514 EAEKLRKLAQDEAEK-LRKQVSEE-------TQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQA 1585
Cdd:COG4913 578 TRAGQVKGNGTRHEKdDRRRIRSRyvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYS 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1586 eiekEKQIKVAheaaqkSAAAELqskhmsfAEKTSKLEEsLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWR 1665
Cdd:COG4913 658 ----WDEIDVA------SAEREI-------AELEAELER-LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1666 QKANEALRLRLQAEDEAHkktlaqEEAEKQKEEAEREAKKRAKAEESALKQKEMAeEELERQRKIAESTAQQkltAEQEL 1745
Cdd:COG4913 720 KELEQAEEELDELQDRLE------AAEDLARLELRALLEERFAAALGDAVERELR-ENLEERIDALRARLNR---AEEEL 789
|
....*..
gi 1988774676 1746 IRLRADF 1752
Cdd:COG4913 790 ERAMRAF 796
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3749-3783 |
3.42e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.42e-06
10 20 30
....*....|....*....|....*....|....*
gi 1988774676 3749 LLEAQAATGFIVDPLKNETLTVDEAVRKGVVGPEI 3783
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1865-2637 |
3.57e-06 |
|
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: 53.51 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1865 LKEKLAAISEATRLKTEAEIALKEKEAENERLRrqaedEAYQRKALEDQASQHKQEIEEKIV--QLKKSSEAEMERQKAI 1942
Cdd:TIGR00606 171 LKQKFDEIFSATRYIKALETLRQVRQTQGQKVQ-----EHQMELKYLKQYKEKACEIRDQITskEAQLESSREIVKSYEN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1943 VDDTLKQRRVVEEEIRilklnfekasSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLrklaleeekrRREAEEKVKK 2022
Cdd:TIGR00606 246 ELDPLKNRLKEIEHNL----------SKIMKLDNEIKALKSRKKQMEKDNSELELKMEKV----------FQGTDEQLND 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2023 IAAAEEEAARQRKAAL----EELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQK 2098
Cdd:TIGR00606 306 LYHNHQRTVREKERELvdcqRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2099 KLKEeyekakklakeaeaaKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfEAAKRAQAEAAAL 2178
Cdd:TIGR00606 386 PFSE---------------RQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKK-GLGRTIELKKEIL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2179 MQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSV---LDEE--LQRLKDEVDDAVKQRGQVEEELFK 2253
Cdd:TIGR00606 450 EKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTetlKKEVksLQNEKADLDRKLRKLDQEMEQLNH 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2254 VKVQMEELLKLKNKIEEENQRLIKKDKDSTQKL--LAEEAENMRKLAEDAARLSVEAQ-----------EAARLRQIAED 2320
Cdd:TIGR00606 530 HTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELtsLLGYFPNKKQLEDWLHSKSKEINqtrdrlaklnkELASLEQNKNH 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2321 DLNQQRALAEKMLK--EKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYH-------KSLEV 2391
Cdd:TIGR00606 610 INNELESKEEQLSSyeDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqRVFQT 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2392 ERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRK 2471
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2472 AIADLENEKARLKKeAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEML------LKKEKLIEDEKKRLESQFEEEV 2545
Cdd:TIGR00606 770 QETLLGTIMPEEES-AKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLdrtvqqVNQEKQEKQHELDTVVSKIELN 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2546 KKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELER---QRLEQERILAEENQKLREKLQQL 2622
Cdd:TIGR00606 849 RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIReikDAKEQDSPLETFLEKDQQEKEEL 928
|
810
....*....|....*
gi 1988774676 2623 EDAQKDQHTRETDKV 2637
Cdd:TIGR00606 929 ISSKETSNKKAQDKV 943
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2446-2619 |
3.61e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2446 QEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQ---NKSKEMADAQQKKIEHEKTvLQQTFMTEKEM 2522
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEkeiKRLELEIEEVEARIKKYEE-QLGNVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2523 L-LKKEklIEDEKKRLeSQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAalsKQKEAEEEMLRKQKEMQELERQR 2601
Cdd:COG1579 92 EaLQKE--IESLKRRI-SDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAER 165
|
170
....*....|....*...
gi 1988774676 2602 LEQERILAEENQKLREKL 2619
Cdd:COG1579 166 EELAAKIPPELLALYERI 183
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1723-1867 |
3.61e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1723 ELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRS---------E 1793
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyealqkE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774676 1794 MDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKE 1867
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1371-1599 |
4.16e-06 |
|
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: 52.23 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1371 QRRLDDEEKAAEKLKA--EERKKMAEMQAELDKQ-KQLAEAHAKAIAKAEKEAQELKLKMQEEVSK---REIAAVDAEKQ 1444
Cdd:pfam13868 65 EERKEERKRYRQELEEqiEEREQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKLEKQRQLREeidEFNEEQAEWKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1445 KTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESElkQLRDRAAEAEKLRKLAQD 1524
Cdd:pfam13868 145 LEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERD--ELRAKLYQEEQERKERQK 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774676 1525 EAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEA 1599
Cdd:pfam13868 223 EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK 297
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1772-1927 |
4.32e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.57 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1772 EVAAAQQQRKQledELAKVRSEMDILIQLKTKAEKETmsntEKSKQLLEAEAAKMKDLAEEASRLRAIS---------EE 1842
Cdd:COG2268 213 EIAIAQANREA---EEAELEQEREIETARIAEAEAEL----AKKKAEERREAETARAEAEAAYEIAEANaerevqrqlEI 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1843 AKHQRQI--AEEEAARQRAEAERILKEKLAAISEATRLKTEAE----IALKEKEAENERLRRQAEdEAYQRKALEDQASQ 1916
Cdd:COG2268 286 AEREREIelQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEaeaiRAKGLAEAEGKRALAEAW-NKLGDAAILLMLIE 364
|
170
....*....|.
gi 1988774676 1917 HKQEIEEKIVQ 1927
Cdd:COG2268 365 KLPEIAEAAAK 375
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1414-1685 |
4.34e-06 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 52.77 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1414 AKAEKEAQELKlKMQEEVSKREIAAVDAEKQKTNIQLELQElknlSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLET 1493
Cdd:PRK11637 40 AHASDNRDQLK-SIQQDIAAKEKSVRQQQQQRASLLAQLKK----QEEAISQASRKLRETQNTLNQLNKQIDELNASIAK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1494 TEKQKYTAESELKQLRDRAaeaeklrkLAQDEAEKLRKQVS-EETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLR 1572
Cdd:PRK11637 115 LEQQQAAQERLLAAQLDAA--------FRQGEHTGLQLILSgEESQRGERILAYFGYLNQARQETIAELKQTREELAAQK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1573 MQAEEAERQVKQAEIEKEKQ---IKVAHEAAQKSAAAelqskhmsfaektskLEESLKQEHGAVLQLQQEAERLKKQQED 1649
Cdd:PRK11637 187 AELEEKQSQQKTLLYEQQAQqqkLEQARNERKKTLTG---------------LESSLQKDQQQLSELRANESRLRDSIAR 251
|
250 260 270
....*....|....*....|....*....|....*..
gi 1988774676 1650 AE-NSREEAEKElekwrqkANEALRLRlQAEDEAHKK 1685
Cdd:PRK11637 252 AErEAKARAERE-------AREAARVR-DKQKQAKRK 280
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1750-2099 |
4.60e-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: 53.42 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1750 ADF-DNAEQQRSLLEDELyRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMK- 1827
Cdd:COG3096 271 ADYmRHANERRELSERAL-ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKi 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1828 -----DLAEEASRLRA---ISEEAKHQRQIAEEEAARQRAEAERiLKEKLA---------------------AISEATRL 1878
Cdd:COG3096 350 eryqeDLEELTERLEEqeeVVEEAAEQLAEAEARLEAAEEEVDS-LKSQLAdyqqaldvqqtraiqyqqavqALEKARAL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1879 KTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQ---ASQHKQEIEeKIVQLKKSSEAEMERQKAivDDTLKQrrvVEE 1955
Cdd:COG3096 429 CGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKlsvADAARRQFE-KAYELVCKIAGEVERSQA--WQTARE---LLR 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1956 EIRILKLNFEKASSGKLDL-ELE-----LNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEE 2029
Cdd:COG3096 503 RYRSQQALAQRLQQLRAQLaELEqrlrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSE 582
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 2030 AARQRKAALEELERLRKKAEEARKQKDEADKEAEkQIVVAQQAAQKCSAAEQQV--QSVLAQQIEDSITQKK 2099
Cdd:COG3096 583 LRQQLEQLRARIKELAARAPAWLAAQDALERLRE-QSGEALADSQEVTAAMQQLleREREATVERDELAARK 653
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1706-1881 |
4.66e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1706 RAKAEESALKQKEMAEEELERQRKIAESTAQQKLT-AEQELIRLRADFDNAEQQRsllEDELYRLKNEVaaaQQQRKQLE 1784
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELRER---RNELQKLEKRL---LQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1785 DELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDL-------AEEASR--LRAISEEAKHQRQI----AE 1851
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELerisgltAEEAKEilLEKVEEEARHEAAVlikeIE 179
|
170 180 190
....*....|....*....|....*....|.
gi 1988774676 1852 EEAarqRAEAERILKEKLA-AIseaTRLKTE 1881
Cdd:PRK12704 180 EEA---KEEADKKAKEILAqAI---QRCAAD 204
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1552-1919 |
4.72e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.56 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1552 EAEKEAAKQK-QKALEDLEKLRmQAEEAERQVKQAEIEKEKQIkVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQeh 1630
Cdd:pfam02029 2 EDEEEAARERrRRAREERRRQK-EEEEPSGQVTESVEPNEHNS-YEEDSELKPSGQGGLDEEEAFLDRTAKREERRQK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1631 gavlQLQQEAERLKKQQED--------AENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTlaqeeaekqkeeaeRE 1702
Cdd:pfam02029 78 ----RLQEALERQKEFDPTiadekesvAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIRE--------------KE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1703 AKKRAKAEEsalkQKEMAEEELERQRKIAESTAQQKltaeqelirlraDFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQ 1782
Cdd:pfam02029 140 YQENKWSTE----VRQAEEEGEEEEDKSEEAEEVPT------------ENFAKEEVKDEKIKKEKKVKYESKVFLDQKRG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1783 LEDELAKVRSEMDILIQLKTKAEKETMSNT----EKSKQLLEAEAAKmkdlaEEASRLRAISE----EAKHQRQiaeEEA 1854
Cdd:pfam02029 204 HPEVKSQNGEEEVTKLKVTTKRRQGGLSQSqereEEAEVFLEAEQKL-----EELRRRRQEKEseefEKLRQKQ---QEA 275
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774676 1855 ARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERL------RRQAEDEAYQRKALEDQASQHKQ 1919
Cdd:pfam02029 276 ELELEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRmkeeieRRRAEAAEKRQKLPEDSSSEGKK 346
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1632-1871 |
4.86e-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: 52.46 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1632 AVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEE 1711
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1712 SALKQKEMAEEELERQRKIAESTAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVR 1791
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQ---PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1792 SEMDILIQLKT--KAEKETMSNTEKSKQLLEAEAAkmKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKL 1869
Cdd:COG4942 171 AERAELEALLAelEEERAALEALKAERQKLLARLE--KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
..
gi 1988774676 1870 AA 1871
Cdd:COG4942 249 AA 250
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
67-166 |
4.90e-06 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 48.81 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 67 DRVQKKTFTKWVNKHLIKA--QRHVTDLYEDLRDGHNLISLLEVLSGETLPREKG--RMRFHKLQNVQIALDFLRHRQVK 142
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 1988774676 143 LVNIRNDDIADGNPKLTLGLIWTI 166
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1529-1708 |
5.58e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1529 LRKQVSEetQKKRQAEEELKR-KSEAEKEAAKQKQKAL----EDLEKLRmqaEEAERQVKQAEIE---KEKQIKVAHEA- 1599
Cdd:PRK12704 24 VRKKIAE--AKIKEAEEEAKRiLEEAKKEAEAIKKEALleakEEIHKLR---NEFEKELRERRNElqkLEKRLLQKEENl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1600 AQKSAAAELQSKHMsfaektSKLEESLKQEHGAVLQLQQEAERLKKQQED-----AENSREEAEKE-LEKWRQKA-NEAL 1672
Cdd:PRK12704 99 DRKLELLEKREEEL------EKKEKELEQKQQELEKKEEELEELIEEQLQeleriSGLTAEEAKEIlLEKVEEEArHEAA 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 1988774676 1673 RLRLQAEDEAHKktlaqeeaekqkeeaerEAKKRAK 1708
Cdd:PRK12704 173 VLIKEIEEEAKE-----------------EADKKAK 191
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2527-2632 |
5.63e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2527 EKLIEDEKKRLESQFEEEVKKAKalkDEQERQKQQMEQEKKTLQATMdAALSKQKEAEEEMLRKQKEMQELERQRLE-QE 2605
Cdd:PRK12704 41 KRILEEAKKEAEAIKKEALLEAK---EEIHKLRNEFEKELRERRNEL-QKLEKRLLQKEENLDRKLELLEKREEELEkKE 116
|
90 100
....*....|....*....|....*..
gi 1988774676 2606 RILAEENQKLREKLQQLEDAQKDQHTR 2632
Cdd:PRK12704 117 KELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2279-2493 |
5.66e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2279 DKDSTQKLLAEEAENMRKLaEDAARLSVEAQE-AARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQK 2357
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL-ERAHEALEDAREqIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2358 DLAQEQAQKLLEDKQLMQQRLEEETEEYhksLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATR 2437
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREEL---DELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2438 LHETEIATQEK----MTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNK 2493
Cdd:COG4913 375 LPASAEEFAALraeaAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1452-1862 |
5.88e-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: 52.38 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1452 LQELKNLSEQQIK---DKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEK 1528
Cdd:pfam05622 26 LQEEKNSLQQENKklqERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1529 LRKQVSEETQKK------RQAEEELKrKSEAEKEAAKQKqkaLEDLEKLRMQA---EEAERQVKQAEIEKEKQIKVA--- 1596
Cdd:pfam05622 106 LTSLAEEAQALKdemdilRESSDKVK-KLEATVETYKKK---LEDLGDLRRQVkllEERNAEYMQRTLQLEEELKKAnal 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1597 --HEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQedaENSREeaekelekwrqkANEALRL 1674
Cdd:pfam05622 182 rgQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIER---DTLRE------------TNEELRC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1675 RLQAEDEAHKKTLAQEEAEKQKEEAEREakkrakaeesaLKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDN 1754
Cdd:pfam05622 247 AQLQQAELSQADALLSPSSDPGDNLAAE-----------IMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLED 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1755 AEQQRSLLEDELyRLKNE-VAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEketmsntEKSKQLLEAEAAKMKdlAEEA 1833
Cdd:pfam05622 316 ANRRKNELETQN-RLANQrILELQQQVEELQKALQEQGSKAEDSSLLKQKLE-------EHLEKLHEAQSELQK--KKEQ 385
|
410 420
....*....|....*....|....*....
gi 1988774676 1834 SRLRAISEEAKHQRQIAEEEAARQRAEAE 1862
Cdd:pfam05622 386 IEELEPKQDSNLAQKIDELQEALRKKDED 414
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
649-741 |
6.09e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.71 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 649 HAFVSAATKELMWLNDKEEEEVNFDWSDRNTNMTAKKDNYSGLMRELELREKKVNDIQALGDRLVRDGHPGKKTVESFTA 728
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1988774676 729 ALQTQWSWILQLC 741
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1477-2005 |
6.81e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1477 RTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKlAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKE 1556
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKS-SNLELENIKKQIADDEKSHSITLKEIERLSIEYNN 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1557 AAKQKQKALEDLEKLRMQAEEAERqvkqaeiekekqikvaHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQL 1636
Cdd:PRK01156 230 AMDDYNNLKSALNELSSLEDMKNR----------------YESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1637 QQEAERLKKQQEDAENSREEAEKelekwrqkaneaLRLRLQAEDEAHKKtLAQEEAEKQKEEAEREAKKRAKAEESALKQ 1716
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSN------------IDAEINKYHAIIKK-LSVLQKDYNDYIKKKSRYDDLNNQILELEG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1717 KEMAEEELER-----QRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLED---ELYRLKNEVAAAQQQRKQLEDELA 1788
Cdd:PRK01156 361 YEMDYNSYLKsieslKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEinvKLQDISSKVSSLNQRIRALRENLD 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1789 KVRSEMDILIQLKTKAEKETMSNTEKSKQLLEaeaakmkDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEK 1868
Cdd:PRK01156 441 ELSRNMEMLNGQSVCPVCGTTLGEEKSNHIIN-------HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1869 LAAISEATRLKTEAE-----IALKEKEAENERLRRQAEDEAYQRKALEDQASQHkqeiEEKIVQLKKSSEAEMERQKAIV 1943
Cdd:PRK01156 514 INKSINEYNKIESARadledIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKR----TSWLNALAVISLIDIETNRSRS 589
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774676 1944 DDTLKQRRVVEEEIRILKLNFEKASS----GKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKL 2005
Cdd:PRK01156 590 NEIKKQLNDLESRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNY 655
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1461-1730 |
6.85e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1461 QQIKDKSQQVDEALHSRTKIEEEIRLIRIQLET--TEKQKYTAE-----SELKQLRDRAAEAEKLRKLAQDEAEKLRKQV 1533
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDElnEELKELAEKrdelnAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1534 SEETQKKRQAEEELKRKSEAEKEAA------KQKQKALEDLEKlRMQAE----EAERQV--KQAEIEKE-KQIKVAHEAA 1600
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNkaggsiDKLRKEIERLEW-RQQTEvlspEEEKELveKIKELEKElEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1601 QK-----SAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRlR 1675
Cdd:COG1340 160 EKlkelrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK-E 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774676 1676 LQAEDEAHKKTLAQEeaekqkeeaerEAKKRAKAEESALKQKEMAEEELERQRKI 1730
Cdd:COG1340 239 LRELRKELKKLRKKQ-----------RALKREKEKEELEEKAEEIFEKLKKGEKL 282
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1402-1594 |
6.87e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1402 QKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREiAAVDAEKQKTNIqLELQELKNLSEQQIKDKSQQVDEALHSRTKIE 1481
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAE-AALEEFRQKNGL-VDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1482 EEIRLIRIQLETTEKQKYT--AESELKQLRDRAAEAE-KLRKLAQD------EAEKLRKQVSEETQKKRQAEEELKRKSE 1552
Cdd:COG3206 240 ARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEaELAELSARytpnhpDVIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1988774676 1553 AEKEAAKQKQKALED-LEKLRMQAEE-AERQVKQAEIEKEKQIK 1594
Cdd:COG3206 320 AELEALQAREASLQAqLAQLEARLAElPELEAELRRLEREVEVA 363
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2225-2496 |
6.92e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2225 VLDEelQRLKDEVDDAVKQRGQ---VEEELFKVKVQMEELLKlknkIEEENQRLikkdkdstqkllAEEAENMRKLAEDA 2301
Cdd:COG4913 217 MLEE--PDTFEAADALVEHFDDlerAHEALEDAREQIELLEP----IRELAERY------------AAARERLAELEYLR 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2302 ARLSV-EAQEAARLRQIAEDDLNQQRALAEKmlkEKMQAIQEASRLKAEAEMLQKQKDLAQ----EQAQKLLEDKQLMQQ 2376
Cdd:COG4913 279 AALRLwFAQRRLELLEAELEELRAELARLEA---ELERLEARLDALREELDELEAQIRGNGgdrlEQLEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2377 RLEEETEEYHKSLeveRKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLE 2456
Cdd:COG4913 356 ERERRRARLEALL---AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1988774676 2457 FERLNTSKEADDLRKAIAD-LENEKARLKKEAEELQNKSKE 2496
Cdd:COG4913 433 RRKSNIPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3949-3987 |
7.08e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.40 E-value: 7.08e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1988774676 3949 YLQGTGCIAGVFLESTKERLSIYQAMKKNMIRPGTAFEL 3987
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2464-2623 |
8.32e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2464 KEADDLRKAIADLENEKARLKKEAEELQNKSKEmADAQQKKIEHEktvlqqtfmtekemLLKKEKLIEDEKKRLESqfee 2543
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELED-LEKEIKRLELE--------------IEEVEARIKKYEEQLGN---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2544 eVKKAKALK------DEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLRE 2617
Cdd:COG1579 85 -VRNNKEYEalqkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*.
gi 1988774676 2618 KLQQLE 2623
Cdd:COG1579 164 EREELA 169
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1711-1944 |
8.42e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 8.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1711 ESALKQKEMAEEELERQRKIAEsTAQQKLTA---EQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDEL 1787
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1788 AKVRSEMDILIQLKTKAEKETmsntekskQLLEAEAakmkDLAEEASRLRaiseeAKHQRQIAeeeAARQRAEAERILKE 1867
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRA--------QLAELEA----ELAELSARYT-----PNHPDVIA---LRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1868 KLAAISEAtrLKTEAEiALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIE--EKIVQ--LKKSSEAEMERQKAIV 1943
Cdd:COG3206 310 EAQRILAS--LEAELE-ALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEvaRELYEslLQRLEEARLAEALTVG 386
|
.
gi 1988774676 1944 D 1944
Cdd:COG3206 387 N 387
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1148-1322 |
8.43e-06 |
|
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: 50.14 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1148 VPSDVKEVETYRAKLKKMRTEAEDEQPVFDSLEEElkkasavSDKMVRVHSERDVELdhfRQQLSSLQDRWKAVFTQIDL 1227
Cdd:cd00176 28 YGDDLESVEALLKKHEALEAELAAHEERVEALNEL-------GEQLIEEGHPDAEEI---QERLEELNQRWEELRELAEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1228 RQRELEQLGRQLGYYRESYDwLIRWIADAKQRQEKIQavPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYID 1307
Cdd:cd00176 98 RRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLE 174
|
170
....*....|....*
gi 1988774676 1308 TIKDYELQLVAYKAQ 1322
Cdd:cd00176 175 EGHPDADEEIEEKLE 189
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1275-1923 |
8.57e-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: 52.33 E-value: 8.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1275 KEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKK-----TKLDSASDNIIQEyvtl 1349
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKnkdkiNKLNSDLSKINSE---- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1350 rtryselmtltsqyIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL---KLK 1426
Cdd:TIGR04523 112 --------------IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELeneLNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1427 MQEEVSKREIAAVDAEKQKTNIQLELQELKNLsEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELK 1506
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK-IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1507 QLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAE---EELKRKSEAE-----KEAAKQKQKALEDLEKLRMQAEEA 1578
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKseiSDLNNQKEQDwnkelKSELKNQEKKLEEIQNQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1579 ERQVKQaEIEKEKQikvaheaaqksaaaELQSKHMSFAEKTSKLEESlkqehgavlqlQQEAERLKKQQEDAENSREEAE 1658
Cdd:TIGR04523 337 ISQLNE-QISQLKK--------------ELTNSESENSEKQRELEEK-----------QNEIEKLKKENQSYKQEIKNLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1659 KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK 1738
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1739 LTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMS-------- 1810
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDledelnkd 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1811 NTEKSKQLLEAEaakMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEklaaISEATRLKTEAEIALKEKE 1890
Cdd:TIGR04523 551 DFELKKENLEKE---IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE----IEEKEKKISSLEKELEKAK 623
|
650 660 670
....*....|....*....|....*....|...
gi 1988774676 1891 AENERLRRQAEDEAYQRKALEDQASQHKQEIEE 1923
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1490-1916 |
9.42e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.83 E-value: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1490 QLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLE 1569
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1570 KLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQED 1649
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1650 AENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRK 1729
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1730 IAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDElyrlknevAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETM 1809
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAE--------AVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEAL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1810 SNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEK 1889
Cdd:COG5278 423 ELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLA 502
|
410 420
....*....|....*....|....*..
gi 1988774676 1890 EAENERLRRQAEDEAYQRKALEDQASQ 1916
Cdd:COG5278 503 LALAALLLAAAEAALAAALAAALASAE 529
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1715-2002 |
1.12e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1715 KQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEM 1794
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1795 DILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQ----IAEEEAARQRAEAERILKEKLA 1870
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEelaaLEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1871 AISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQR 1950
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 1951 RVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKL 2002
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2264-2626 |
1.12e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2264 LKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEdaARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEA 2343
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLH--GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2344 SRLKAEAEMLQKQKDLAQEQAQKlleDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSeaqaraeee 2423
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKK---QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVT--------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2424 akKFKKQADKVATRLheteiatQEKMTVVERLEFERLNTSKEADDL---RKAIADLENEKARLKKEAEElQNKSKEMADA 2500
Cdd:TIGR00618 304 --QIEQQAQRIHTEL-------QSKMRSRAKLLMKRAAHVKQQSSIeeqRRLLQTLHSQEIHIRDAHEV-ATSIREISCQ 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2501 QQKKIEHEKTVLQQtfmteKEMLLKKEKLIedekKRLESQFEEEVKKAKALKDEQERQKQQMeqekktlqatmdAALSKQ 2580
Cdd:TIGR00618 374 QHTLTQHIHTLQQQ-----KTTLTQKLQSL----CKELDILQREQATIDTRTSAFRDLQGQL------------AHAKKQ 432
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1988774676 2581 KEAEEEMLRKQKEMQELERQRLEQERILAEE-NQKLREKLQQLEDAQ 2626
Cdd:TIGR00618 433 QELQQRYAELCAAAITCTAQCEKLEKIHLQEsAQSLKEREQQLQTKE 479
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1432-1604 |
1.14e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.70 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1432 SKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDksqqvdEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQlrdr 1511
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKE------EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1512 aaeaeKLRKLaqdeaEKLRKQVSEETQKKRQAEEELKRKseaEKEAAKQKQKALEDLEKL-RMQAEEAERQV-----KQA 1585
Cdd:PRK12704 101 -----KLELL-----EKREEELEKKEKELEQKQQELEKK---EEELEELIEEQLQELERIsGLTAEEAKEILlekveEEA 167
|
170
....*....|....*....
gi 1988774676 1586 EIEKEKQIKVAHEAAQKSA 1604
Cdd:PRK12704 168 RHEAAVLIKEIEEEAKEEA 186
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2034-2489 |
1.15e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2034 RKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSvLAQQIEDSITQKKLKEEYEKAKKLAKE 2113
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2114 AEAAKEKAEReaalLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfeaakraqaeaaalmqkqqadtemAKHKK 2193
Cdd:COG4717 127 LLPLYQELEA----LEAELAELPERLEELEERLEELRELEEELEELEAELA------------------------ELQEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2194 LAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELfkvkvqmeELLKLKNKIEEENQ 2273
Cdd:COG4717 179 LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL--------EAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2274 RLI------------KKDKDSTQK----------LLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRA---- 2327
Cdd:COG4717 251 LLLiaaallallglgGSLLSLILTiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAalgl 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2328 ---LAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKlledKQLMQQRLEEETEEYHKSLEVERKRQlEIMAEAE 2404
Cdd:COG4717 331 ppdLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI----AALLAEAGVEDEEELRAALEQAEEYQ-ELKEELE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2405 RLRLQVSQLSEAQARAEEEAKKF--KKQADKVATRLHETEIATQEKMTVVERLEfERLNTSKEADDLRKAIADLENEKAR 2482
Cdd:COG4717 406 ELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELE-AELEQLEEDGELAELLQELEELKAE 484
|
....*..
gi 1988774676 2483 LKKEAEE 2489
Cdd:COG4717 485 LRELAEE 491
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2527-2635 |
1.16e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2527 EKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTlqatmdaalskqkEAEEEMLRKQKEMQELERQRLEQER 2606
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRN-------------EFEKELRERRNELQKLEKRLLQKEE 96
|
90 100
....*....|....*....|....*....
gi 1988774676 2607 ILAEENQKLREKLQQLEDAQKDQHTRETD 2635
Cdd:PRK12704 97 NLDRKLELLEKREEELEKKEKELEQKQQE 125
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1153-1681 |
1.27e-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: 51.71 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1153 KEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKA--------------SAVSDKM----VRVHSERD---VELDHFRQQL 1211
Cdd:pfam01576 517 RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLqrelealtqqleekAAAYDKLektkNRLQQELDdllVDLDHQRQLV 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1212 SSLQDRWKavftQIDLRQRELEQLGRQLGYYRESydwlirwiADAKQRQEKIQAVPITdsktlkeqlaqekKLLEEIEQN 1291
Cdd:pfam01576 597 SNLEKKQK----KFDQMLAEEKAISARYAEERDR--------AEAEAREKETRALSLA-------------RALEEALEA 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1292 KDKVDECQKYAKAYIDtikdyelQLVAYKAQVEPLVSPLKKTKldSASDNIIQEyvtLRTRYSElmtltsqyikfitdtq 1371
Cdd:pfam01576 652 KEELERTNKQLRAEME-------DLVSSKDDVGKNVHELERSK--RALEQQVEE---MKTQLEE---------------- 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1372 rrLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKA-EKEAQELKLKMQEEVSKREIAAvdAEKQKtnIQL 1450
Cdd:pfam01576 704 --LEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQlVKQVRELEAELEDERKQRAQAV--AAKKK--LEL 777
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1451 ELQELknlsEQQIKDKSQQVDEALHSRTKIE----------EEIRLIR----IQLETTEKQKYTAESELKQLRDRAAEAE 1516
Cdd:pfam01576 778 DLKEL----EAQIDAANKGREEAVKQLKKLQaqmkdlqrelEEARASRdeilAQSKESEKKLKNLEAELLQLQEDLAASE 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1517 KLRKLAQDEAEKLRKQVSEETQKKRQAEEElKRKSEAEkeaAKQKQKALEDLE-KLRMQAEEAERQVKQAE-IEKEKQIK 1594
Cdd:pfam01576 854 RARRQAQQERDELADEIASGASGKSALQDE-KRRLEAR---IAQLEEELEEEQsNTELLNDRLRKSTLQVEqLTTELAAE 929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1595 VAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEH-GAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALr 1673
Cdd:pfam01576 930 RSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFkSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVL- 1008
|
....*...
gi 1988774676 1674 lrLQAEDE 1681
Cdd:pfam01576 1009 --LQVEDE 1014
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2463-2596 |
1.29e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2463 SKEADDLRKAIADLENEKARLKKEAEELQNKSKEmadAQQKKiehektvlqqtfmteKEMLLKKEKLIEDEKK---RLES 2539
Cdd:PRK00409 512 GEDKEKLNELIASLEELERELEQKAEEAEALLKE---AEKLK---------------EELEEKKEKLQEEEDKlleEAEK 573
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 2540 QFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDA-----ALSKQKEAEEEMLRKQKEMQE 2596
Cdd:PRK00409 574 EAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELiearkRLNKANEKKEKKKKKQKEKQE 635
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1371-1585 |
1.31e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1371 QRRLDDEEKAAEKLKAEERKKMAEMQaelDKQKQLAEAHAKAIAKAEKEAQElKLKMqeevSKREIAAVDAEKQktniQL 1450
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELE---EKKEKLQEEEDKLLEEAEKEAQQ-AIKE----AKKEADEIIKELR----QL 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1451 ELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYtaeSELKQlrdraaEAEKLRKLAQDEAeklr 1530
Cdd:PRK00409 597 QKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEVKY---LSLGQ------KGEVLSIPDDKEA---- 663
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 1531 kQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEK------LR-MQAEEAERQVKQA 1585
Cdd:PRK00409 664 -IVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTvsleldLRgMRYEEALERLDKY 724
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2282-2625 |
1.33e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2282 STQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQ-QRALAekmLKEKMQAIQE-----ASRLkAEAEMLQK 2355
Cdd:COG3096 296 GARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLvQTALR---QQEKIERYQEdleelTERL-EEQEEVVE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2356 QKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQ------LEIMAEAERLrLQVSQLSEAQARAEEEAkkFKK 2429
Cdd:COG3096 372 EAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiqyqqaVQALEKARAL-CGLPDLTPENAEDYLAA--FRA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2430 QADKV-------ATRLHETEIATQE---KMTVVERL--EFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEM 2497
Cdd:COG3096 449 KEQQAteevlelEQKLSVADAARRQfekAYELVCKIagEVERSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2498 AdaQQKKIEHEKTVLQQTFMTEkemlLKKEKLIEDEKKRLESQFEE---EVKKAKALKDEQERQKQQMEQEKKTLQA--- 2571
Cdd:COG3096 529 R--QQQNAERLLEEFCQRIGQQ----LDAAEELEELLAELEAQLEEleeQAAEAVEQRSELRQQLEQLRARIKELAArap 602
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774676 2572 ---TMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDA 2625
Cdd:COG3096 603 awlAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQ 659
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1459-2005 |
1.33e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1459 SEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQdEAEKLRKQVSEETQ 1538
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIK-TAESDLSMELEKNN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1539 KKRQAEEELKRkseAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAeiekEKQIKVAHEAAQKsaAAELQSKHMSFAEK 1618
Cdd:PRK01156 274 YYKELEERHMK---IINDPVYKNRNYINDYFKYKNDIENKKQILSNI----DAEINKYHAIIKK--LSVLQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1619 TSKLEE------SLKQEHGAVLQLQQEAERLKKQqedaensREEAEKELEKWRQKANEALRLRLQAEDE--AHKKTLAQE 1690
Cdd:PRK01156 345 KSRYDDlnnqilELEGYEMDYNSYLKSIESLKKK-------IEEYSKNIERMSAFISEILKIQEIDPDAikKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1691 EAEKQKEEAEREAKKRakaeesALKQKEMaeeELERQRKIAESTAQQKLT----AEQELIRLRADFDNaeqQRSLLEDEL 1766
Cdd:PRK01156 418 LQDISSKVSSLNQRIR------ALRENLD---ELSRNMEMLNGQSVCPVCgttlGEEKSNHIINHYNE---KKSRLEEKI 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1767 YRLKNEVAAAQQQRKQLE--------DELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRA 1838
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKkrkeylesEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1839 ISEE---AKHQRQIAEEEAARQRAEaerilkEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAY----QRKALE 1911
Cdd:PRK01156 566 KRTSwlnALAVISLIDIETNRSRSN------EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANnlnnKYNEIQ 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1912 DQASQhKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRvVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQS 1991
Cdd:PRK01156 640 ENKIL-IEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIND-IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDR 717
|
570
....*....|....
gi 1988774676 1992 KIRAEEEAEKLRKL 2005
Cdd:PRK01156 718 INDINETLESMKKI 731
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2313-2640 |
1.33e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 51.55 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2313 RLRQIAEDDLNQQRALAEKMLKEKMQAIQE---ASRLKAEAEMLQKQKDLAqEQAQKLLEDKQLMQQRLEEETEEY---- 2385
Cdd:NF033838 92 KLSDIKTEYLYELNVLKEKSEAELTSKTKKeldAAFEQFKKDTLEPGKKVA-EATKKVEEAEKKAKDQKEEDRRNYptnt 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2386 HKSLEVERKRQLEIMAEAERlrlqvsQLSEAQARAEEEAKKFKKQADKVATRlheteiatQEKMTVVERLEFERlntsKE 2465
Cdd:NF033838 171 YKTLELEIAESDVEVKKAEL------ELVKEEAKEPRDEEKIKQAKAKVESK--------KAEATRLEKIKTDR----EK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2466 ADDLRKAIADLENEKARLKKEAEELQNKSKEMA--------DAQQKKIEHEKT----VLQQTFMTEKemlLKKEKLI-ED 2532
Cdd:NF033838 233 AEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAkrgvlgepATPDKKENDAKSsdssVGEETLPSPS---LKPEKKVaEA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2533 EKKRLESQfeeevKKAKALKDEQERQKQQMEQekKTLQATMDAALSKQKEAEEEMLRKQ-KEMQELERQRLEQERILAEE 2611
Cdd:NF033838 310 EKKVEEAK-----KKAKDQKEEDRRNYPTNTY--KTLELEIAESDVKVKEAELELVKEEaKEPRNEEKIKQAKAKVESKK 382
|
330 340 350
....*....|....*....|....*....|...
gi 1988774676 2612 NQKLR-EKLQQLEDAQKDQHTR---ETDKVLHK 2640
Cdd:NF033838 383 AEATRlEKIKTDRKKAEEEAKRkaaEEDKVKEK 415
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
69-170 |
1.41e-05 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 47.41 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 69 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRF----HKLQNVQIALDFLRHRQVKLV 144
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 1988774676 145 NIRNDDIADGNPKLTLGLIWTIILHF 170
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1603-1862 |
1.53e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1603 SAAAELQSKHMSFAEKTSKLEESLKQehgaVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAlrlrlQAEDEA 1682
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-----EAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1683 HKKTLaqeeaekqkeeaereaKKRAKAE-------------------ESALKQKEMAEEELERQRKIAESTAQQKLTAEQ 1743
Cdd:COG3883 84 RREEL----------------GERARALyrsggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1744 ELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEA 1823
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 1988774676 1824 AKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAE 1862
Cdd:COG3883 228 AAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1354-1611 |
1.67e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 51.37 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1354 SELMTLTSQYIKFITD---TQRRLDDEEKAaeklkAEERKKMaemqaELDKQKQLAeahakAIAKAEKEAQELKLKMQEE 1430
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERA-----EADRQRL-----EQEKQQQLA-----AISGSQSQLESTDQNALET 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1431 VSKREIAAVDAEKQKTNIQLE--LQELKNLSEQQ-----------------IKDKSQ-QVDEA-LHSRTKIEEeirliri 1489
Cdd:NF012221 1603 NGQAQRDAILEESRAVTKELTtlAQGLDALDSQAtyagesgdqwrnpfaggLLDRVQeQLDDAkKISGKQLAD------- 1675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1490 qlettEKQKYTAesELKQLRDRAAEAEKlrklAQDEAEKLRKQVSEETQKKR-QAEeelKRKSEA---EKEAAKQKQKAL 1565
Cdd:NF012221 1676 -----AKQRHVD--NQQKVKDAVAKSEA----GVAQGEQNQANAEQDIDDAKaDAE---KRKDDAlakQNEAQQAESDAN 1741
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1988774676 1566 EDLEKLRMQaeeAERQVKQAEIEKEKqikvaheaAQKSAAAELQSK 1611
Cdd:NF012221 1742 AAANDAQSR---GEQDASAAENKANQ--------AQADAKGAKQDE 1776
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
65-173 |
1.68e-05 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 46.90 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 65 ERDRVQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEV---------LSGETLPREKGRMRfhKLQNVQIALDF 135
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1988774676 136 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQVS 173
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
2306-2613 |
1.70e-05 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 51.49 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2306 VEAQEAARLRQIAEDDLNQQRAlaekmlkekmQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLE--DKQLMQQR--LEEE 2381
Cdd:pfam15818 10 LEALEELRMRREAETQYEEQIG----------KIIVETQELKWQKETLQNQKETLAKQHKEAMAvfKKQLQMKMcaLEEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2382 TEEYHKSLEVERKrqlEIMAEAERLR-LQVSQLSEAQARAEEEAKKfkkQADKVATRLHETEIATQEK--MTVVERLEFE 2458
Cdd:pfam15818 80 KGKYQLATEIKEK---EIEGLKETLKaLQVSKYSLQKKVSEMEQKL---QLHLLAKEDHHKQLNEIEKyyATITGQFGLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2459 RLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEhEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLE 2538
Cdd:pfam15818 154 KENHGKLEQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIK-SKVTCQYKMGEENINLTIKEQKFQELQERLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2539 SQFEEEVKKAKALKDEQERQK---------QQMEQEKKTLQATMDAALSKQKEaEEEMLRKQKEMQElERQRLEQERILA 2609
Cdd:pfam15818 233 MELELNKKINEEITHIQEEKQdiiisfqhmQQLLQQQTQANTEMEAELKALKE-NNQTLERDNELQR-EKVKENEEKFLN 310
|
....
gi 1988774676 2610 EENQ 2613
Cdd:pfam15818 311 LQNE 314
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1371-1596 |
1.72e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 50.14 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1371 QRRLDDEEKAAEKLK----AEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEevskreiaavdAEKQKT 1446
Cdd:pfam09787 17 ARILQSKEKLIASLKegsgVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE-----------LEAQQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1447 NIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRiqlETTEKQKYTAESELKQLrdraaeaeklrklaQDEA 1526
Cdd:pfam09787 86 EEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLE---EELRRSKATLQSRIKDR--------------EAEI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774676 1527 EKLRKQVSEETQKKRQaEEELKRKSEAEKEAAKQKQKALEDL--EK--LRMQAEEAERQVKQAEIEKEKQIKVA 1596
Cdd:pfam09787 149 EKLRNQLTSKSQSSSS-QSELENRLHQLTETLIQKQTMLEALstEKnsLVLQLERMEQQIKELQGEGSNGTSIN 221
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1376-1628 |
1.75e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.11 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1376 DEEKAAEKLKAEERKKMAEMQAELDKQKQLAEahakaiAKAEKEAQELKLKMQEEvskreiaavdaekqktniqLELqel 1455
Cdd:pfam15709 329 EQEKASRDRLRAERAEMRRLEVERKRREQEEQ------RRLQQEQLERAEKMREE-------------------LEL--- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1456 knlsEQQikdksqqvdealhsrtKIEEEIRLIRIQLEttEKQKYTAESELKQLRDRAAEAEKLRKlaqdEAEKLRKQVSE 1535
Cdd:pfam15709 381 ----EQQ----------------RRFEEIRLRKQRLE--EERQRQEEEERKQRLQLQAAQERARQ----QQEEFRRKLQE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1536 ETQKKRQAEEElkrKSEAEKEAAKQKQKALEDLEKLRMQAEEAER----QVKQAEIEKEKQikvahEAAQKSAAAELQSK 1611
Cdd:pfam15709 435 LQRKKQQEEAE---RAEAEKQRQKELEMQLAEEQKRLMEMAEEERleyqRQKQEAEEKARL-----EAEERRQKEEEAAR 506
|
250
....*....|....*..
gi 1988774676 1612 hMSFAEKTSKLEESLKQ 1628
Cdd:pfam15709 507 -LALEEAMKQAQEQARQ 522
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2338-2626 |
1.82e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2338 QAIQEASRLKAEAEMLqKQKDLAQEQAQKLLEDKQLMQQRLEEET--EEYHKSLEVERKRQLEIM---------AEAERL 2406
Cdd:COG3206 75 SLSASDSPLETQIEIL-KSRPVLERVVDKLNLDEDPLGEEASREAaiERLRKNLTVEPVKGSNVIeisytspdpELAAAV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2407 ------RLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEkmtvverleFER----LNTSKEADDLRKAIADL 2476
Cdd:COG3206 154 analaeAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE---------FRQknglVDLSEEAKLLLQQLSEL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2477 ENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEkemLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQE 2556
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ---LRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774676 2557 RQKQQMEQEKKTLQATMDAALSKQKeAEEEMLRKQ--------KEMQELERQRLEQERILAEENQKLREKLQQLEDAQ 2626
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAELEALQ-AREASLQAQlaqlearlAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2298-2509 |
1.83e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2298 AEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQR 2377
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2378 LEEETEEYhksleVERKRQLEIMAEAERLRLQVSQ------------LSEAQARAEEEAKKFKKQADKVATRLHETEIAT 2445
Cdd:COG4942 99 LEAQKEEL-----AELLRALYRLGRQPPLALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774676 2446 QEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEK 2509
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1481-1671 |
1.95e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1481 EEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQ 1560
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1561 KQKALEDLEKL--------------RMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSkhmsFAEKTSKLEESL 1626
Cdd:COG3883 95 LYRSGGSVSYLdvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1988774676 1627 KQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEA 1671
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2452-2641 |
1.97e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2452 VERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMAD-------AQQKKIEHEKTVLQQTFMTEKEMLL 2524
Cdd:PHA02562 236 IEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2525 KKEKLIEDEKKRLESQFEEEVKKAKALKDeqerqkqQMEQEKKTLQATMDAALskqkeaeeemlRKQKEMQELERQRLEQ 2604
Cdd:PHA02562 316 EKLDTAIDELEEIMDEFNEQSKKLLELKN-------KISTNKQSLITLVDKAK-----------KVKAAIEELQAEFVDN 377
|
170 180 190
....*....|....*....|....*....|....*..
gi 1988774676 2605 ERILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKD 2641
Cdd:PHA02562 378 AEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1254-1570 |
2.03e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.07 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1254 ADAKQRQEKI--QAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQ-VEPLVSPL 1330
Cdd:PRK11281 39 ADVQAQLDALnkQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDnDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1331 KKT-------KLDSASDNIIQEYVTLRTRYSELMTLTSQYI---KFITDTQRR-------LDDEEKAAEKLKAEERKKMA 1393
Cdd:PRK11281 119 STLslrqlesRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraqAALYANSQRlqqirnlLKGGKVGGKALRPSQRVLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1394 EMQAELDKQ-------------------KQLAEAHAKaIAKAEKEAQEL-------KLKMQEEVSKREIAAVDAEKQKTN 1447
Cdd:PRK11281 199 AEQALLNAQndlqrkslegntqlqdllqKQRDYLTAR-IQRLEHQLQLLqeainskRLTLSEKTVQEAQSQDEAARIQAN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1448 --IQLEL--------------QELKNLSEQQIKDKsQQVDEALHSRTKIEEEIR-------LIRIQLEttEKQKYTAESE 1504
Cdd:PRK11281 278 plVAQELeinlqlsqrllkatEKLNTLTQQNLRVK-NWLDRLTQSERNIKEQISvlkgsllLSRILYQ--QQQALPSADL 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774676 1505 LKQLRDRAAeaeKLRkLAQDEAEKLRKQVSE-----ETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEK 1570
Cdd:PRK11281 355 IEGLADRIA---DLR-LEQFEINQQRDALFQpdayiDKLEAGHKSEVTDEVRDALLQLLDERRELLDQLNK 421
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1536-1853 |
2.17e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 50.36 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1536 ETQKKRQAE--EELKRKSEAEKEAAKQKQKALEDLEKlrmqaeeAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHM 1613
Cdd:PRK07735 8 EDLKKEAARraKEEARKRLVAKHGAEISKLEEENREK-------EKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1614 SFAEKTSklEESLKQEHGAVLQLQQEAERLKKQQEdaENSREEAEKELEKWRQKANEALRLRLQAedeahkktlaqeeae 1693
Cdd:PRK07735 81 GTEEVTE--EEKAKAKAKAAAAAKAKAAALAKQKR--EGTEEVTEEEKAAAKAKAAAAAKAKAAA--------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1694 kqkeeaerEAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQqrslleDELYRLKNEV 1773
Cdd:PRK07735 142 --------LAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTE------EEKAKAKAKA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1774 AAAQQQRKQledELAKvrsemdiliQLKTKAEKETMSNTEKSKQlleAEAAKMKdlAEEASRLRAISEEAKHQRQIAEEE 1853
Cdd:PRK07735 208 AAAAKAKAA---ALAK---------QKASQGNGDSGDEDAKAKA---IAAAKAK--AAAAARAKTKGAEGKKEEEPKQEE 270
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1154-2064 |
2.19e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.21 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1154 EVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRW-KAVFTQIDLRQREL 1232
Cdd:TIGR01612 780 ELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFlNKVDKFINFENNCK 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1233 EQLGRQlgyyRESYDWLIRWI-ADAKQRQEKIQAVPITDSKTLkeqLAQEKKLLEEIEQNKD---KVDECQKYAKAYIDT 1308
Cdd:TIGR01612 860 EKIDSE----HEQFAELTNKIkAEISDDKLNDYEKKFNDSKSL---INEINKSIEEEYQNINtlkKVDEYIKICENTKES 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1309 IKDYELQLVAYKAQVEPLVSPLKKTkldsasdNIIQEyvtlrtryselmTLTSQYIKFITDTQRRLDDEEKAAEkLKAEE 1388
Cdd:TIGR01612 933 IEKFHNKQNILKEILNKNIDTIKES-------NLIEK------------SYKDKFDNTLIDKINELDKAFKDAS-LNDYE 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1389 RKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAqelklkmQEEVSKREIAAVDAEKQKTNIQLELQ-ELKNLSEQQIKDKS 1467
Cdd:TIGR01612 993 AKNNELIKYFNDLKANLGKNKENMLYHQFDEK-------EKATNDIEQKIEDANKNIPNIEIAIHtSIYNIIDEIEKEIG 1065
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1468 QQVdEALHSRTKIEEEIRLIRIQlETTEKQKYTAESELKQlRDRAAEAEKLRKLAQDeaeklRKQVSEETQKKRQAEEEL 1547
Cdd:TIGR01612 1066 KNI-ELLNKEILEEAEINITNFN-EIKEKLKHYNFDDFGK-EENIKYADEINKIKDD-----IKNLDQKIDHHIKALEEI 1137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1548 KRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAE-----IEKEKQI-----KVAHEAAQ----KSAAAELQSKHM 1613
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIEnivtkIDKKKNIydeikKLLNEIAEiekdKTSLEEVKGINL 1217
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1614 SFAEKTSKL------EESLKQEH--GAVLQLQQEAERLKKQQEDAENsreeaEKELEKWRQKANEALRLRlQAEDEAHKK 1685
Cdd:TIGR01612 1218 SYGKNLGKLflekidEEKKKSEHmiKAMEAYIEDLDEIKEKSPEIEN-----EMGIEMDIKAEMETFNIS-HDDDKDHHI 1291
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1686 TLAQEEAEKQKEEAEREAKKRAKAEESALK--QKEMAEEELERQRKIAE-STAQQKLTAEQELIRL---RADFDNAEQQR 1759
Cdd:TIGR01612 1292 ISKKHDENISDIREKSLKIIEDFSEESDINdiKKELQKNLLDAQKHNSDiNLYLNEIANIYNILKLnkiKKIIDEVKEYT 1371
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1760 SLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKM-------KDLAEE 1832
Cdd:TIGR01612 1372 KEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIdtyfknaDENNEN 1451
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1833 ASRLRAISEEAKHQRQ-IAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEaENERLRRQAEDEA------Y 1905
Cdd:TIGR01612 1452 VLLLFKNIEMADNKSQhILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIE-KNKELFEQYKKDVtellnkY 1530
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1906 QRKALEDQASQHKQEIEEKIVQLKKSS-----EAEMERQKaiVDDTLKQRRVVEEEIRilklNFEKASSGKLDLELEL-- 1978
Cdd:TIGR01612 1531 SALAIKNKFAKTKKDSEIIIKEIKDAHkkfilEAEKSEQK--IKEIKKEKFRIEDDAA----KNDKSNKAAIDIQLSLen 1604
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1979 --NKLKNIAD-ETQQSKIRAEEEA--EKLRKLALEEEKRRreaeekvkkiAAAEEEAARQRKAALEELERLRKKAEEARK 2053
Cdd:TIGR01612 1605 feNKFLKISDiKKKINDCLKETESieKKISSFSIDSQDTE----------LKENGDNLNSLQEFLESLKDQKKNIEDKKK 1674
|
970
....*....|.
gi 1988774676 2054 QKDEADKEAEK 2064
Cdd:TIGR01612 1675 ELDELDSEIEK 1685
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1819-2004 |
2.20e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1819 LEAEAAKMKDLAEEASRLRAISEEAKHQR----QIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENE 1894
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIellePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1895 RLRRQAEDEAY---QRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKL--------- 1962
Cdd:COG4913 303 ELARLEAELERleaRLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLplpasaeef 382
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1988774676 1963 --NFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRK 2004
Cdd:COG4913 383 aaLRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
70-167 |
2.22e-05 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 47.35 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 70 QKKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 136
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1988774676 137 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 167
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQII 135
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1641-1885 |
2.38e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.26 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1641 ERLKKQQEDAENSREEAEKELEKWRQKANealrlRLQAEDEAHKKtlaqeeaekqkeeaeREAKKRAKAEESALKQKEMA 1720
Cdd:COG2268 192 RKIAEIIRDARIAEAEAERETEIAIAQAN-----REAEEAELEQE---------------REIETARIAEAEAELAKKKA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1721 EEELERQRKIAESTAQQKLtaeqelirlradfdnaeqqrslledelyrlknevaAAQQQRKQLEDELAKVRSEMDILIQL 1800
Cdd:COG2268 252 EERREAETARAEAEAAYEI-----------------------------------AEANAEREVQRQLEIAEREREIELQE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1801 KTKAEKEtmsNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKhqrqiAEEEAARQRAEAERILKEklAAISEAtRLKT 1880
Cdd:COG2268 297 KEAEREE---AELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGL-----AEAEGKRALAEAWNKLGD--AAILLM-LIEK 365
|
....*
gi 1988774676 1881 EAEIA 1885
Cdd:COG2268 366 LPEIA 370
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2480-2652 |
2.45e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.34 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2480 KARLKKEAEELQNKSKEMADAQQKKIEhektvLQQTFMTEkEMLLKKEKLiEDEKKRLEsqfEEEVKKAKALKDEQERQK 2559
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELE-----LEQQRRFE-EIRLRKQRL-EEERQRQE---EEERKQRLQLQAAQERAR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2560 QQMEQEKKTLQatmDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAE--ENQKLREKLQQLEDAQKDQHTRETDKV 2637
Cdd:pfam15709 423 QQQEEFRRKLQ---ELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEmaEEERLEYQRQKQEAEEKARLEAEERRQ 499
|
170
....*....|....*
gi 1988774676 2638 LHKDIIHLTTIETTK 2652
Cdd:pfam15709 500 KEEEAARLALEEAMK 514
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1750-2201 |
2.45e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.68 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1750 ADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKE---TMSNTEKSKQLLEAeaakM 1826
Cdd:COG5278 79 EPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEaalALVRSGEGKALMDE----I 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1827 KDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQ 1906
Cdd:COG5278 155 RARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALEL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1907 RKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAD 1986
Cdd:COG5278 235 LAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1987 ETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQI 2066
Cdd:COG5278 315 AAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2067 VVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEA 2146
Cdd:COG5278 395 IAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAAL 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774676 2147 ANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQ 2201
Cdd:COG5278 475 AALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAE 529
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2195-2366 |
2.85e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2195 AEQTLkQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELL------KLKNKI 2268
Cdd:COG3206 194 AEAAL-EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLqspviqQLRAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2269 EEENQRLIKKDKDST------QKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQE 2342
Cdd:COG3206 273 AELEAELAELSARYTpnhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
170 180 190
....*....|....*....|....*....|..
gi 1988774676 2343 ASRLKAEAE--------MLQKQKDLAQEQAQK 2366
Cdd:COG3206 353 LRRLEREVEvarelyesLLQRLEEARLAEALT 384
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2260-2634 |
2.99e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 50.57 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2260 ELLKLKNKIEEENQRLIKKDKDSTQ-KLLAEEAENMRKLAEDAARL----------SVEaQEAARLRQIAEDDLNQQRAL 2328
Cdd:PRK10246 455 EQTQRNAALNEMRQRYKEKTQQLADvKTICEQEARIKDLEAQRAQLqagqpcplcgSTS-HPAVEAYQALEPGVNQSRLD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2329 AekMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDkqlmQQRLEEETEEYHKSLEVERKRQLEI---MAEAER 2405
Cdd:PRK10246 534 A--LEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQE----EQALTQQWQAVCASLNITLQPQDDIqpwLDAQEE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2406 LRLQVSQLSeaqaraeeeaKKFKKQADKVATRLHETEIATQekmtvverLEFERLNTSKEADDLRKAIADLENEKARL-- 2483
Cdd:PRK10246 608 HERQLRLLS----------QRHELQGQIAAHNQQIIQYQQQ--------IEQRQQQLLTALAGYALTLPQEDEEASWLat 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2484 -KKEAEELQNKSKEMADAQQKKieHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQfeeevkkAKALKDEQERQKQQM 2562
Cdd:PRK10246 670 rQQEAQSWQQRQNELTALQNRI--QQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQ-------CLSLHSQLQTLQQQD 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2563 EQEKKTL---QATMDAALSKQ----KEA-------EEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKD 2628
Cdd:PRK10246 741 VLEAQRLqkaQAQFDTALQASvfddQQAflaalldEETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDL 820
|
....*.
gi 1988774676 2629 QHTRET 2634
Cdd:PRK10246 821 TVTVEQ 826
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1479-1629 |
3.08e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1479 KIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKS------- 1551
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyea 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1552 -EAEKEAAKQKQKALEDLEK-LRMQAEEAERQVK--QAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLK 1627
Cdd:COG1579 94 lQKEIESLKRRISDLEDEILeLMERIEELEEELAelEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
..
gi 1988774676 1628 QE 1629
Cdd:COG1579 174 PE 175
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2178-2631 |
3.09e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.12 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2178 LMQKQQADTEMAKHKKLAEQTLKQKFqveqeLTKVKLKLDETDKQKSVLDEELQRLKDEVDD----AVKQRGQVEEELFK 2253
Cdd:pfam05557 59 LLEKREAEAEEALREQAELNRLKKKY-----LEALNKKLNEKESQLADAREVISCLKNELSElrrqIQRAELELQSTNSE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2254 VKVQMEELLKLKNKIEEENQRliKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEA----ARLRQIAEDDLNQQRALA 2329
Cdd:pfam05557 134 LEELQERLDLLKAKASEAEQL--RQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVknskSELARIPELEKELERLRE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2330 E-KMLKEkmqAIQEASRLKAEAEMLQKQKDlAQEQAQKLLEDKQLMQQRLEEETEEYHK----------SLEVERKRQLE 2398
Cdd:pfam05557 212 HnKHLNE---NIENKLLLKEEVEDLKRKLE-REEKYREEAATLELEKEKLEQELQSWVKlaqdtglnlrSPEDLSRRIEQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2399 IMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLEN 2478
Cdd:pfam05557 288 LQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDK 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2479 E---------KARLKKEAEEL----QNKSKEMaDAQQKKIEHEKTVL-QQTFMTEKEMLLKKEKLIEDEKKRLESQFEEE 2544
Cdd:pfam05557 368 EltmsnyspqLLERIEEAEDMtqkmQAHNEEM-EAQLSVAEEELGGYkQQAQTLERELQALRQQESLADPSYSKEEVDSL 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2545 VKKAKALKDEQERQKQQ-----MEQEKKTLQATMDAALSKQkeaeeeMLRKQKEMQELERQRLEQERILAEENQKLREKL 2619
Cdd:pfam05557 447 RRKLETLELERQRLREQkneleMELERRCLQGDYDPKKTKV------LHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLL 520
|
490
....*....|..
gi 1988774676 2620 QQLEDAQKDQHT 2631
Cdd:pfam05557 521 KKLEDDLEQVLR 532
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4157-4185 |
3.14e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 3.14e-05
10 20
....*....|....*....|....*....
gi 1988774676 4157 VRKRRVVIVDPETGKEMTVYEAYRKGLID 4185
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2524-2628 |
3.15e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.68 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2524 LKKEKLIEDEKKRLESQFEEevkkAKALKDEQERQKQQMEQEKKTLQAtmdaALSKQKEAEEEMLRKQKEMQELERQRLE 2603
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQ----TLALLDKIDRQKEETEQLKQQLAQ----APAKLRQAQAELEALKDDNDEETRETLS 119
|
90 100
....*....|....*....|....*
gi 1988774676 2604 QERiLAEENQKLREKLQQLEDAQKD 2628
Cdd:PRK11281 120 TLS-LRQLESRLAQTLDQLQNAQND 143
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2307-2629 |
3.41e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.87 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2307 EAQEAAR-LRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDkqlMQQRLEEETEEY 2385
Cdd:pfam02029 3 DEEEAAReRRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDR---TAKREERRQKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2386 HKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKV---ATRLHETEIATQEKMTVVERLEfERLNT 2462
Cdd:pfam02029 80 QEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYkeeETEIREKEYQENKWSTEVRQAE-EEGEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2463 SKEADDLRKAI--ADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQ 2540
Cdd:pfam02029 159 EEDKSEEAEEVptENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2541 FEEEVKKAKALKDEQERQKQQME-QEKKTLQatmdaalSKQKEAE---EEMLRKQKE---MQELERQRLEQERILA---- 2609
Cdd:pfam02029 239 EAEVFLEAEQKLEELRRRRQEKEsEEFEKLR-------QKQQEAElelEELKKKREErrkLLEEEEQRRKQEEAERklre 311
|
330 340
....*....|....*....|...
gi 1988774676 2610 -EENQKLREKLQ--QLEDAQKDQ 2629
Cdd:pfam02029 312 eEEKRRMKEEIErrRAEAAEKRQ 334
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1162-1668 |
3.41e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1162 LKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQlgrqlgy 1241
Cdd:TIGR04523 234 IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1242 yresyDWlirwiadakqrqekiqavpitdSKTLKEQLAQEKKLLEEIEqnkDKVDECQKYAKAYIDTIKDyelqlvayka 1321
Cdd:TIGR04523 307 -----DW----------------------NKELKSELKNQEKKLEEIQ---NQISQNNKIISQLNEQISQ---------- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1322 qveplvspLKKTKLDSASDNiiqeyvtlRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKkmaemqaeLDK 1401
Cdd:TIGR04523 347 --------LKKELTNSESEN--------SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK--------IQN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1402 QKQLAEAHAKAIAKAEKEAQEL-----KLKMQEEVSKREIAavDAEKQKTNIQLELQELKNLSEQQikdkSQQVDEalhs 1476
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLekeieRLKETIIKNNSEIK--DLTNQDSVKELIIKNLDNTRESL----ETQLKV---- 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1477 rtkIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKlrklaqdEAEKLRKQVSEETQKKRQAEEElkrKSEAEKE 1556
Cdd:TIGR04523 473 ---LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEE-------KVKDLTKKISSLKEKIEKLESE---KKEKESK 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1557 AAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQehgaVLQL 1636
Cdd:TIGR04523 540 ISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK----ISSL 615
|
490 500 510
....*....|....*....|....*....|..
gi 1988774676 1637 QQEAERLKKQQEDAENSREEAEKELEKWRQKA 1668
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2315-2623 |
3.70e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.15 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2315 RQIAEDDLNQQRALAEKMLKEKMQAIQEasRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERK 2394
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEE--EEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2395 RQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKvatrlheteiatQEKMTVVERLEFERLNTSKEADdlrkaia 2474
Cdd:pfam13868 110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE------------EEREEDERILEYLKEKAEREEE------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2475 dLENEKARLKKEAEELQNKskemADAQQKKIEHEKTvlqqtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDE 2554
Cdd:pfam13868 171 -REAEREEIEEEKEREIAR----LRAQQEKAQDEKA--------ERDELRAKLYQEEQERKERQKEREEAEKKARQRQEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2555 QERQKQQMEQEKKTLQATMDaalsKQKEAEEEMLRKQKEMQELERQRLEQERI-----------LAEENQKLREKLQQLE 2623
Cdd:pfam13868 238 QQAREEQIELKERRLAEEAE----REEEEFERMLRKQAEDEEIEQEEAEKRRMkrlehrrelekQIEEREEQRAAEREEE 313
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1477-1570 |
3.71e-05 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 46.28 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1477 RTKIEEEIRLIRIQLETTEKQKYTAESELKQLRdraAEAEKLRKLAQDEAEKLRKQVseetqkKRQAEEELKR-KSEAEK 1555
Cdd:cd06503 32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEAR---AEAQEIIEEARKEAEKIKEEI------LAEAKEEAERiLEQAKA 102
|
90
....*....|....*
gi 1988774676 1556 EAAKQKQKALEDLEK 1570
Cdd:cd06503 103 EIEQEKEKALAELRK 117
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1388-2602 |
3.93e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.44 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1388 ERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELK---LKMQEEVSK--REIAAVDAEKQKTN-IQLELQE-LKNLSe 1460
Cdd:TIGR01612 535 KAKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENedsIHLEKEIKDlfDKYLEIDDEIIYINkLKLELKEkIKNIS- 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1461 qqikDKSQQVDEALHSRTKIEEEIRLIRiqlETTEKQKYTAESELKQlRDRAAEAEK--LRKLAQDEAEKLRKQVSEETQ 1538
Cdd:TIGR01612 614 ----DKNEYIKKAIDLKKIIENNNAYID---ELAKISPYQVPEHLKN-KDKIYSTIKseLSKIYEDDIDALYNELSSIVK 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1539 KKRQAEEELKRKSEAEKEAAKQKQKALEDleklrMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSaaaelqskHMSFAEK 1618
Cdd:TIGR01612 686 ENAIDNTEDKAKLDDLKSKIDKEYDKIQN-----METATVELHLSNIENKKNELLDIIVEIKKHI--------HGEINKD 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1619 TSKLEESLKQEhgavlqlqqeaerlKKQQEDAENSREEAEKELEKWRQKANEalrLRLQAEDEAHKKTLAQEEAEKQKEE 1698
Cdd:TIGR01612 753 LNKILEDFKNK--------------EKELSNKINDYAKEKDELNKYKSKISE---IKNHYNDQINIDNIKDEDAKQNYDK 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1699 AEREAKKRAKAEESALK----QKEMAEEELERQRKIA--ESTAQQKLTAEQELI-----RLRADFdnAEQQRSLLEDEL- 1766
Cdd:TIGR01612 816 SKEYIKTISIKEDEIFKiineMKFMKDDFLNKVDKFInfENNCKEKIDSEHEQFaeltnKIKAEI--SDDKLNDYEKKFn 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1767 --YRLKNEVAAAQQQRKQLEDELAKVRSEMDIliqlkTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLraiseEAK 1844
Cdd:TIGR01612 894 dsKSLINEINKSIEEEYQNINTLKKVDEYIKI-----CENTKESIEKFHNKQNILKEILNKNIDTIKESNLI-----EKS 963
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1845 HQRQIaEEEAARQRAEAERILKEklAAISEATRLKTEAeiaLKEKEAENERLRRQAEDEAYQRKaleDQASQHKQEIEEK 1924
Cdd:TIGR01612 964 YKDKF-DNTLIDKINELDKAFKD--ASLNDYEAKNNEL---IKYFNDLKANLGKNKENMLYHQF---DEKEKATNDIEQK 1034
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1925 IVQLKKS-SEAEMERQKAIVDDTLKQRRVVEEEIRILKLN-FEKASSGKLDLELELNKLK--NIADETQQSKIRAEEEae 2000
Cdd:TIGR01612 1035 IEDANKNiPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEiLEEAEINITNFNEIKEKLKhyNFDDFGKEENIKYADE-- 1112
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2001 klrklaleeekrrreaeekVKKIAAAEEEAARQRKAALEELERLRKKAE----EARKQKDEADKEAEKQIvvaqqAAQKC 2076
Cdd:TIGR01612 1113 -------------------INKIKDDIKNLDQKIDHHIKALEEIKKKSEnyidEIKAQINDLEDVADKAI-----SNDDP 1168
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2077 SAAEQQVQSVLAQ-----QIEDSItQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAK 2151
Cdd:TIGR01612 1169 EEIEKKIENIVTKidkkkNIYDEI-KKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEA 1247
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2152 AQEDAERLRKEAEfeaaKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQ--ELTKVKLKLDETDKQKSVLDEE 2229
Cdd:TIGR01612 1248 YIEDLDEIKEKSP----EIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENisDIREKSLKIIEDFSEESDINDI 1323
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2230 LQRLKDEVDDAVKQRGQVEE------------ELFKVKVQMEELLKLKNKIEEENQRlIKKDKDSTQKLLAEEAEN---- 2293
Cdd:TIGR01612 1324 KKELQKNLLDAQKHNSDINLylneianiynilKLNKIKKIIDEVKEYTKEIEENNKN-IKDELDKSEKLIKKIKDDinle 1402
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2294 ------------------MRKLAEDAAR-LSVEAQEAARLRQIAEDDLNQQRALAE-KMLKEKMQAIQEASR-------- 2345
Cdd:TIGR01612 1403 eckskiestlddkdidecIKKIKELKNHiLSEESNIDTYFKNADENNENVLLLFKNiEMADNKSQHILKIKKdnatndhd 1482
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2346 -----LKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLE--------IMAEAERLRLQVSQ 2412
Cdd:TIGR01612 1483 fnineLKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAktkkdseiIIKEIKDAHKKFIL 1562
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2413 LSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSkeadDLRKAIADLENEKARLKKEAEELQn 2492
Cdd:TIGR01612 1563 EAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKIS----DIKKKINDCLKETESIEKKISSFS- 1637
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2493 kskemADAQQKKIEHEKTVLQ--QTFMtekEMLLKKEKLIEDEKKRLESqfeeevkkakaLKDEQERQKQQMEQEKKTLQ 2570
Cdd:TIGR01612 1638 -----IDSQDTELKENGDNLNslQEFL---ESLKDQKKNIEDKKKELDE-----------LDSEIEKIEIDVDQHKKNYE 1698
|
1290 1300 1310
....*....|....*....|....*....|..
gi 1988774676 2571 ATMDAALSKQKEAEEEMLRKQKEMQELERQRL 2602
Cdd:TIGR01612 1699 IGIIEKIKEIAIANKEEIESIKELIEPTIENL 1730
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1369-1662 |
4.24e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 49.59 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1369 DTQRRLDD-EEKAAEKLKAEERKKMAEMQAElDKQKQLAEAHAKAIAKAEKEAQELklkmqEEVSKREIAAVDAEKQKTN 1447
Cdd:PRK07735 2 DPEKDLEDlKKEAARRAKEEARKRLVAKHGA-EISKLEEENREKEKALPKNDDMTI-----EEAKRRAAAAAKAKAAALA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1448 IQLELQELKNLSEQQIKDKSQQVDEAlhsrtkieeeirliRIQLETTEKQKYTAESELKQlRDRAAEAEKLRKLAQDEAE 1527
Cdd:PRK07735 76 KQKREGTEEVTEEEKAKAKAKAAAAA--------------KAKAAALAKQKREGTEEVTE-EEKAAAKAKAAAAAKAKAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1528 KLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVaheAAQKSAAAE 1607
Cdd:PRK07735 141 ALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAA---AAAKAKAAA 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774676 1608 LQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKkqQEDAENSREEAEKELE 1662
Cdd:PRK07735 218 LAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAK--TKGAEGKKEEEPKQEE 270
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1475-1646 |
4.51e-05 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 49.66 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1475 HSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAE-AEKLRKlAQDEAEKLRKQVSEETQKKRQAEEELkrkSEA 1553
Cdd:pfam10168 554 LAREEIQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKlAEKYEE-IKDKQEKLMRRCKKVLQRLNSQLPVL---SDA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1554 EKEAAKQkqkaledLEKLRMQAEEAERQVKQAEIEKEKQIKvaHEAAQKSAAaelQSKHMSFAEKTSK-LEESLKQEHGA 1632
Cdd:pfam10168 630 EREMKKE-------LETINEQLKHLANAIKQAKKKMNYQRY--QIAKSQSIR---KKSSLSLSEKQRKtIKEILKQLGSE 697
|
170
....*....|....
gi 1988774676 1633 VLQLQQEAERLKKQ 1646
Cdd:pfam10168 698 IDELIKQVKDINKH 711
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
2530-2664 |
4.60e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.86 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2530 IEDEKKRLeSQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATmdaaLSKQKEAEEEMLRKQKEMQELER--QRLEQERI 2607
Cdd:COG2433 408 LTEEEEEI-RRLEEQVERLEAEVEELEAELEEKDERIERLERE----LSEARSEERREIRKDREISRLDReiERLERELE 482
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774676 2608 -LAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDIIHLTTIETTKTVYnGQNVGDVV 2664
Cdd:COG2433 483 eERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEY-GLKEGDVV 539
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4024-4055 |
4.89e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.89e-05
10 20 30
....*....|....*....|....*....|..
gi 1988774676 4024 KLLSAERAVTGYRDPYTGKTISLFQAMKKGLI 4055
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1367-1564 |
4.96e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1367 ITDTQRRLDDEEKAAEKLKAEER---KKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEvsKREIAAVDAEK 1443
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAaleRRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ--KEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1444 QKTNIQLELQELKNLSE-QQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDR---------AA 1513
Cdd:COG4942 114 YRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEleeeraaleAL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 1514 EAEKLRKLAQDEAEKlrKQVSEETQKKRQAEEELKRK-SEAEKEAAKQKQKA 1564
Cdd:COG4942 194 KAERQKLLARLEKEL--AELAAELAELQQEAEELEALiARLEAEAAAAAERT 243
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1376-1674 |
4.99e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.45 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1376 DEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQEL 1455
Cdd:PRK04778 105 HEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1456 KNLSEQ----QIKDKSQQVDEALHSRTKIEEEIRLIRIQLETT---------------EKQKY-----TAESELKQLRDR 1511
Cdd:PRK04778 185 VELTESgdyvEAREILDQLEEELAALEQIMEEIPELLKELQTElpdqlqelkagyrelVEEGYhldhlDIEKEIQDLKEQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1512 AAEAEK-LRKLAQDEAEKLRKQVSEETQkkrQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQ----AEEAERqVKQA- 1585
Cdd:PRK04778 265 IDENLAlLEELDLDEAEEKNEEIQERID---QLYDILEREVKARKYVEKNSDTLPDFLEHAKEQnkelKEEIDR-VKQSy 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1586 -----EIEK----EKQIKvAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEhgAVLQLQQE--AERLkKQQEDAENsr 1654
Cdd:PRK04778 341 tlnesELESvrqlEKQLE-SLEKQYDEITERIAEQEIAYSELQEELEEILKQL--EEIEKEQEklSEML-QGLRKDEL-- 414
|
330 340
....*....|....*....|
gi 1988774676 1655 eEAEKELEKWRQKANEALRL 1674
Cdd:PRK04778 415 -EAREKLERYRNKLHEIKRY 433
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1371-1686 |
5.00e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 48.88 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1371 QRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKqLAEAHAKaiAKAEKEAQELKLKMQEEvskreiaavdaekqktniql 1450
Cdd:pfam15558 78 ERRRADRREKQVIEKESRWREQAEDQENQRQEK-LERARQE--AEQRKQCQEQRLKEKEE-------------------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1451 ELQELKNLSEQQIKDKSQQvdeALHSRTKIEEEIRLIRIQLETTEKQKYTAeseLKQLRDRAAEAEKLRKLAQDEAEKLR 1530
Cdd:pfam15558 135 ELQALREQNSLQLQERLEE---ACHKRQLKEREEQKKVQENNLSELLNHQA---RKVLVDCQAKAEELLRRLSLEQSLQR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1531 KQVSEETQKKRQAeEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQikVAHEAAQKSAA----- 1605
Cdd:pfam15558 209 SQENYEQLVEERH-RELREKAQKEEEQFQRAKWRAEEKEEERQEHKEALAELADRKIQQARQ--VAHKTVQDKAQrarel 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1606 -AELQSKHMSFAEKTSKLEESLKQEhgavlqlqqEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHK 1684
Cdd:pfam15558 286 nLEREKNHHILKLKVEKEEKCHREG---------IKEAIKKKEQRSEQISREKEATLEEARKTARASFHMREKVREETNN 356
|
..
gi 1988774676 1685 KT 1686
Cdd:pfam15558 357 RT 358
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3122-3158 |
5.18e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 5.18e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1988774676 3122 KLLSAERAVTGYRDPYTGKTVSLFQAMKKDLIPKEQG 3158
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2197-2621 |
5.37e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 49.26 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2197 QTLKQKFQVEQELTKVKlkldetdkqksvldEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEEL-LKLKNKIEEENQrl 2275
Cdd:pfam05701 32 QTVERRKLVELELEKVQ--------------EEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELkLNLERAQTEEAQ-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2276 IKKDKDstqklLAE-EAENMRKLAEDAARLSVEAQ-EAARLRQIAeddlnqqrALAE-KMLKEKMQAIQEasrlkaEAEM 2352
Cdd:pfam05701 96 AKQDSE-----LAKlRVEEMEQGIADEASVAAKAQlEVAKARHAA--------AVAElKSVKEELESLRK------EYAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2353 LQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEY---HKSLEVERKRQLEimAEAERLRLQVSqlseaqaraeeeakkfkK 2429
Cdd:pfam05701 157 LVSERDIAIKRAEEAVSASKEIEKTVEELTIELiatKESLESAHAAHLE--AEEHRIGAALA-----------------R 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2430 QADKVAtrlHETEIATQEKmtvverlEFERLNtskeaDDLRKAiadlENEKARLKKEAEELQNKSKEMADAQQKKIEHEK 2509
Cdd:pfam05701 218 EQDKLN---WEKELKQAEE-------ELQRLN-----QQLLSA----KDLKSKLETASALLLDLKAELAAYMESKLKEEA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2510 TVLQQTFMTE---KEMLLKKEKLIEDEKKRLESQfEEEVK----KAKALKDEQERQK------QQ-----------MEQE 2565
Cdd:pfam05701 279 DGEGNEKKTStsiQAALASAKKELEEVKANIEKA-KDEVNclrvAAASLRSELEKEKaelaslRQregmasiavssLEAE 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2566 KKTLQATMDAALSKQKEAEEEMLRKQKEMQElERQRLEQERILA----EENQKLREKLQQ 2621
Cdd:pfam05701 358 LNRTKSEIALVQAKEKEAREKMVELPKQLQQ-AAQEAEEAKSLAqaarEELRKAKEEAEQ 416
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1229-1961 |
5.38e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1229 QRELEQLGRQLGYYRESYDWLIRWIADAKQRQEKIQavpitdskTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDT 1308
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQ--------TRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEE 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1309 IKDYELQLVAYKAQVEplvsplkkTKLDSASDniiqeyvtLRTRYSELMTLtsqyIKFITDTQRRLDDEEKAAEKLKAEE 1388
Cdd:PRK04863 447 FQAKEQEATEELLSLE--------QKLSVAQA--------AHSQFEQAYQL----VRKIAGEVSRSEAWDVARELLRRLR 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1389 RKKMaemqaeLDKQKQLAEAHAKAIAKAEKEAQELKlKMQEEVSKREIAAVDAEKqktniqlELQELKNLSEQQIKDKSQ 1468
Cdd:PRK04863 507 EQRH------LAEQLQQLRMRLSELEQRLRQQQRAE-RLLAEFCKRLGKNLDDED-------ELEQLQEELEARLESLSE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1469 QVDEALHSRTKIEEEIRLIRIQ---LETTEKQKYTAESELKQLRDRAAEA----EKLRKLAQDEAEKLRK---QVSEETQ 1538
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARiqrLAARAPAWLAAQDALARLREQSGEEfedsQDVTEYMQQLLEREREltvERDELAA 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1539 KKRQAEEELKRKSEAEK-------------------------------------------------EAAKQKQKALEDL- 1568
Cdd:PRK04863 653 RKQALDEEIERLSQPGGsedprlnalaerfggvllseiyddvsledapyfsalygparhaivvpdlSDAAEQLAGLEDCp 732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1569 EKLRM-------------QAEEAERQV------KQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESlkqe 1629
Cdd:PRK04863 733 EDLYLiegdpdsfddsvfSVEELEKAVvvkiadRQWRYSRFPEVPLFGRAAREKRIEQLRAEREELAERYATLSFD---- 808
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1630 hgavlqlQQEAERLKKQQEDAENS------REEAEKELEKWRQKANEALRlRLQAEDEAHKKTLAQEEAEKQKEEAEREA 1703
Cdd:PRK04863 809 -------VQKLQRLHQAFSRFIGShlavafEADPEAELRQLNRRRVELER-ALADHESQEQQQRSQLEQAKEGLSALNRL 880
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1704 KKRAK--AEESALKQKEMAEEELERQRKIAESTAQQKLTA---EQELIRLRADFDNAEQqrslledelyrLKNEVAAAQQ 1778
Cdd:PRK04863 881 LPRLNllADETLADRVEEIREQLDEAEEAKRFVQQHGNALaqlEPIVSVLQSDPEQFEQ-----------LKQDYQQAQQ 949
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1779 QRKQLedelakvrsemdiliQLKTKAEKETMSNTEkskQLLEAEAAKMkdLAEEA---SRLRAISEEAKHQRQIAEEEAA 1855
Cdd:PRK04863 950 TQRDA---------------KQQAFALTEVVQRRA---HFSYEDAAEM--LAKNSdlnEKLRQRLEQAEQERTRAREQLR 1009
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1856 RQRAEAERILKEKLAAISEATRLKTEaeiaLKEKEAENERLRRQAEDEAyqrkalEDQASQHKQEIEEKIV--QLKKSS- 1932
Cdd:PRK04863 1010 QAQAQLAQYNQVLASLKSSYDAKRQM----LQELKQELQDLGVPADSGA------EERARARRDELHARLSanRSRRNQl 1079
|
810 820
....*....|....*....|....*....
gi 1988774676 1933 EAEMERQKAIVDDTLKQRRVVEEEIRILK 1961
Cdd:PRK04863 1080 EKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3492-3527 |
5.77e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 5.77e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1988774676 3492 LLEAQIVSGGIIDPVKSHRVPTDVAYQKNILSRDIA 3527
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1863-2629 |
5.85e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1863 RILKEKLAAISEATRLKTEAEIALKEKEAENERL---RRQAEDEAYQRKALEDQ-------------ASQHKQEIEEKIV 1926
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDyqaasdhlnlvqtALRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1927 QLKKSSEAeMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKiRAEEEAEKLRKLA 2006
Cdd:PRK04863 356 DLEELEER-LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAV-QALERAKQLCGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2007 LEEEkrrreaeekvkkiaaaeeeaarqrKAALEELERLRKKAEEArkqkDEADKEAEKQIVVAQQAAQKCSAAEQQVQSv 2086
Cdd:PRK04863 434 DLTA------------------------DNAEDWLEEFQAKEQEA----TEELLSLEQKLSVAQAAHSQFEQAYQLVRK- 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2087 LAQQIEDSITQKKLKEeyekakklAKEAEAAKEKAEREAALLRQQAEEAERQktaaeeeaanqAKAQEDAERLRKEAEFE 2166
Cdd:PRK04863 485 IAGEVSRSEAWDVARE--------LLRRLREQRHLAEQLQQLRMRLSELEQR-----------LRQQQRAERLLAEFCKR 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2167 AAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSV---LDEELQRLKDEVDDAVKQ 2243
Cdd:PRK04863 546 LGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFED 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2244 RGQVEEelfkvkvQMEELLKLKNKIEEENQRLikkdkdstqkllaeeAENMRKLAEDAARLS-VEAQEAARLRQIAE--- 2319
Cdd:PRK04863 626 SQDVTE-------YMQQLLERERELTVERDEL---------------AARKQALDEEIERLSqPGGSEDPRLNALAErfg 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2320 --------DDLNQQRA-LAEKMLKEKMQAIQeASRLKAEAEMLQKQKDlaqeqaqkLLEDKQLMQ---QRLEE---ETEE 2384
Cdd:PRK04863 684 gvllseiyDDVSLEDApYFSALYGPARHAIV-VPDLSDAAEQLAGLED--------CPEDLYLIEgdpDSFDDsvfSVEE 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2385 YHKSLEVErkrqleimaEAERlRLQVSQLSEA----QARAEEEAKKFKKQADKVATRLHETEIATQEkmtvVERL--EFE 2458
Cdd:PRK04863 755 LEKAVVVK---------IADR-QWRYSRFPEVplfgRAAREKRIEQLRAEREELAERYATLSFDVQK----LQRLhqAFS 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2459 R-----LNTSKEAD------DLRKAIADLENEKARLKKEAEELQN---KSKEMADAQQKKIEHEKTVLQQTFMTEKEMLl 2524
Cdd:PRK04863 821 RfigshLAVAFEADpeaelrQLNRRRVELERALADHESQEQQQRSqleQAKEGLSALNRLLPRLNLLADETLADRVEEI- 899
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2525 kKEKLIEDEK-----KRLESQFEEEVKKAKALKDEQE------RQKQQMEQEKKTLQATMDA---------ALSKQKEAe 2584
Cdd:PRK04863 900 -REQLDEAEEakrfvQQHGNALAQLEPIVSVLQSDPEqfeqlkQDYQQAQQTQRDAKQQAFAltevvqrraHFSYEDAA- 977
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1988774676 2585 eEMLRKQKEMQELERQRLEQ-ERILAEENQKLREKLQQLedAQKDQ 2629
Cdd:PRK04863 978 -EMLAKNSDLNEKLRQRLEQaEQERTRAREQLRQAQAQL--AQYNQ 1020
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1636-2089 |
5.99e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 49.26 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1636 LQQEAERLKKQQEDAENSREEAEKELEKWRqKANEALRLRL---QAEDEAHKK--TLAQEEAEKQKEEAEREAKKRAKAE 1710
Cdd:pfam05701 47 VQEEIPEYKKQSEAAEAAKAQVLEELESTK-RLIEELKLNLeraQTEEAQAKQdsELAKLRVEEMEQGIADEASVAAKAQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1711 --------ESALKQKEMAEEELERQRKIAESTAQQK-----------------------LTAE-----QELIRLRADFDN 1754
Cdd:pfam05701 126 levakarhAAAVAELKSVKEELESLRKEYASLVSERdiaikraeeavsaskeiektveeLTIEliatkESLESAHAAHLE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1755 AEQQR------------------SLLEDELYRLKNEVAAAQQQRKQLE---DELAKVRSEMDILIQLKTKAEKETMSNTE 1813
Cdd:pfam05701 206 AEEHRigaalareqdklnwekelKQAEEELQRLNQQLLSAKDLKSKLEtasALLLDLKAELAAYMESKLKEEADGEGNEK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1814 KSKQLLEAEAAKMKDLAEEasrLRAISEEAKHQRQIAEEEAARQRAEAErilKEKlAAISEATRLKTEAEIALKEKEAEN 1893
Cdd:pfam05701 286 KTSTSIQAALASAKKELEE---VKANIEKAKDEVNCLRVAAASLRSELE---KEK-AELASLRQREGMASIAVSSLEAEL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1894 ERLRrqAEDEAYQRKALEDQasqhkqeieEKIVQL-KKSSEAEMErqkaiVDDTLKQRRVVEEEIRILKLNFEKASSGKL 1972
Cdd:pfam05701 359 NRTK--SEIALVQAKEKEAR---------EKMVELpKQLQQAAQE-----AEEAKSLAQAAREELRKAKEEAEQAKAAAS 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1973 DLELELnklkniadETQQSKIRAEEEAEKLRKLALEEEKRRREAEEkvkkiAAAEEEAARQRKAALEELERLRKKAEEAR 2052
Cdd:pfam05701 423 TVESRL--------EAVLKEIEAAKASEKLALAAIKALQESESSAE-----STNQEDSPRGVTLSLEEYYELSKRAHEAE 489
|
490 500 510
....*....|....*....|....*....|....*..
gi 1988774676 2053 KQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQ 2089
Cdd:pfam05701 490 ELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEE 526
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1632-1960 |
6.04e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.76 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1632 AVLQLQQEAERLKKQQEDAENSREEAEKELEkwRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEE 1711
Cdd:pfam13868 22 KERDAQIAEKKRIKAEEKEEERRLDEMMEEE--RERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1712 SALKQKEMAEEELERQRKIAESTAQQKLTAE--QELIRLRADFDNAEQQRSLLEDElyRLKNEVAAAQQQRKQLEDELAK 1789
Cdd:pfam13868 100 REQMDEIVERIQEEDQAEAEEKLEKQRQLREeiDEFNEEQAEWKELEKEEEREEDE--RILEYLKEKAEREEEREAEREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1790 VRSEMDILIQLKTKAEKETMsnteksKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKL 1869
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQ------DEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1870 AAIsEATRLKTEAEIALKEKEAENERLRRQAEDeayQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQ 1949
Cdd:pfam13868 252 LAE-EAEREEEEFERMLRKQAEDEEIEQEEAEK---RRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAER 327
|
330
....*....|.
gi 1988774676 1950 RRVVEEEIRIL 1960
Cdd:pfam13868 328 RERIEEERQKK 338
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1378-1625 |
6.36e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.10 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1378 EKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIqlelqelkn 1457
Cdd:pfam02029 137 EKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEV--------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1458 lseqqikdKSQQVDEALHSRTKIEEEIRLIRIQLETTE---KQKYTAESELKQLRDRAAEAEklrklaQDEAEKLRkqvs 1534
Cdd:pfam02029 208 --------KSQNGEEEVTKLKVTTKRRQGGLSQSQEREeeaEVFLEAEQKLEELRRRRQEKE------SEEFEKLR---- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1535 eetQKKRQAE---EELKRKSEaekeaakQKQKALEDlEKLRMQAEEAERQVKqaEIEKEKQIKvaheaaqksaaAELQSK 1611
Cdd:pfam02029 270 ---QKQQEAElelEELKKKRE-------ERRKLLEE-EEQRRKQEEAERKLR--EEEEKRRMK-----------EEIERR 325
|
250
....*....|....
gi 1988774676 1612 HMSFAEKTSKLEES 1625
Cdd:pfam02029 326 RAEAAEKRQKLPED 339
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3416-3449 |
6.56e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 6.56e-05
10 20 30
....*....|....*....|....*....|....
gi 1988774676 3416 LLEAQAASGFIVDPVRNQCLSVDEAVKSGVVGPE 3449
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1482-1629 |
6.71e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 48.85 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1482 EEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKE--AAK 1559
Cdd:pfam05262 199 DMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKqvAEN 278
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1560 QKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSaAAELQSKHMSFAEKTSKLEESLKQE 1629
Cdd:pfam05262 279 QKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDK-ELEAQKKREPVAEDLQKTKPQVEAQ 347
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1701-1924 |
6.92e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 49.45 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1701 REAKKRAKAEESALKQKEMAEE-----ELERQRKIAE-STAQQKLTAEQELirlrADFDNAEQQRSLLEDELYRLKNEVA 1774
Cdd:NF012221 1548 SKHAKQDDAAQNALADKERAEAdrqrlEQEKQQQLAAiSGSQSQLESTDQN----ALETNGQAQRDAILEESRAVTKELT 1623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1775 AAQQQRKQLEDE-------------------LAKVRSEMDiliqlktKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASR 1835
Cdd:NF012221 1624 TLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLD-------DAKKISGKQLADAKQRHVDNQQKVKDAVAKSEA 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1836 LRAISEeakHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAledQAS 1915
Cdd:NF012221 1697 GVAQGE---QNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQA---DAK 1770
|
....*....
gi 1988774676 1916 QHKQEIEEK 1924
Cdd:NF012221 1771 GAKQDESDK 1779
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
70-167 |
7.69e-05 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 45.82 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 70 QKKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 136
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1988774676 137 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 167
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 135
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
71-136 |
7.93e-05 |
|
first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409070 Cd Length: 106 Bit Score: 44.57 E-value: 7.93e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 71 KKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREK----GRMRFHKLQNVQIALDFL 136
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1436-1657 |
7.96e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1436 IAAVDAEKQKTNIQLELQELKNLSEQ---QIKDKSQQVDEAlhsrtkiEEEIRLIRIQLETTEKQKYTAESELKQLRDRA 1512
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAaqaELDALQAELEEL-------NEEYNELQAELEALQAEIDKLQAEIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1513 AEA-EKLRKLAQDEAEK------------------------LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQkalED 1567
Cdd:COG3883 82 EERrEELGERARALYRSggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKL---AE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1568 LEKLRMQAEEAERQVKQAEIEKEKQIkvaheaaqksaaAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQ 1647
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALL------------AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
250
....*....|
gi 1988774676 1648 EDAENSREEA 1657
Cdd:COG3883 227 AAAAAAAAAA 236
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
1393-1791 |
7.96e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 49.20 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1393 AEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDE 1472
Cdd:COG4995 76 LLLALALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1473 ALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSE 1552
Cdd:COG4995 156 AAAAAAAAALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1553 AEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSkhmsfAEKTSKLEESLKQEHGA 1632
Cdd:COG4995 236 LLLALLALAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALAL-----AAAALALALLLAAAAAA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1633 VLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEES 1712
Cdd:COG4995 311 ALAALALLLLAALLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALL 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1713 ALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQ-QRSLLEDELYRLkneVAAAQQQRKQLEDELAKVR 1791
Cdd:COG4995 391 AALLLLAAALLALAAAQLLRLLLAALALLLALAAYAAARLALLALiEYIILPDRLYAF---VQLYQLLIAPIEAELPGIK 467
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1501-1660 |
7.99e-05 |
|
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: 46.98 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1501 AESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQA----EEELKRKSEAEKEAAKQKQKALE-DLEKLRMQA 1575
Cdd:pfam04012 34 MQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAAltkgNEELAREALAEKKSLEKQAEALEtQLAQQRSAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1576 EEAERQV-----KQAEIEKEKQIKVAHEAAQKSAAAELQSKH-MSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQED 1649
Cdd:pfam04012 114 EQLRKQLaaletKIQQLKAKKNLLKARLKAAKAQEAVQTSLGsLSTSSATDSFERIEEKIEEREARADAAAELASAVDLD 193
|
170
....*....|.
gi 1988774676 1650 AENSREEAEKE 1660
Cdd:pfam04012 194 AKLEQAGIQME 204
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1819-1949 |
8.02e-05 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 45.93 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1819 LEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAarqRAEAERILKEklaAISEATRLKTEaeiALKEKEAENERLRR 1898
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEA---RAEAAEIIAE---ARKEAEAIAEE---AKAEAEAEAERIIA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774676 1899 QAEDEAYQ-----RKALEDQASQHKQEIEEKIVQlkksSEAEMERQKAIVDDTLKQ 1949
Cdd:COG0711 100 QAEAEIEQerakaLAELRAEVADLAVAIAEKILG----KELDAAAQAALVDRFIAE 151
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1770-1948 |
8.11e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 49.25 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1770 KNEVAAAQQQRKQLEDElAKVRSEmdiLIQLKTKAEKEtmsntEKSKQLLEAEAakmKDLAEEAS-RLRAISEeakhqrq 1848
Cdd:PTZ00491 662 KSQEAAARHQAELLEQE-ARGRLE---RQKMHDKAKAE-----EQRTKLLELQA---ESAAVESSgQSRAEAL------- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1849 iAEEEAARQRAEAErilkeklaaiSEATRLKTEAEIALKEKEAENERLRRQAEdeayqrkaLEDQASQHKQEIEEKivql 1928
Cdd:PTZ00491 723 -AEAEARLIEAEAE----------VEQAELRAKALRIEAEAELEKLRKRQELE--------LEYEQAQNELEIAKA---- 779
|
170 180
....*....|....*....|....
gi 1988774676 1929 KKSSEAEMERQKAIVD----DTLK 1948
Cdd:PTZ00491 780 KELADIEATKFERIVEalgrETLI 803
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1495-1663 |
8.30e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1495 EKQKYTAESELKQLRDRA-AEAEKLRKL----AQDEAEKLRKQVSEETQKKR-----------QAEEELKRKSeaekEAA 1558
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAkKEAEAIKKEalleAKEEIHKLRNEFEKELRERRnelqklekrllQKEENLDRKL----ELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1559 KQKQKALEDLEKlRMQAEEAERQVKQAEIEK--EKQIKVAHEAAQksaaaelqskhMSFAEKTSKLEESLKQEhgavlqL 1636
Cdd:PRK12704 106 EKREEELEKKEK-ELEQKQQELEKKEEELEEliEEQLQELERISG-----------LTAEEAKEILLEKVEEE------A 167
|
170 180
....*....|....*....|....*..
gi 1988774676 1637 QQEAERLKKQQEdaENSREEAEKELEK 1663
Cdd:PRK12704 168 RHEAAVLIKEIE--EEAKEEADKKAKE 192
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
178-291 |
8.54e-05 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 44.80 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 178 DIQVNGQSEDMTAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVA 256
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQ---NKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKpVTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|....*
gi 1988774676 257 EKDLGVTRLLDPEDVDVPHPDEKSIITYVSSLYDA 291
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1575-2049 |
8.69e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1575 AEEAERQVKQA-EIEKEKQIKVAHEAAQKSAAAELQSKhmsfAEKTSKLEESLKQEHGAV---LQLQQEAERLKKQQEDA 1650
Cdd:PRK04863 278 ANERRVHLEEAlELRRELYTSRRQLAAEQYRLVEMARE----LAELNEAESDLEQDYQAAsdhLNLVQTALRQQEKIERY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1651 ENSREEAEKELEkwrqkanEALRLRLQAEDEAhkktlaqeeaekqkeeAEREAKKRAkAEESALK-QKEMA--EEELERQ 1727
Cdd:PRK04863 354 QADLEELEERLE-------EQNEVVEEADEQQ----------------EENEARAEA-AEEEVDElKSQLAdyQQALDVQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1728 --RKIAESTAQQKLTAEQELIRLRA-DFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKA 1804
Cdd:PRK04863 410 qtRAIQYQQAVQALERAKQLCGLPDlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEV 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1805 EKETMSNTEKSkqlLEAEAAKMKDLAEEASRLRAISEEAKhQRQIAEEEAARQRAEAERILKEKLAAISEATRLkteaei 1884
Cdd:PRK04863 490 SRSEAWDVARE---LLRRLREQRHLAEQLQQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQL------ 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1885 aLKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEE--KIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKL 1962
Cdd:PRK04863 560 -QEELEARLESLSESVSEARERRMALRQQLEQLQARIQRlaARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLE 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1963 NfEKassgkldlELELNKlkniaDETQQSKIRAEEEAEKLRklaleeekrrreaeekvkkiaaaeeeaarQRKAAleELE 2042
Cdd:PRK04863 639 R-ER--------ELTVER-----DELAARKQALDEEIERLS-----------------------------QPGGS--EDP 673
|
....*..
gi 1988774676 2043 RLRKKAE 2049
Cdd:PRK04863 674 RLNALAE 680
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1507-1763 |
1.04e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1507 QLRDRAAEAEKLRKLAQDEAEKLRKQVSEetqkKRQAEEELKRKS-----EAEKEAAKQKQKALED-LEKLRMQAEEAER 1580
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEE----AEAALEEFRQKNglvdlSEEAKLLLQQLSELESqLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1581 QVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKkqqedaensreeaeke 1660
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALR---------------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1661 lekwRQKANEALRLRLQAEDEAhkktlaqeeaekqkeeaereakKRAKAEESALKQkemaeeELERQRKIAESTAQQklt 1740
Cdd:COG3206 305 ----AQLQQEAQRILASLEAEL----------------------EALQAREASLQA------QLAQLEARLAELPEL--- 349
|
250 260
....*....|....*....|....
gi 1988774676 1741 aEQELIRLRADFDNAEQQ-RSLLE 1763
Cdd:COG3206 350 -EAELRRLEREVEVARELyESLLQ 372
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1440-1853 |
1.09e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.92 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1440 DAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESEL--KQLRDRAAEAEK 1517
Cdd:COG5022 814 SYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELaeRQLQELKIDVKS 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1518 LRKLA----QDEAE--KLRKQVSEETQKKRQA-------EEELKRKSEAEKEAAKQKQKaLEDLEKLRMQ-------AEE 1577
Cdd:COG5022 894 ISSLKlvnlELESEiiELKKSLSSDLIENLEFkteliarLKKLLNNIDLEEGPSIEYVK-LPELNKLHEVesklketSEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1578 AERQVKQAEIEKEKQIKVAHEAAQ-KSAAAELQSKHMSFAEKTSkleeSLKQEHGAVLQLQQEAERLKkqQEDAENSREE 1656
Cdd:COG5022 973 YEDLLKKSTILVREGNKANSELKNfKKELAELSKQYGALQESTK----QLKELPVEVAELQSASKIIS--SESTELSILK 1046
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1657 AEKELEKWRQKANEALRLRLQAEDEAhKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQ 1736
Cdd:COG5022 1047 PLQKLKGLLLLENNQLQARYKALKLR-RENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKL 1125
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1737 QKLTAEQELIRLRADF-DNAEQQRSLLEDELYRLKNEvaaaqqqrKQLEDELAKVRsemdiLIQLKTKAEKETMSNTEKS 1815
Cdd:COG5022 1126 NLLQEISKFLSQLVNTlEPVFQKLSVLQLELDGLFWE--------ANLEALPSPPP-----FAALSEKRLYQSALYDEKS 1192
|
410 420 430
....*....|....*....|....*....|....*...
gi 1988774676 1816 KQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEE 1853
Cdd:COG5022 1193 KLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEG 1230
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1529-1817 |
1.09e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 48.36 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1529 LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAE-EAERQVKQAEIEKEKqIKVAHEAAQKSAAAE 1607
Cdd:pfam15964 319 VRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELErQKERLEKELASQQEK-RAQEKEALRKEMKKE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1608 ---LQSKHMSFAEKTSKLEESL----KQEHGAVLQLQQEAERLKKQQED--------------AENSREEAEKELEKWRQ 1666
Cdd:pfam15964 398 reeLGATMLALSQNVAQLEAQVekvtREKNSLVSQLEEAQKQLASQEMDvtkvcgemryqlnqTKMKKDEAEKEHREYRT 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1667 KANEALRLrlqAEDEAHKKTLAQEEAEKQKEEAEREAkkrAKAEESALKQKEMAEE--------ELER---QRKIAESTA 1735
Cdd:pfam15964 478 KTGRQLEI---KDQEIEKLGLELSESKQRLEQAQQDA---ARAREECLKLTELLGEsehqlhltRLEKesiQQSFSNEAK 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1736 QQKLTAEQELIRLRADFDNAEQQRSLLEDELYRL---KNEVAAAQQQR-----KQLEDELAKVRSEMDILIQ----LKTK 1803
Cdd:pfam15964 552 AQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLltsQNTFIAKLKEEcctlaKKLEEITQKSRSEVEQLSQekeyLQDR 631
|
330
....*....|....
gi 1988774676 1804 AEKETMSNTEKSKQ 1817
Cdd:pfam15964 632 LEKLQKRNEELEEQ 645
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1818-2064 |
1.13e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1818 LLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEeAARQRAEAERILKEKLAAISEATRL--KTEAEIALKEKEAE--N 1893
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAelE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1894 ERLRRQAEDEAYQRKALEDQ--ASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRvveEEIRILKLNFEKASSGK 1971
Cdd:COG4942 90 KEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR---EQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1972 LDLELELNKLKNIADETQQSKIRAEEEAEKLRKLAleeekrrREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEA 2051
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLL-------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
250
....*....|...
gi 1988774676 2052 RKQKDEADKEAEK 2064
Cdd:COG4942 240 AERTPAAGFAALK 252
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
70-167 |
1.17e-04 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 45.35 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 70 QKKTFTKWVN---------KHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 136
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1988774676 137 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 167
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
2204-2627 |
1.17e-04 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 48.32 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2204 QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDST 2283
Cdd:pfam09730 38 ELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRDEIKEYKVREARLLQDYSELEEENISLQKQVSVLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2284 QKLLAEEA--ENMRKLAEDAARLSVEAQEAARLRQIaeddlnqqralAEKMLKEKMQAIQEASRLKAeaemlqkqkDLAQ 2361
Cdd:pfam09730 118 QNQVEFEGlkHEITRKEEETELLNSQLEEAIRLREI-----------AERQLDEALETLKTEREQKN---------SLRK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2362 EQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLhet 2441
Cdd:pfam09730 178 ELSHYMTLNDFDYVSHLSISLDGLKFSEDEGAGTEPNNDGEAMDGGENGGGGLKNSGLDNRTSTPRKSEVFPPAPSL--- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2442 eiatqekmtvVERLeFERLNTSkEADDLRKAIADLENEKARLKKEAEELQnksKEMADAQQKKIEHEKTVLQqtfMTEKE 2521
Cdd:pfam09730 255 ----------VSDL-LSELNIS-EIQKLKQQLIQVEREKVSLLSTLQESQ---KQLEQAKGALSEQQEKVNR---LTENL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2522 MLLKKeklIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEqekkTLQATMDAALSKQKEAEEEMLRKQKEMQELERQR 2601
Cdd:pfam09730 317 EAMRG---LQASKERQDALDSEKDRDSHEDGDYYEVDINGPE----ILECKYRVAVEEAGELREELKALKARYNTLEERY 389
|
410 420
....*....|....*....|....*.
gi 1988774676 2602 LEQERILAEENQKLREKLQQLEDAQK 2627
Cdd:pfam09730 390 KEEKTRWEAEAQDLAEKIRQLEKASH 415
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1767-2082 |
1.20e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.41 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1767 YRL-KNEVAAAQQQRKQleDELAKVRSEMDILIQLKTKAEKEtmsntEKSKQLLEAEAAKMKD-LAEEASRLRAISEEAK 1844
Cdd:PRK05035 431 YRQaKAEIRAIEQEKKK--AEEAKARFEARQARLEREKAARE-----ARHKKAAEARAAKDKDaVAAALARVKAKKAAAT 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1845 HQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAedeayqRKALEDQASQhkqEIEEK 1924
Cdd:PRK05035 504 QPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKA------KKAAQQAANA---EAEEE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1925 IVQLKKSSEAEMERQKAivddtlkqrrvveeeiRILKLNFEKASSGKLDLELELNKlkniadetqqSKIRAEEEAEKLRK 2004
Cdd:PRK05035 575 VDPKKAAVAAAIARAKA----------------KKAAQQAASAEPEEQVAEVDPKK----------AAVAAAIARAKAKK 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2005 LALEEEKRRREAEEKvkkiaaaeeeaarqRKAALE-ELERLR-KKAEEARKQKDEADKEAE-KQIVVAQQAAQKCSAAEQ 2081
Cdd:PRK05035 629 AEQQANAEPEEPVDP--------------RKAAVAaAIARAKaRKAAQQQANAEPEEAEDPkKAAVAAAIARAKAKKAAQ 694
|
.
gi 1988774676 2082 Q 2082
Cdd:PRK05035 695 Q 695
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1722-2244 |
1.21e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1722 EELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQ--QQRKQLEDELAKVRSEmdiliq 1799
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPER------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1800 lktkaeketmsntekskqlLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLK 1879
Cdd:COG4717 148 -------------------LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1880 TEAEIALKEKEAENERLRRQAEDEayqrkaledQASQHKQEIEEKIVQLKKSSEAEmerqKAIVDDTLKQRRVVEEEIRI 1959
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQL---------ENELEAAALEERLKEARLLLLIA----AALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1960 LKLNFekASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALeeekrrreaeekvKKIAAAEEEAARQRKAALE 2039
Cdd:COG4717 276 AGVLF--LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEL-------------EELLAALGLPPDLSPEELL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2040 ELERLRKKAEEARKQKDEADKEAEKQivvaqqaaqkcsAAEQQVQSVLAQQIEDSItqkklkEEYEKAKKLAKEAEAAKE 2119
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLE------------ELEQEIAALLAEAGVEDE------EELRAALEQAEEYQELKE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2120 KAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAakraqaeaaalMQKQQADTEMAKHKKLAEQTL 2199
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEE-----------LREELAELEAELEQLEEDGEL 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 2200 KQKfqvEQELTKVKLKLDETDKQ-------KSVLDEELQRLKDEVDDAVKQR 2244
Cdd:COG4717 472 AEL---LQELEELKAELRELAEEwaalklaLELLEEAREEYREERLPPVLER 520
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2183-2384 |
1.24e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2183 QADTEMAKHKKLAEQTL---KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQR------GQVEEELFK 2253
Cdd:PRK11281 53 LLEAEDKLVQQDLEQTLallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2254 VKVQMEEllkLKNKIEEENQRLIkkdkdsTQKLLAEEA-----ENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRAL 2328
Cdd:PRK11281 133 TLDQLQN---AQNDLAEYNSQLV------SLQTQPERAqaalyANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQAL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774676 2329 AEKMLKEKMQAIQEASRLKaeaEMLQKQKDLAQEQAQKLLEDKQLMQ-----QRLeEETEE 2384
Cdd:PRK11281 204 LNAQNDLQRKSLEGNTQLQ---DLLQKQRDYLTARIQRLEHQLQLLQeainsKRL-TLSEK 260
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1377-1644 |
1.24e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 48.05 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1377 EEKAAEKLKAEErkKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNiqlELQELK 1456
Cdd:PRK07735 38 EEENREKEKALP--KNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAA---ALAKQK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1457 NLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEklrklAQDEAEKLRKqvsee 1536
Cdd:PRK07735 113 REGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAA-----AKAKAAALAK----- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1537 tQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSfa 1616
Cdd:PRK07735 183 -QKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAKTKGAE-- 259
|
250 260 270
....*....|....*....|....*....|
gi 1988774676 1617 ektSKLEESLKQEHGAVLQ--LQQEAERLK 1644
Cdd:PRK07735 260 ---GKKEEEPKQEEPSVNQpyLNKYVEVIK 286
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1302-1534 |
1.26e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1302 AKAYIDTIKDYELQLVAYKAQVEPLVSPLKKTKldSASDNIIQEYVTLRTRYSELMTL---TSQYIKFITDTQRRLDDEE 1378
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALK--KEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1379 KAAEKLKAEERKKMAEMQAELdkQKQLAEAHAKAIAKAEKEAQELK-LKMQEEVSKREIAAVDAEKQKTNiqlELQELKN 1457
Cdd:COG4942 93 AELRAELEAQKEELAELLRAL--YRLGRQPPLALLLSPEDFLDAVRrLQYLKYLAPARREQAEELRADLA---ELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774676 1458 LSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKL-RKLAQDEAEKLRKQVS 1534
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiARLEAEAAAAAERTPA 245
|
|
| SH3_and_anchor |
TIGR04211 |
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ... |
2204-2293 |
1.27e-04 |
|
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.
Pssm-ID: 275056 [Multi-domain] Cd Length: 198 Bit Score: 46.15 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2204 QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLknkiEEENQRLIKKDKDST 2283
Cdd:TIGR04211 70 ELQQELAELQEELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIKQISANAIEL----DEENRELREELAELK 145
|
90
....*....|
gi 1988774676 2284 QKLLAEEAEN 2293
Cdd:TIGR04211 146 QENEALEAEN 155
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2319-2593 |
1.28e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2319 EDDLNQQRALAEKMLKE----KMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEEteeyhksleveRK 2394
Cdd:COG1340 10 LEELEEKIEELREEIEElkekRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL-----------KE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2395 RQLEIMAEAERLRLQVSQLSEAQARAEEEA---KKFKKQADKVATRLHETEIATQEKMTVVERLE--FERLNTSKEADDL 2469
Cdd:COG1340 79 ERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKelEKELEKAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2470 RKAIADLENEKARLKKEAEELQNKSKEMADAQQKKieHEKtvlqqtfMTEkemLLKKEKLIEDEKKRLESQFEEEVKKAK 2549
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQEL--HEE-------MIE---LYKEADELRKEADELHKEIVEAQEKAD 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1988774676 2550 ALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKE 2593
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1538-1670 |
1.30e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 44.55 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1538 QKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEaerqvkqaeiekekqikvaheaAQKSAAAELQsKHMSFAE 1617
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIARE----------------------AQQNYERELV-LHAEDIK 57
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 1618 KTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANE 1670
Cdd:pfam07926 58 ALQALREELNELKAEIAELKAEAESAKAELEESEESWEEQKKELEKELSELEK 110
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
953-1552 |
1.32e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 953 RLIMRNLELHYQDFMRDSQDSQLFGPDDRMQVEDDYTKSTQHFDNLLRSmeKGQQNETLCKNYISELKDLRLRIEDCEAG 1032
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ--KLEERSQKESKARSGLKVLLALIKDGVGG 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1033 TVARIRKPVEKEPLKEYIQKTTEQKKVQGELDGLKKDLDKVSVKTQEVLASPQPSASAPVLRSELDLTVQKMDHAHMLSS 1112
Cdd:pfam02463 523 RIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPI 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1113 VYLEKLKTVEMVIRNTQGAEGVLKQYEDCLREVHTVPSDVKEVETYRAK-------LKKMRTEAEDEQPVFDSLEEELKK 1185
Cdd:pfam02463 603 LNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGvsleeglAEKSEVKASLSELTKELLEIQELQ 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1186 ASAVSDKMVRVHSERDVELDhFRQQLSSLQDRWKAVFTQIDLRQRELEQLGRQLGYYREsydwLIRWIADAKQRQEKIQA 1265
Cdd:pfam02463 683 EKAESELAKEEILRRQLEIK-KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKL----LKQKIDEEEEEEEKSRL 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1266 VPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKayidtIKDYELQLVAYKAQVEPLVSPLKKTKLDSASDNIIQE 1345
Cdd:pfam02463 758 KKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEK-----LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKE 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1346 YVTLRTRYSELMTLTSQYiKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQlaeahakaiaKAEKEAQELKL 1425
Cdd:pfam02463 833 EELEELALELKEEQKLEK-LAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES----------KEEKEKEEKKE 901
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1426 KMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKqkytaesEL 1505
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL-------GK 974
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1988774676 1506 KQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSE 1552
Cdd:pfam02463 975 VNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1638-1859 |
1.33e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.53 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1638 QEAERLKKQQEDAENSREEAEKELEkwrQKAnEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQK 1717
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLE---QQA-EEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1718 EMAEEELERQRK-IAESTAQQKLTAEQELIRLRADFDNAEQQRsllEDELYRLKNEVAAAQQQRKQLEDELAKVRSEmdi 1796
Cdd:TIGR02794 126 AKQAAEAKAKAEaEAERKAKEEAAKQAEEEAKAKAAAEAKKKA---EEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE--- 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 1797 liQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRA 1859
Cdd:TIGR02794 200 --AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1539-1872 |
1.36e-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: 47.61 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1539 KKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQaeiEKEKQIKVAHEAAQKSAAAELQSKHMsfaek 1618
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQ---ELEEQIEEREQKRQEEYEEKLQEREQ----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1619 tskLEESLKQEHgavLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKtlaqeeaekqkeE 1698
Cdd:pfam13868 103 ---MDEIVERIQ---EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKE------------K 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1699 AEREAKKRAKAEEsalkQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 1778
Cdd:pfam13868 165 AEREEEREAEREE----IEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1779 QRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQR 1858
Cdd:pfam13868 241 REEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERL 320
|
330
....*....|....
gi 1988774676 1859 AEAERILKEKLAAI 1872
Cdd:pfam13868 321 REEEAERRERIEEE 334
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1633-1957 |
1.42e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 47.72 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1633 VLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRL-------QAEDEAHKKTLAQEEAEKQKEEAEREAKK 1705
Cdd:pfam15558 13 MLARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLqqsqeqwQAEKEQRKARLGREERRRADRREKQVIEK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1706 RAKAEESALKQKEMAEEELERQRKIAESTAQ---QKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVaaAQQQRKQ 1782
Cdd:pfam15558 93 ESRWREQAEDQENQRQEKLERARQEAEQRKQcqeQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKER--EEQKKVQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1783 LEDELAKVRSE-MDILIQLKTKAEKETMSNT---------EKSKQLLEAEAAKMKDLA----EEASRLRAISEEAKHQRQ 1848
Cdd:pfam15558 171 ENNLSELLNHQaRKVLVDCQAKAEELLRRLSleqslqrsqENYEQLVEERHRELREKAqkeeEQFQRAKWRAEEKEEERQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1849 ------IAEEEAARQRAE--AERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKaledqasqhkqe 1920
Cdd:pfam15558 251 ehkealAELADRKIQQARqvAHKTVQDKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKK------------ 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 1988774676 1921 iEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEI 1957
Cdd:pfam15558 319 -EQRSEQISREKEATLEEARKTARASFHMREKVREET 354
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
76-166 |
1.42e-04 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 44.21 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 76 KWVNKHLIKAQR---HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM---RFHKLQNVQIALDFLRhrQVKLVN-IRN 148
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
|
90
....*....|....*...
gi 1988774676 149 DDIADGNPKLTLGLIWTI 166
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1548-1959 |
1.46e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.73 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1548 KRKSEAEKEAAKQKQKALEDLEKLRMQAEE----AERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLE 1623
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEaeqkAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1624 ESLKQEHGAVLQLQQEAERLKKQQEDAENSREEA----EKELEKWRQKANEALRLRLQAE-DEAHKKTLAQEEAEKQKEE 1698
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAaaaeKEKAEEAKRKAEEEAKRKAEEErKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1699 AEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 1778
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1779 QRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQR 1858
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1859 AEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMER 1938
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGL 400
|
410 420
....*....|....*....|.
gi 1988774676 1939 QKAIVDDTLKQRRVVEEEIRI 1959
Cdd:COG3064 401 LGLRLDLGAALLEAASAVELR 421
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2206-2643 |
1.46e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2206 EQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIeeeNQRLIKKDKDStqK 2285
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKF---LTEIKKKEKEL--E 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2286 LLAEEAENMRKLAEDaarlsVEAQEAARLRQIAE-----DDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKdla 2360
Cdd:TIGR04523 156 KLNNKYNDLKKQKEE-----LENELNLLEKEKLNiqkniDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQN--- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2361 qeqaQKLLEDKQLMQQRLEEETEEYHKSLEverkrqleimaeaerlrlQVSQLseaqaraeeeakkfKKQADKVATRLhe 2440
Cdd:TIGR04523 228 ----NQLKDNIEKKQQEINEKTTEISNTQT------------------QLNQL--------------KDEQNKIKKQL-- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2441 teiatQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKAR--LKKEAEELQNKSKEMADAQQKKIEHEKTVLQqtfMT 2518
Cdd:TIGR04523 270 -----SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQ---LN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2519 EKEMLLKKEKL-IEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQekktlqatmdaaLSKQKEAEEEMLRKQKEMQEL 2597
Cdd:TIGR04523 342 EQISQLKKELTnSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN------------LESQINDLESKIQNQEKLNQQ 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1988774676 2598 ERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDII 2643
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1530-1669 |
1.58e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 46.24 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1530 RKQvsEETQKKRQAEEELKRKSEAEKEAAKQ--KQKALEDLEKlrmqaeeaerqvKQAEIEKEKQIKVAHEAAQKSAAAE 1607
Cdd:pfam13904 63 AKQ--RQRQKELQAQKEEREKEEQEAELRKRlaKEKYQEWLQR------------KARQQTKKREESHKQKAAESASKSL 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774676 1608 LQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSR--EEAEKELEKWRQKAN 1669
Cdd:pfam13904 129 AKPERKVSQEEAKEVLQEWERKKLEQQQRKREEEQREQLKKEEEEQErkQLAEKAWQKWMKNVK 192
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1404-1603 |
1.66e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 47.71 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1404 QLAEAHAKAIAKAEKEAQELKLKMQEEVSkreiaavdaekqktniqlELQELKNLSEQQIKDKSQQVDEALHSRTKIEEE 1483
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQQREEELE------------------ELQEQLEDLESSIQELEKEIKKLESSIKQVEEE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1484 IRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLrKQVSEETQKKRQAE-EELKRKSEAEKEAAKQKQ 1562
Cdd:pfam05667 372 LEELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRL-VELAGQWEKHRVPLiEEYRALKEAKSNKEDESQ 450
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1988774676 1563 KALEDLEKLRMQAEEAERQVKQAEiEKEKQIKVAHEAAQKS 1603
Cdd:pfam05667 451 RKLEEIKELREKIKEVAEEAKQKE-ELYKQLVAEYERLPKD 490
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1527-1720 |
1.70e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 47.69 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1527 EKLRKQVSEETQKKRQAEEELKRKSEaekEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAA 1606
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDLKERESQ---EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1607 ELQSKHMSFAEKtSKLEESLKQEhgavlqlqqeaerLKKQQEDAENSREEAEKELEkwrQKANEALRLRLQAEDEAHKKT 1686
Cdd:pfam05262 261 PKPADTSSPKED-KQVAENQKRE-------------IEKAQIEIKKNDEEALKAKD---HKAFDLKQESKASEKEAEDKE 323
|
170 180 190
....*....|....*....|....*....|....
gi 1988774676 1687 LAQEEAEKQKEEAEREAKKRAKAEESALKQKEMA 1720
Cdd:pfam05262 324 LEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAID 357
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2200-2381 |
1.75e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 46.80 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2200 KQKFQ--VEQELTKVKLKLDETDKQKSV--LDEELQRLKDEVDDAVKQ---------------RGQVEEELFKVK---VQ 2257
Cdd:cd16269 88 DQKFQkkLMEQLEEKKEEFCKQNEEASSkrCQALLQELSAPLEEKISQgsysvpggyqlyledREKLVEKYRQVPrkgVK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2258 MEELLK--LKNKIEEENQRLiKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAaRLRQIAEDdlnQQRALAE--KML 2333
Cdd:cd16269 168 AEEVLQefLQSKEAEAEAIL-QADQALTEKEKEIEAERAKAEAAEQERKLLEEQQR-ELEQKLED---QERSYEEhlRQL 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1988774676 2334 KEKMQaiQEASRLKAEAEMLQKQKDlaQEQAQKLLEDKQLMQQRLEEE 2381
Cdd:cd16269 243 KEKME--EERENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEE 286
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2832-2868 |
1.91e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 1.91e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1988774676 2832 IRVLEAQLATGGIIDPINSHRVPTETAYKQGHYDAEM 2868
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1829-2002 |
1.98e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1829 LAEEASRLRAiSEEAKHQRQIAEEEAARQRAEAERI---LKEKLAAISEATRLKTEAEIALKEKEAENERLRrqaEDEAY 1905
Cdd:pfam07888 40 LQERAELLQA-QEAANRQREKEKERYKRDREQWERQrreLESRVAELKEELRQSREKHEELEEKYKELSASS---EELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1906 QRKALEDQASQHKQEIEE------KIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELN 1979
Cdd:pfam07888 116 EKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170 180
....*....|....*....|...
gi 1988774676 1980 KLKNIADETQQSKIRAEEEAEKL 2002
Cdd:pfam07888 196 ELRNSLAQRDTQVLQLQDTITTL 218
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1815-1958 |
2.09e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1815 SKQLLEAEAAKMKDLAEEASRLRAISEEAKHQrqiAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENE 1894
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLE---AKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774676 1895 RLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKsseaEMERQKAIVDDTLKQR--RVVEEEIR 1958
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEAR 168
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1711-2005 |
2.11e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1711 ESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKV 1790
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1791 RSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLA 1870
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1871 AISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQR 1950
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774676 1951 RVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKL 2005
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADL 342
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2437-2601 |
2.19e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2437 RLHETEIATQEKMTVVERLE--FERLNTSKEADDLRKAIADLENEKARLKKEAEELQnksKEMADAQQKKIEHEKTVLQQ 2514
Cdd:COG4913 259 ELAERYAAARERLAELEYLRaaLRLWFAQRRLELLEAELEELRAELARLEAELERLE---ARLDALREELDELEAQIRGN 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2515 TFmTEKEMLLKKEKLIEDEKKRLE---SQFEEEVKKA-----------KALKDEQERQKQQMEQEKKTLQATMDAALSKQ 2580
Cdd:COG4913 336 GG-DRLEQLEREIERLERELEERErrrARLEALLAALglplpasaeefAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
170 180
....*....|....*....|.
gi 1988774676 2581 KEAEEEMLRKQKEMQELERQR 2601
Cdd:COG4913 415 RDLRRELRELEAEIASLERRK 435
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1577-1827 |
2.21e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1577 EAERQvkqaEIEKEKQIKVAHEAAqksaaaELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREE 1656
Cdd:pfam17045 5 EAELQ----ELMKQIDIMVAHKKS------EWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1657 AEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKR--AKAEESALKQKEMAEEELERQRKIAEST 1734
Cdd:pfam17045 75 LVAKYEQQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRlnGKLEEFRQKSLEWEQQRLQYQQQVASLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1735 AQQKLTAEQ-ELIRLRADFDNAEQQRSLLED---ELYRLKNEVAAAQQQRKQLEDELAKVRSEMDIL------IQLKTKA 1804
Cdd:pfam17045 155 AQRKALAEQsSLIQSAAYQVQLEGRKQCLEAsqsEIQRLRSKLERAQDSLCAQELELERLRMRVSELgdsnrkLLEEQQR 234
|
250 260
....*....|....*....|...
gi 1988774676 1805 EKETMSNTEKSKQLLEAEAAKMK 1827
Cdd:pfam17045 235 LLEELRMSQRQLQVLQNELMELK 257
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3083-3118 |
2.22e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.22e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1988774676 3083 LNLLEAQAGTGYLVDPVHNQKYTVDEAVKAGVVGPE 3118
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2338-2506 |
2.28e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.17 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2338 QAIQEASRLKAEAEmlqKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQlEIMAEAERLRLQVSQlseAQ 2417
Cdd:COG2268 196 EIIRDARIAEAEAE---RETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKA-EERREAETARAEAEA---AY 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2418 ARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEferlntskeADDLRKAIADLENEKARLKKEAEELQNKSKEM 2497
Cdd:COG2268 269 EIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELE---------ADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAE 339
|
....*....
gi 1988774676 2498 ADAQQKKIE 2506
Cdd:COG2268 340 AEGKRALAE 348
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4411-4448 |
2.31e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.31e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1988774676 4411 QRFLEVQYLTGGLIEPDVEGRVSIDESIRKGTIDARTA 4448
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2365-2641 |
2.50e-04 |
|
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: 47.38 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2365 QKLLEDKQLMQQRLEEEteEYHKSLEVERKRQLeiMAEAERLRLQVSQLSEAQARAEEEAKKFKkQADKVATRLHEteia 2444
Cdd:pfam05622 3 SEAQEEKDELAQRCHEL--DQQVSLLQEEKNSL--QQENKKLQERLDQLESGDDSGTPGGKKYL-LLQKQLEQLQE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2445 tqekmtvverlEFERLNTSKeaDDLRKAIADLENEKARLKKEAEELQNKSKEmadAQQKKIEHEktVLQQTfmteKEMLL 2524
Cdd:pfam05622 74 -----------ENFRLETAR--DDYRIKCEELEKEVLELQHRNEELTSLAEE---AQALKDEMD--ILRES----SDKVK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2525 KKEKLIEDEKKRLES-----------------------QFEEEVKKAKALKDEQERQKQQMEQekktLQATMDAALSKQK 2581
Cdd:pfam05622 132 KLEATVETYKKKLEDlgdlrrqvklleernaeymqrtlQLEEELKKANALRGQLETYKRQVQE----LHGKLSEESKKAD 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2582 EAEEEMLRKQKEMQELERqrlEQERILAEENQkLREKLQQLEDAQKDQHTRETDKVLHKD 2641
Cdd:pfam05622 208 KLEFEYKKLEEKLEALQK---EKERLIIERDT-LRETNEELRCAQLQQAELSQADALLSP 263
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1791-2586 |
2.53e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1791 RSEMDILIQLKTKAEKETMS---NTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEeAARQR--------- 1858
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTsrrQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQT-ALRQQekieryqad 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1859 -AEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDeaYQRkALEDQ---ASQHKQEIE--EKIVQLKKSS 1932
Cdd:PRK04863 357 lEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAD--YQQ-ALDVQqtrAIQYQQAVQalERAKQLCGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1933 EAEMERQKAIVDDTLKQRRVVEEEIRIL--KLNFEKASSGKLDLELELnkLKNIADET-----QQSKIRAEEEAEKLRKL 2005
Cdd:PRK04863 434 DLTADNAEDWLEEFQAKEQEATEELLSLeqKLSVAQAAHSQFEQAYQL--VRKIAGEVsrseaWDVARELLRRLREQRHL 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2006 AleeekrrreaeekvkkiaaaeeEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQS 2085
Cdd:PRK04863 512 A----------------------EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLES 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2086 vLAQQIEDSITQKklkeeyekakklakeaeaakekaereaALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRkeAEF 2165
Cdd:PRK04863 570 -LSESVSEARERR---------------------------MALRQQLEQLQARIQRLAARAPAWLAAQDALARLR--EQS 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2166 EAAKRAQAEAAALMQKQQadtemakhKKLAEQTLkQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKD---------- 2235
Cdd:PRK04863 620 GEEFEDSQDVTEYMQQLL--------ERERELTV-ERDELAARKQALDEEIERLSQPGGSEDPRLNALAErfggvllsei 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2236 ----EVDDA---------------VKQRGQVEEEL-------------------FKVKVQMEELLKlKNKIEEENQRLIK 2277
Cdd:PRK04863 691 yddvSLEDApyfsalygparhaivVPDLSDAAEQLagledcpedlyliegdpdsFDDSVFSVEELE-KAVVVKIADRQWR 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2278 KDKDSTQKLLAEEAENMR---------KLAEDAARLSVEAQEAARLRQIAEDDLNQQRALA-----EKMLKEKMQAIQEA 2343
Cdd:PRK04863 770 YSRFPEVPLFGRAAREKRieqlraereELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVEL 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2344 SRLKAEAE----MLQKQKDLAQEQAQ---------KLLEDKQLmQQRLEEETEEYHKSLEVERK--------RQLEIMAE 2402
Cdd:PRK04863 850 ERALADHEsqeqQQRSQLEQAKEGLSalnrllprlNLLADETL-ADRVEEIREQLDEAEEAKRFvqqhgnalAQLEPIVS 928
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2403 A--------ERLRLQVSQLseaqaraEEEAKKFKKQADKVAtrlheteiatqekmTVVERLefERLNTSKEADDLRKAIA 2474
Cdd:PRK04863 929 VlqsdpeqfEQLKQDYQQA-------QQTQRDAKQQAFALT--------------EVVQRR--AHFSYEDAAEMLAKNSD 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2475 DLENEKARLkKEAEELQNKSKEMADAQQKKIEHEKTV---LQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEevkKAKAL 2551
Cdd:PRK04863 986 LNEKLRQRL-EQAEQERTRAREQLRQAQAQLAQYNQVlasLKSSYDAKRQMLQELKQELQDLGVPADSGAEE---RARAR 1061
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1988774676 2552 KDE-QER------QKQQMEQEKKTLQATMDAALSKQKEAEEE 2586
Cdd:PRK04863 1062 RDElHARlsanrsRRNQLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2485-2627 |
2.70e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2485 KEAEELQNKSKEMADAQQKKiehEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQfEEEVKKAKALKDEQERQKQQMEQ 2564
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQR---KKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ-EQKKQAEEAAKQAALKQKQAEEA 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774676 2565 EKKTLQATMDAALSKQKEAEEemLRKQKEMQELERQRLEQERILAEENQKLRE---KLQQLEDAQK 2627
Cdd:PRK09510 138 AAKAAAAAKAKAEAEAKRAAA--AAKKAAAEAKKKAEAEAAKKAAAEAKKKAEaeaAAKAAAEAKK 201
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1492-1913 |
2.75e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 46.96 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1492 ETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKL 1571
Cdd:COG3064 30 EAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1572 RMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAE 1651
Cdd:COG3064 110 AEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1652 NSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIA 1731
Cdd:COG3064 190 VEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1732 ESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSN 1811
Cdd:COG3064 270 GAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1812 TEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEA 1891
Cdd:COG3064 350 AAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGA 429
|
410 420
....*....|....*....|..
gi 1988774676 1892 ENERLRRQAEDEAYQRKALEDQ 1913
Cdd:COG3064 430 AGAVVALLVKLVADLAGGLVGI 451
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1369-2230 |
2.75e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1369 DTQRRLDDEEKAAEKLkAEERKKMAEMQAELDKQKQLAEAH----AKAIAKAEK--------EAQELKLKMQEEVSK-RE 1435
Cdd:COG3096 296 GARRQLAEEQYRLVEM-ARELEELSARESDLEQDYQAASDHlnlvQTALRQQEKieryqedlEELTERLEEQEEVVEeAA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1436 IAAVDAEKQKTNIQLELQELKNlseqQIKDKSQQVDEaLHSRTkieeeirlirIQLETTEKQKYTAEsELKQLRDRAAEA 1515
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSLKS----QLADYQQALDV-QQTRA----------IQYQQAVQALEKAR-ALCGLPDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1516 eklrklAQDEAEKLRKQVSEETQKKRQAEEELkrkSEAEkEAAKQKQKALEDLEKL-----RMQAEEAERQVkqaeieke 1590
Cdd:COG3096 439 ------AEDYLAAFRAKEQQATEEVLELEQKL---SVAD-AARRQFEKAYELVCKIageveRSQAWQTAREL-------- 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1591 kqikVAHEAAQKSAAAELQSKHMSFAEktskLEESLKQEHGAVLQLQQEAERLKKQQEDA---ENSREEAEKELEKWRQK 1667
Cdd:COG3096 501 ----LRRYRSQQALAQRLQQLRAQLAE----LEQRLRQQQNAERLLEEFCQRIGQQLDAAeelEELLAELEAQLEELEEQ 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1668 ANEAL--RLRLQAEDEAHKktlaqeeaekqkeEAEREAKKRA----KAEESALKQKEMAEEELERQRKIAEsTAQQKLTA 1741
Cdd:COG3096 573 AAEAVeqRSELRQQLEQLR-------------ARIKELAARApawlAAQDALERLREQSGEALADSQEVTA-AMQQLLER 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1742 EQELIRLRadfDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVR-SEM--DILIqlktkaeketmsntekskql 1818
Cdd:COG3096 639 EREATVER---DELAARKQALESQIERLSQPGGAEDPRLLALAERLGGVLlSEIydDVTL-------------------- 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1819 leaeaakmkdlaEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAIS-------EATRLKTEAEIALKEKEA 1891
Cdd:COG3096 696 ------------EDAPYFSALYGPARHAIVVPDLSAVKEQLAGLEDCPEDLYLIEgdpdsfdDSVFDAEELEDAVVVKLS 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1892 ENE-RLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSS--EAEMERQKAIVDDTLKQRRVV------EEEIRILKl 1962
Cdd:COG3096 764 DRQwRYSRFPEVPLFGRAAREKRLEELRAERDELAEQYAKASfdVQKLQRLHQAFSQFVGGHLAVafapdpEAELAALR- 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1963 nfekASSGKLDLELElnklkNIADETQQSKIRAEEEAEKLRKLAleeekrrreaeekvKKIAAAEEEAARQRKAALEELE 2042
Cdd:COG3096 843 ----QRRSELERELA-----QHRAQEQQLRQQLDQLKEQLQLLN--------------KLLPQANLLADETLADRLEELR 899
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2043 RLRKKAEEAR---KQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQieDSITQKKLKEEYEKAKKLAKEAEAAKE 2119
Cdd:COG3096 900 EELDAAQEAQafiQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQ--RRLKQQIFALSEVVQRRPHFSYEDAVG 977
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2120 KAEREAAL---LRQQAEEAERQKTAAEEEAANQAKAQEDA-------------------ERLRKEAEFEAAKRAQAEAAA 2177
Cdd:COG3096 978 LLGENSDLnekLRARLEQAEEARREAREQLRQAQAQYSQYnqvlaslkssrdakqqtlqELEQELEELGVQADAEAEERA 1057
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 2178 LMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEEL 2230
Cdd:COG3096 1058 RIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1557-1747 |
2.82e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1557 AAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKekqikvaheAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQL 1636
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAEL---------AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1637 QQEAERLKKQQEDAENSRE--EAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESAL 1714
Cdd:COG1579 72 EARIKKYEEQLGNVRNNKEyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180 190
....*....|....*....|....*....|...
gi 1988774676 1715 KQKEMAEEELERQRKIAESTAQQKLTAEQELIR 1747
Cdd:COG1579 152 AELEAELEELEAEREELAAKIPPELLALYERIR 184
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
70-167 |
2.89e-04 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 44.23 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 70 QKKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 136
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1988774676 137 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 167
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3453-3484 |
2.92e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.92e-04
10 20 30
....*....|....*....|....*....|..
gi 1988774676 3453 KLLSAEKAVTGYKDPFTGNKISLFEAMQKDLI 3484
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2269-2409 |
3.33e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.87 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2269 EEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDdlnQQRALAEKMLKEKMQAIQEASRLKa 2348
Cdd:pfam15709 356 EQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEE---RKQRLQLQAAQERARQQQEEFRRK- 431
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774676 2349 eaeMLQKQKDLAQEQAQKLLEDKQlMQQRLEEETEEyhkslevERKRQLEiMAEAERLRLQ 2409
Cdd:pfam15709 432 ---LQELQRKKQQEEAERAEAEKQ-RQKELEMQLAE-------EQKRLME-MAEEERLEYQ 480
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1701-1985 |
3.37e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1701 REAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQR 1780
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1781 KQLEDELAKVRSEMDIL------IQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQ--RQIAEE 1852
Cdd:COG4372 83 EELNEQLQAAQAELAQAqeelesLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEleEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1853 EAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSS 1932
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 1933 EAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIA 1985
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALEL 295
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1512-1663 |
3.58e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1512 AAEAEKLRKLAQ---------DEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQV 1582
Cdd:COG1579 3 PEDLRALLDLQEldseldrleHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1583 K-----------QAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAE 1651
Cdd:COG1579 83 GnvrnnkeyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|..
gi 1988774676 1652 NSREEAEKELEK 1663
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1253-1531 |
3.60e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1253 IADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKK 1332
Cdd:COG1340 24 IEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1333 TKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKaEERKKMAEMQAELDKQKQLAEAHAKA 1412
Cdd:COG1340 104 LNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKAL-EKNEKLKELRAELKELRKEAEEIHKK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1413 IAKAEKEAQELKLKMQEEVSKREiaavdaekqktniqlELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLE 1492
Cdd:COG1340 183 IKELAEEAQELHEEMIELYKEAD---------------ELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
250 260 270
....*....|....*....|....*....|....*....
gi 1988774676 1493 TTEKQKYTAEselkqlrdRAAEAEKLRKLAQDEAEKLRK 1531
Cdd:COG1340 248 KLRKKQRALK--------REKEKEELEEKAEEIFEKLKK 278
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1726-1952 |
3.68e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.86 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1726 RQRKiAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELyRLKnevAAAQQQRKQLEDE----LAKVRSEMDILIQLK 1801
Cdd:PRK05035 432 RQAK-AEIRAIEQEKKKAEEAKARFEARQARLEREKAAREA-RHK---KAAEARAAKDKDAvaaaLARVKAKKAAATQPI 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1802 TKAEKETMSNTEkskqllEAEAAKMKDLAEEASRLRAISEEAKHQRQiAEEEAARQRAEAERILKEKLAAISEATRLKTE 1881
Cdd:PRK05035 507 VIKAGARPDNSA------VIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKKAAQQAANAEAEEEVDPKK 579
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774676 1882 AEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDtlKQRRV 1952
Cdd:PRK05035 580 AAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDP--RKAAV 648
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1402-1593 |
3.82e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1402 QKQLAEAHAKaIAKAEKEAQELKLK-----MQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQ---QIKDKSQQVDEA 1473
Cdd:COG3206 181 EEQLPELRKE-LEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAlraQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1474 LHSRTKIEEEIRLIRIQLE-TTEKQKYTAES-ELKQLRDRAAEAEK-LRKLAQDEAEKLRKQVSEETQKK---RQAEEEL 1547
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAElAELSARYTPNHpDVIALRAQIAALRAqLQQEAQRILASLEAELEALQAREaslQAQLAQL 339
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1988774676 1548 KRKSEAEKEAAkQKQKALE-DLEKLRMQAEEAERQVKQAEIEKEKQI 1593
Cdd:COG3206 340 EARLAELPELE-AELRRLErEVEVARELYESLLQRLEEARLAEALTV 385
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1479-1596 |
3.85e-04 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 45.75 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1479 KIEEEIRLIRIQLETtEKQKYTAESELKQLRDRAAEAEklRKLAQDEAEKLRkQVSEETQKKRQAEEE-LKRKSEAEKEA 1557
Cdd:cd03406 159 KIPEAIRRNYEAMEA-EKTKLLIAEQHQKVVEKEAETE--RKRAVIEAEKDA-EVAKIQMQQKIMEKEaEKKISEIEDEM 234
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1988774676 1558 AKQKQKALEDLE--KLRMQAEEAERQVKQAEIEKEKQIKVA 1596
Cdd:cd03406 235 HLAREKARADAEyyRALREAEANKLKLTPEYLELKKYQAIA 275
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1253-1479 |
3.88e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1253 IADAKQRQEKIQAvpitdskTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKK 1332
Cdd:COG3883 25 LSELQAELEAAQA-------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1333 TKLDSASDNII---QEYVTLRTRYSelmtltsqYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAH 1409
Cdd:COG3883 98 SGGSVSYLDVLlgsESFSDFLDRLS--------ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 1410 AKAI--AKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTK 1479
Cdd:COG3883 170 KAELeaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1717-1939 |
3.92e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.07 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1717 KEMAEEELERQRKIAESTAQQKLTAEQELIRLRADfdnAEQQRSLLEDELyRLKNEV-AAAQQQRKQLEDE-LAKVRSEM 1794
Cdd:pfam00038 49 YSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLA---AEDFRQKYEDEL-NLRTSAeNDLVGLRKDLDEAtLARVDLEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1795 DI------LIQLKTKAE---KETMSNTEKSKQLLEAEAAKMKDLAeeasrlRAISEeakhQRQIAEEEAARQRAEAERIL 1865
Cdd:pfam00038 125 KIeslkeeLAFLKKNHEeevRELQAQVSDTQVNVEMDAARKLDLT------SALAE----IRAQYEEIAAKNREEAEEWY 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1866 KEKLAAISEATRLKTEAEIALKEKEAENERL--RRQAEDEAY--QRKALEDQ--------ASQHKQ------EIEEKIVQ 1927
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTiqSLEIELQSLkkQKASLERQlaeteeryELQLADyqelisELEAELQE 274
|
250
....*....|..
gi 1988774676 1928 LKksseAEMERQ 1939
Cdd:pfam00038 275 TR----QEMARQ 282
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1618-1751 |
4.01e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 46.53 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1618 KTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKtlAQEEAEKQKE 1697
Cdd:pfam05262 204 KERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKE--DKQVAENQKR 281
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774676 1698 EAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK-LTAEQELIRLRAD 1751
Cdd:pfam05262 282 EIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKeLEAQKKREPVAED 336
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2470-2602 |
4.06e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2470 RKAIADLENEKARLKKEAE-ELQNKSKEM-----ADAQQKKIEHEKTV---------LQQTFMTEKEMLLKKEKLIEDEK 2534
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKkEAEAIKKEAlleakEEIHKLRNEFEKELrerrnelqkLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774676 2535 KRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATmdAALSKQkEAEEEMLRKQKEMQELERQRL 2602
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI--SGLTAE-EAKEILLEKVEEEARHEAAVL 174
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1160-1572 |
4.33e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1160 AKLKKMRTEAEDeqpvfdsLEEELKKASAVSDKMVRVHSerdveldHFRQQLSSLQDRW-----KAVFTQIDLRQRELEq 1234
Cdd:COG3096 785 KRLEELRAERDE-------LAEQYAKASFDVQKLQRLHQ-------AFSQFVGGHLAVAfapdpEAELAALRQRRSELE- 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1235 lgRQLGYYResydwlirwiADAKQRQEKIQAvpitdsktLKEQLAQEKKLL------------EEIEQNKDKVDECQkYA 1302
Cdd:COG3096 850 --RELAQHR----------AQEQQLRQQLDQ--------LKEQLQLLNKLLpqanlladetlaDRLEELREELDAAQ-EA 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1303 KAYIDtikdyelQLVAYKAQVEPLVSPLKKTKLDSasDNIIQEYVTLrtrySELMTLTSQYIKFIT------------DT 1370
Cdd:COG3096 909 QAFIQ-------QHGKALAQLEPLVAVLQSDPEQF--EQLQADYLQA----KEQQRRLKQQIFALSevvqrrphfsyeDA 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1371 QRRLDDEEKAAEKLKAeerkKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKlkmqeevskreiAAVDAEKQktniql 1450
Cdd:COG3096 976 VGLLGENSDLNEKLRA----RLEQAEEARREAREQLRQAQAQYSQYNQVLASLK------------SSRDAKQQ------ 1033
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1451 ELQELKN-LSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAE-- 1527
Cdd:COG3096 1034 TLQELEQeLEELGVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqa 1113
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774676 1528 KLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQK----------QKALEDLEKLR 1572
Cdd:COG3096 1114 KAGWCAVLRLARDNDVERRLHRRELAYLSADELRsmsdkalgalRLAVADNEHLR 1168
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1919-2406 |
4.46e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1919 QEIEEKIVQLKksseaEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAdETQQSKIRAEEE 1998
Cdd:COG4717 71 KELKELEEELK-----EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ-ELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1999 AEKLRKLaleeEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSA 2078
Cdd:COG4717 145 PERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2079 AEQQVQSVLAqQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAER 2158
Cdd:COG4717 221 ELEELEEELE-QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2159 LRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQeltkVKLKLDETDKQKSVLdeELQRLKDEVD 2238
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE----LQELLREAEELEEEL--QLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2239 DAVKQRGQVEEELFKVKV-QMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENmrkLAEDAARLSVEAQEAARLRqi 2317
Cdd:COG4717 374 ALLAEAGVEDEEELRAALeQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE---LEEELEELEEELEELEEEL-- 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2318 aeDDLNQQRALAEKMLKEkMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLledkQLMQQRLEEETEEYHksleveRKRQL 2397
Cdd:COG4717 449 --EELREELAELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWAAL----KLALELLEEAREEYR------EERLP 515
|
....*....
gi 1988774676 2398 EIMAEAERL 2406
Cdd:COG4717 516 PVLERASEY 524
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1655-2007 |
4.60e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1655 EEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQkemAEEELERQRKIAEST 1734
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQ---ARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1735 AQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEM--------DILIQLKTKAEK 1806
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIaereeelkELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1807 ETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIAL 1886
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1887 KEKEAENER-LRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFE 1965
Cdd:COG4372 246 EDKEELLEEvILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1988774676 1966 KASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLAL 2007
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2302-2636 |
4.90e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2302 ARLSVEAQEAARLRQIAE--DDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQR-L 2378
Cdd:pfam07888 67 DREQWERQRRELESRVAElkEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRvL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2379 EEETEEYHKSLEVERKRQLEIMAEAERLRLQvSQLSEAQARAEEEAKKFKK------QADKVATRLHETEIATQEKMTVV 2452
Cdd:pfam07888 147 ERETELERMKERAKKAGAQRKEEEAERKQLQ-AKLQQTEEELRSLSKEFQElrnslaQRDTQVLQLQDTITTLTQKLTTA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2453 ERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEEL-QNKSKEMADAQQKKIEHEKTVLQqtfMTEKEMLLKKEKlie 2531
Cdd:pfam07888 226 HRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMaAQRDRTQAELHQARLQAAQLTLQ---LADASLALREGR--- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2532 dekkrleSQFEeevkkakalkdeQERQ--KQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILA 2609
Cdd:pfam07888 300 -------ARWA------------QEREtlQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLS 360
|
330 340
....*....|....*....|....*..
gi 1988774676 2610 EENQKLREKLQQLEDAQKDQHTRETDK 2636
Cdd:pfam07888 361 ESRRELQELKASLRVAQKEKEQLQAEK 387
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1851-1950 |
5.14e-04 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 43.07 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1851 EEEAARQRAEAERILKEKLAAISEAtrlkteaEIALKEKEAENERLRRQAEDEAYQ-RKALEDQASQHkqeieekIVQLK 1929
Cdd:pfam00430 32 RELIADEIAEAEERRKDAAAALAEA-------EQQLKEARAEAQEIIENAKKRAEKlKEEIVAAAEAE-------AERII 97
|
90 100
....*....|....*....|.
gi 1988774676 1930 KSSEAEMERQKAIVDDTLKQR 1950
Cdd:pfam00430 98 EQAAAEIEQEKDRALAELRQQ 118
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1372-1536 |
5.19e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1372 RRLDDEEKAAEKLKAEERKKMAEMQAELDKQKqlaeahaKAIAKAEKEAQELKLKMQEevSKREIAAVDAEKQKTNIQLE 1451
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLE-------KEIKRLELEIEEVEARIKK--YEEQLGNVRNNKEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1452 LQELKnlseQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQkytAESELKQLRDRAAEAEKLRKLAQDEAEKLRK 1531
Cdd:COG1579 98 IESLK----RRISDLEDEILELMERIEELEEELAELEAELAELEAE---LEEKKAELDEELAELEAELEELEAEREELAA 170
|
....*
gi 1988774676 1532 QVSEE 1536
Cdd:COG1579 171 KIPPE 175
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
1560-1960 |
5.62e-04 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 46.21 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1560 QKQKALEDLEkLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGavlQLQQE 1639
Cdd:pfam04747 50 QRKEAFASLE-LTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEARRAEAEAKKRAAQEEEHK---QWKAE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1640 AERLKKQQEdaenSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEM 1719
Cdd:pfam04747 126 QERIQKEQE----KKEADLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTPTNTP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1720 AEEELERQRKIAESTAQQKLTAEQELIRLRADFDN-AEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILI 1798
Cdd:pfam04747 202 AEPAEQVQEITGKKNKKNKKKSESEATAAPASVEQvVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASETPVEP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1799 -----------QLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASR--LRAISEEAKHQRQIAEEEAARQRAEAERIL 1865
Cdd:pfam04747 282 vvettppasenQKKNKKDKKKSESEKVVEEPVQAEAPKSKKPTADDNMdfLDFVTAKEEPKDEPAETPAAPVEEVVENVV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1866 KEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALED--QASQHKQEIEEKIVQLKKSSEAEMERQKAIV 1943
Cdd:pfam04747 362 ENVVEKSTTPPATENKKKNKKDKKKSESEKVTEQPVESAPAPPQVEQvvETTPPASENKKKNKKDKKKSESEKAVEEPVQ 441
|
410
....*....|....*..
gi 1988774676 1944 DDTLKQRRVVEEEIRIL 1960
Cdd:pfam04747 442 AAPSSKKPTADDNMDFL 458
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3377-3413 |
5.98e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.98e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1988774676 3377 KYLQGSSSIAGLYLEPTKEKLSIYQAMKKKLLRHNTG 3413
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1516-1738 |
6.01e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 46.14 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1516 EKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQikv 1595
Cdd:TIGR00927 628 GDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEA--- 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1596 ahEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLR 1675
Cdd:TIGR00927 705 --DHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGE 782
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774676 1676 LQA-EDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK 1738
Cdd:TIGR00927 783 IQAgEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAK 846
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1505-1643 |
6.11e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.86 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1505 LKQLRDRAAEAEKLRKLAQDEAEKLRKQV------------SEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLR 1572
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAAlleakelllrerNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 1573 MQAEEAERQVKQAEIE-KEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQ-LQQEAERL 1643
Cdd:PRK12705 105 NQLEEREKALSARELElEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEeADLEAERK 177
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1854-2099 |
6.33e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1854 AARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSsE 1933
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL-R 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1934 AEMERQKAIVDDTLkqrRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQqskiraeEEAEKLRKLALEEEKRR 2013
Cdd:COG4942 97 AELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR-------EQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2014 REAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIED 2093
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
....*.
gi 1988774676 2094 SITQKK 2099
Cdd:COG4942 247 GFAALK 252
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2182-2314 |
6.38e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2182 QQADTEMAKHKKLAEQTLKQKF-----QVEQELTKVKLKLDETDKQ----KSVLDEELQRLKDEVDDAVKQRGQVEEELF 2252
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIhklrnEFEKELRERRNELQKLEKRllqkEENLDRKLELLEKREEELEKKEKELEQKQQ 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 2253 KVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENmrKLAEDAARLSVEAQEAARL 2314
Cdd:PRK12704 125 ELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVEE--EARHEAAVLIKEIEEEAKE 184
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1371-1573 |
6.56e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.63 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1371 QRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREiaavdaekqktnIQL 1450
Cdd:COG2268 225 EAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAERE------------REI 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1451 ELQELKnlseqqikdksqqvdealhsrtKIEEEIRLIRIQLETTEKQKYTAESElkqlrdRAAEAEKLRKLAQDEAEKLR 1530
Cdd:COG2268 293 ELQEKE----------------------AEREEAELEADVRKPAEAEKQAAEAE------AEAEAEAIRAKGLAEAEGKR 344
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1988774676 1531 KQVseETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRM 1573
Cdd:COG2268 345 ALA--EAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITI 385
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1635-1789 |
6.63e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1635 QLQQEAERLKKQQEDAENSREEAEKELEKWRQ--KANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEES 1712
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTelEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774676 1713 ALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQrslLEDELYRLKNEVAAAQQQRKQLEDELAK 1789
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAKIPP 174
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1258-1562 |
6.74e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 45.77 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1258 QRQEKIQAVPITDSKTLKEQLAQ-EKKLLE-EIEQNKDKVDECQKYakayiDTIKDYELQLVAYKAQVeplvSPLKKTKL 1335
Cdd:NF033838 158 QKEEDRRNYPTNTYKTLELEIAEsDVEVKKaELELVKEEAKEPRDE-----EKIKQAKAKVESKKAEA----TRLEKIKT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1336 D--SASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAE------LDKQKQLAE 1407
Cdd:NF033838 229 DreKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSVGEEtlpspsLKPEKKVAE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1408 AHaKAIAKAEKeaqelKLKMQEEVSKR------------EIAAVDAEKQKTNIQLELQELKnlsEQQIKDKSQQVDEALH 1475
Cdd:NF033838 309 AE-KKVEEAKK-----KAKDQKEEDRRnyptntyktlelEIAESDVKVKEAELELVKEEAK---EPRNEEKIKQAKAKVE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1476 SRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEA-----EKLRKQVSEETQKKRQAEEELKRK 1550
Cdd:NF033838 380 SKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKpapkpEKPAEQPKAEKPADQQAEEDYARR 459
|
330
....*....|..
gi 1988774676 1551 SEAEKEAAKQKQ 1562
Cdd:NF033838 460 SEEEYNRLTQQQ 471
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1742-2001 |
6.80e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1742 EQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQlktkaeketmsNTEKSKQLLEA 1821
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNE-----------KVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1822 EAAKMKDLAEEASRLRAISEE--------AKHQRQIAEEEAARQRA----EAERILKEKLAAIS---EATRLKTEAEIAL 1886
Cdd:COG1340 83 LNEKLNELREELDELRKELAElnkaggsiDKLRKEIERLEWRQQTEvlspEEEKELVEKIKELEkelEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1887 KEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDdtlKQRRVVEEEIRILKLNFEK 1966
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVE---AQEKADELHEEIIELQKEL 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1988774676 1967 AssgklDLELELNKLKNIADETQQSKIRAEEEAEK 2001
Cdd:COG1340 240 R-----ELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
72-191 |
7.40e-04 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 45.70 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 72 KTFTKWVNKHLIKAQrhVTDLYEDLRDGHNLISLLEVLSGE---TLPREKGR-------MRFHKLQNVQIALDFLRHRQV 141
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGF 459
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774676 142 KLVNIRNDDIADGNpKLTLGLIW-------TIILHFQVSSS--ISDIQVNGQSEDMTAK 191
Cdd:COG5069 460 SLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKDGcgLSDSDLCAWLGSLGLK 517
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
209-290 |
7.61e-04 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 42.29 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 209 RCDNFTTSWRDGKLFNAVIHKHYPRLIN---MGKVYQQTNLE-NLEQAFSVAEKdLGVTRLLDPEDVDVPHPDEksIITY 284
Cdd:cd21218 32 RVTNFSSDLKDGEVYALLLHSLAPELCDkelVLEVLSEEDLEkRAEKVLQAAEK-LGCKYFLTPEDIVSGNPRL--NLAF 108
|
....*.
gi 1988774676 285 VSSLYD 290
Cdd:cd21218 109 VATLFN 114
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
839-883 |
8.24e-04 |
|
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212702 [Multi-domain] Cd Length: 54 Bit Score: 40.33 E-value: 8.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1988774676 839 IQAVCDFK---QQEITVHKGDECALLNNSQPFKWKVLNRSGHEAMVPS 883
Cdd:cd11768 2 VVALYDFQpiePGDLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPS 49
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2247-2596 |
8.28e-04 |
|
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: 45.72 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2247 VEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAE------- 2319
Cdd:COG5185 188 LLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEqntdlrl 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2320 DDLNQQRALAEKMLKEKMQAIQEASRLKAE-AEMLQKQKDLA-----QEQAQKLLEDKQLMQQRLEEETEEYHKSLEVEr 2393
Cdd:COG5185 268 EKLGENAESSKRLNENANNLIKQFENTKEKiAEYTKSIDIKKateslEEQLAAAEAEQELEESKRETETGIQNLTAEIE- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2394 KRQLEIMAEAERLRLQVSQLSEAQARAEEEAK--KFKKQADKVATRLHETEIATQEKMTVVER-LEFERLNTSKEADDLR 2470
Cdd:COG5185 347 QGQESLTENLEAIKEEIENIVGEVELSKSSEEldSFKDTIESTKESLDEIPQNQRGYAQEILAtLEDTLKAADRQIEELQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2471 KAIADLENEKARLKKEAEELQNkskEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKA 2550
Cdd:COG5185 427 RQIEQATSSNEEVSKLLNELIS---ELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEK 503
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1988774676 2551 LKDEQERQKQQMEQEKKTLQATMDAALSKQKEA---EEEMLRKQKEMQE 2596
Cdd:COG5185 504 LRAKLERQLEGVRSKLDQVAESLKDFMRARGYAhilALENLIPASELIQ 552
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1339-1684 |
8.37e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1339 SDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEK 1418
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1419 EAQELKLKMQEEVSKREiaavDAEKQKTNIQLELQELknlsEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQK 1498
Cdd:COG4372 81 ELEELNEQLQAAQAELA----QAQEELESLQEEAEEL----QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1499 YTAESELKQLRDRAAEAEK-----LRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRM 1573
Cdd:COG4372 153 KELEEQLESLQEELAALEQelqalSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1574 QAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENS 1653
Cdd:COG4372 233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
330 340 350
....*....|....*....|....*....|.
gi 1988774676 1654 REEAEKELEKWRQKANEALRLRLQAEDEAHK 1684
Cdd:COG4372 313 LEDALLAALLELAKKLELALAILLAELADLL 343
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2262-2401 |
8.47e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2262 LKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQ 2341
Cdd:PRK00409 497 LGLPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ 576
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 2342 EA-SRLKAEAEMLQKQKDLAQEQAQKLLEDKQL--MQQRLEEETEEYHKSLEVERKRQLEIMA 2401
Cdd:PRK00409 577 QAiKEAKKEADEIIKELRQLQKGGYASVKAHELieARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1487-1586 |
8.69e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1487 IRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLA-QDEAEKLRKqvsEETQKKRQAEEeLKRKSEAEKEAAKQKQKAL 1565
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAsFERLAELRD---ELAELEEELEA-LKARWEAEKELIEEIQELK 477
|
90 100
....*....|....*....|.
gi 1988774676 1566 EDLEKLRMQAEEAERQVKQAE 1586
Cdd:COG0542 478 EELEQRYGKIPELEKELAELE 498
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2432-2632 |
8.71e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2432 DKVATRLHETEIATQEKMTVVERLEFERlNTSKEADDLRKAIADLE-NEKARLKKEAEelqnKSKEMADAQQKKIEHEKT 2510
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRRER-EKAERYQALLKEKREYEgYELLKEKEALE----RQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2511 vlqqtfmtekemllKKEKLIEDEKKRLESqfeeevkKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRK 2590
Cdd:TIGR02169 255 --------------KLTEEISELEKRLEE-------IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEK 313
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1988774676 2591 QKEMQELErqrlEQERILAEENQKLREKLQQLEDAQKDQHTR 2632
Cdd:TIGR02169 314 ERELEDAE----ERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2354-2586 |
9.11e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2354 QKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLE--IMAEAERLRLQVSQLSeaqaraeeeakkfKKQA 2431
Cdd:PRK05035 441 IEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAKDKdaVAAALARVKAKKAAAT-------------QPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2432 DKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKE-------------MA 2498
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEeevdpkkaavaaaIA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2499 DAQQKKIEHEKTVLQQTFMTEKEMLLK--------KEKLIEDEKKRLESQFEEE----------VKKAKALKDEQERQKQ 2560
Cdd:PRK05035 588 RAKAKKAAQQAASAEPEEQVAEVDPKKaavaaaiaRAKAKKAEQQANAEPEEPVdprkaavaaaIARAKARKAAQQQANA 667
|
250 260
....*....|....*....|....*...
gi 1988774676 2561 QMEQEKKTLQATMDAALS--KQKEAEEE 2586
Cdd:PRK05035 668 EPEEAEDPKKAAVAAAIAraKAKKAAQQ 695
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2797-2827 |
9.13e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 9.13e-04
10 20 30
....*....|....*....|....*....|.
gi 1988774676 2797 LLAERAVVGYKDPYTGGKISVFEAMKKGLIE 2827
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1177-1524 |
9.37e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1177 DSLEEELKKASAVSDKMVRVHserdvelDHFRQQLSSLQDRWKAVFTQIDLR--QRELEQLGRQLGYYREsydwlirwia 1254
Cdd:PRK04863 796 EELAERYATLSFDVQKLQRLH-------QAFSRFIGSHLAVAFEADPEAELRqlNRRRVELERALADHES---------- 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1255 daKQRQEKIQAvpitdsKTLKEQLAQEKKLL------------EEIEQNKDKVDECQKyAKAYIDtikdyelQLVAYKAQ 1322
Cdd:PRK04863 859 --QEQQQRSQL------EQAKEGLSALNRLLprlnlladetlaDRVEEIREQLDEAEE-AKRFVQ-------QHGNALAQ 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1323 VEPLVSPLKktkldsaSDNiiQEYVTLRTRYSELMTLTSQYIKFI---------------TDTQRRLDDEEKAAEKLKAe 1387
Cdd:PRK04863 923 LEPIVSVLQ-------SDP--EQFEQLKQDYQQAQQTQRDAKQQAfaltevvqrrahfsyEDAAEMLAKNSDLNEKLRQ- 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1388 erkKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKlkmqeevskreiAAVDAEKQktNIQLELQELKNL-------SE 1460
Cdd:PRK04863 993 ---RLEQAEQERTRAREQLRQAQAQLAQYNQVLASLK------------SSYDAKRQ--MLQELKQELQDLgvpadsgAE 1055
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 1461 QQIKDKSQQVDEALHS----RTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEK----LRKLAQD 1524
Cdd:PRK04863 1056 ERARARRDELHARLSAnrsrRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAgwcaVLRLVKD 1127
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2478-2629 |
9.76e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2478 NEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKL--IEDEKKRLESQFEEEVKKAKALKDEQ 2555
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIraLEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2556 ERQKQQMEQEKKTLQ-----------------------ATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQER-ILAEE 2611
Cdd:COG4942 100 EAQKEELAELLRALYrlgrqpplalllspedfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERaELEAL 179
|
170
....*....|....*...
gi 1988774676 2612 NQKLREKLQQLEDAQKDQ 2629
Cdd:COG4942 180 LAELEEERAALEALKAER 197
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1549-1743 |
1.03e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1549 RKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKtsklEESLKQ 1628
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK----EENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1629 EHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAL-RL-RLQAEdEAHKKTLaqeeaekqkeeaeREAKKR 1706
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELeRIsGLTAE-EAKEILL-------------EKVEEE 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 1988774676 1707 AKAEESAL-KQKEM-AEEELERQRKIAESTAQQKLTAEQ 1743
Cdd:PRK12704 167 ARHEAAVLiKEIEEeAKEEADKKAKEILAQAIQRCAADH 205
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1523-1602 |
1.10e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.33 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1523 QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAK------QKQKALE-DLEKLRMQAEEAERQvkqaeiEKEKQIKV 1595
Cdd:PRK11448 148 QQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGlaaeleEKQQELEaQLEQLQEKAAETSQE------RKQKRKEI 221
|
....*..
gi 1988774676 1596 AHEAAQK 1602
Cdd:PRK11448 222 TDQAAKR 228
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1701-2099 |
1.11e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1701 REAKKRAKAEESALKqkemAEEELERQRKiaestaqqKLTAEQE-LIRLRADFDNAEQQRSLLEDELYRLK---NEVAAA 1776
Cdd:PRK04863 276 RHANERRVHLEEALE----LRRELYTSRR--------QLAAEQYrLVEMARELAELNEAESDLEQDYQAASdhlNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1777 QQQRKQLEdelakvRSEMDILiQLKTKAEKETMSNTEKSKQLLEAEAAKmkDLAEEaSRLRAISEEAKHQRQIaeeEAAR 1856
Cdd:PRK04863 344 LRQQEKIE------RYQADLE-ELEERLEEQNEVVEEADEQQEENEARA--EAAEE-EVDELKSQLADYQQAL---DVQQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1857 QRAEAERilkEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHK--QEIEEKIVQLKKSSEA 1934
Cdd:PRK04863 411 TRAIQYQ---QAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQaaHSQFEQAYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1935 EMERQKAivDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNK---LKNIADETQQSKIRAEEEAEKLRKLALEEEK 2011
Cdd:PRK04863 488 EVSRSEA--WDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEA 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2012 RRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEkQIVVAQQAAQKCSAAEQQVQSVL--AQ 2089
Cdd:PRK04863 566 RLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLRE-QSGEEFEDSQDVTEYMQQLLEREreLT 644
|
410
....*....|
gi 1988774676 2090 QIEDSITQKK 2099
Cdd:PRK04863 645 VERDELAARK 654
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2182-2335 |
1.14e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2182 QQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVK------ 2255
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2256 -VQME-ELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKML 2333
Cdd:COG1579 93 aLQKEiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
..
gi 1988774676 2334 KE 2335
Cdd:COG1579 173 PP 174
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2314-2505 |
1.15e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2314 LRQIAEDDLNQQRALAEKMLKEKmqaiqeasrlKAEAEMLQKQKDL-AQEQAQKLledkqlmQQRLEEETEEYHKSLEve 2392
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEA----------KKEAEAIKKEALLeAKEEIHKL-------RNEFEKELRERRNELQ-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2393 rkrQLEimaeaERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETE--IATQEKMTVVERLEFERLN--TSKEADD 2468
Cdd:PRK12704 86 ---KLE-----KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEkkEEELEELIEEQLQELERISglTAEEAKE 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1988774676 2469 --LRKAIADLENEKARLKKEAEElqnKSKEMADAQQKKI 2505
Cdd:PRK12704 158 ilLEKVEEEARHEAAVLIKEIEE---EAKEEADKKAKEI 193
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2465-2566 |
1.17e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2465 EADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKkeklIEDEKKRLESQFEEE 2544
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEE----IQELKEELEQRYGKI 487
|
90 100
....*....|....*....|..
gi 1988774676 2545 VKKAKALKDEQERQKQQMEQEK 2566
Cdd:COG0542 488 PELEKELAELEEELAELAPLLR 509
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1638-1861 |
1.19e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1638 QEAERLKKQQEDAENSREEAEKELEkwrQKANEalrlrLQAEDEAHkktlaqeeaekqkeeaeRE-----AKKRAKAEES 1712
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRKKKEQ---QQAEE-----LQQKQAAE-----------------QErlkqlEKERLAAQEQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1713 ALKQKEMAEEELERQRKIAESTAQQ----KLTAEQELIRLRADFDNAEQQrslledelyrlKNEVAAAQQQRKQLEDELA 1788
Cdd:PRK09510 117 KKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAAKKAAAE-----------AKKKAEAEAAKKAAAEAKK 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 1789 KVRSEMdiliqlKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEA 1861
Cdd:PRK09510 186 KAEAEA------AAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2425-2605 |
1.25e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2425 KKFKKQADKVATRLHETEIATQEKmtvVERLEFERLntskEADDLRKAIADLENEKARLKKEAEELQNKSKEM----ADA 2500
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQER---LKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAakakAEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2501 QQK-------KIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQfeeevKKAKALKDEQERQKQQMEQEKKTLQATM 2573
Cdd:PRK09510 152 EAKraaaaakKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAE-----AKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
170 180 190
....*....|....*....|....*....|..
gi 1988774676 2574 DAALSKQKEAEEEMLRKQKEMQELERQRLEQE 2605
Cdd:PRK09510 227 AAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
63-171 |
1.27e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 41.90 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 63 ADERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLRH 138
Cdd:cd21337 14 APDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQD 93
|
90 100 110
....*....|....*....|....*....|...
gi 1988774676 139 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 171
Cdd:cd21337 94 GGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1958-2384 |
1.29e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1958 RILKLNFEKASSGKLDLELELNKLKNIADETQQ-SKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKA 2036
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2037 ALEELERLRKKAEEaRKQKDEADKEAEKQIvvaQQAAQKCSAAEQQVQSVLAQQIEDsitqkkLKEEYEKAKKLAKEAEA 2116
Cdd:COG4717 144 LPERLEELEERLEE-LRELEEELEELEAEL---AELQEELEELLEQLSLATEEELQD------LAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2117 AKEKAEREAALLRQQAEEAERQKTaaeeeaanqakAQEDAERLrKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLA- 2195
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELE-----------AAALEERL-KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2196 ---------EQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKN 2266
Cdd:COG4717 282 vlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2267 KI-----EEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLsveAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQ 2341
Cdd:COG4717 362 ELqleelEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELE 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1988774676 2342 EA-SRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEE 2384
Cdd:COG4717 439 EElEELEEELEELREELAELEAELEQLEEDGELAELLQELEELK 482
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1847-2023 |
1.30e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1847 RQIAEEEAARQRAEAERILKEklaAISEATRLKTEAEIALKEkeaENERLRRQAEDEAYQRKA----LEDQASQHKQEIE 1922
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEE---AKKEAEAIKKEALLEAKE---EIHKLRNEFEKELRERRNelqkLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1923 EKIVQLKKSsEAEMERQKAIVDDTLKQRRVVEEEIRILKLnfekassgKLDLELE--------------LNKLKNIADET 1988
Cdd:PRK12704 100 RKLELLEKR-EEELEKKEKELEQKQQELEKKEEELEELIE--------EQLQELErisgltaeeakeilLEKVEEEARHE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1988774676 1989 QQSKIR-----AEEEAEKlrklaleeekrrreaeeKVKKI 2023
Cdd:PRK12704 171 AAVLIKeieeeAKEEADK-----------------KAKEI 193
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1506-1606 |
1.36e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.47 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1506 KQLRDRAAEAEKLRKlaqdEAEKLRKQVSEETQK-KRQAEEELKrksEAEKEAAKQKQKALEDLEklrmqaEEAERQVKQ 1584
Cdd:COG0711 34 EKIADGLAEAERAKE----EAEAALAEYEEKLAEaRAEAAEIIA---EARKEAEAIAEEAKAEAE------AEAERIIAQ 100
|
90 100
....*....|....*....|..
gi 1988774676 1585 AEIEKEKQIKVAHEAAQKSAAA 1606
Cdd:COG0711 101 AEAEIEQERAKALAELRAEVAD 122
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2442-2563 |
1.36e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2442 EIATQ----EKMTVVERLEFErlntSKEADDLRKAIADLENEKAR---LKKEAE----ELQNKSKEMADAQQK--KIEHE 2508
Cdd:PTZ00491 658 EITTKsqeaAARHQAELLEQE----ARGRLERQKMHDKAKAEEQRtklLELQAEsaavESSGQSRAEALAEAEarLIEAE 733
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 2509 KTVlQQTFMTEKEMLLKKEKLIEDEKKRLE-------SQFEEEVKKAKALKD-EQERQKQQME 2563
Cdd:PTZ00491 734 AEV-EQAELRAKALRIEAEAELEKLRKRQEleleyeqAQNELEIAKAKELADiEATKFERIVE 795
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1655-1900 |
1.37e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1655 EEAE-KELEKWRQKANEAlRLRLQA-----EDEAhkktlaqeeaekqkeeAEREAKKRAKAEESALKQKEMAEEELER-Q 1727
Cdd:PRK05035 434 AKAEiRAIEQEKKKAEEA-KARFEArqarlEREK----------------AAREARHKKAAEARAAKDKDAVAAALARvK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1728 RKIAESTAQQKLTAEQE--------LIRLRADFDNAEQQRSLLEDELYRLKNEVAAA----QQQRKQLEDELAKVRSEMD 1795
Cdd:PRK05035 497 AKKAAATQPIVIKAGARpdnsaviaAREARKAQARARQAEKQAAAAADPKKAAVAAAiaraKAKKAAQQAANAEAEEEVD 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1796 iliQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEE-AKHQRQIAEEEAARQRAEAERILKEKLAAISE 1874
Cdd:PRK05035 577 ---PKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKAAVAAAIA 653
|
250 260
....*....|....*....|....*.
gi 1988774676 1875 ATRLKTEAEIALKEKEAENERLRRQA 1900
Cdd:PRK05035 654 RAKARKAAQQQANAEPEEAEDPKKAA 679
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2233-2632 |
1.41e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2233 LKDEVDDAVKQRGQVEEELFKVKVQMEELLK---LKNKIEEENQRLIKKDKDSTQKLLAE-EAENMRKLAEDAARLSVEA 2308
Cdd:pfam12128 198 VKSMIVAILEDDGVVPPKSRLNRQQVEHWIRdiqAIAGIMKIRPEFTKLQQEFNTLESAElRLSHLHFGYKSDETLIASR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2309 QEAarlRQIAEDDLNQQRALAEKMLKEKMQAI-QEASRLKAEAEMLQKQKDLAQEQAQklledkqlmqQRLEEETEEYHk 2387
Cdd:pfam12128 278 QEE---RQETSAELNQLLRTLDDQWKEKRDELnGELSAADAAVAKDRSELEALEDQHG----------AFLDADIETAA- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2388 sleverkrqleimAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRlheTEIATQEKMTVVERLEfERLNTSKEAD 2467
Cdd:pfam12128 344 -------------ADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRR---RSKIKEQNNRDIAGIK-DKLAKIREAR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2468 DLRKAIA--DLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLK--KEKLIEDEKKRLESQFEE 2543
Cdd:pfam12128 407 DRQLAVAedDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLenFDERIERAREEQEAANAE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2544 ------EVKKAKALKDEQERQKQQMEQEKKTLQATMDAA--------------LSKQKEAEEEMLRKQKEMQELERQ--- 2600
Cdd:pfam12128 487 verlqsELRQARKRRDQASEALRQASRRLEERQSALDELelqlfpqagtllhfLRKEAPDWEQSIGKVISPELLHRTdld 566
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 2601 -----------------RLEQERILAEE----NQKLREKLQQLEDAQKDQHTR 2632
Cdd:pfam12128 567 pevwdgsvggelnlygvKLDLKRIDVPEwaasEEELRERLDKAEEALQSAREK 619
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1756-1892 |
1.42e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1756 EQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSemdiliqLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASR 1835
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEA-------LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ 577
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774676 1836 LR--AISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAE 1892
Cdd:PRK00409 578 AIkeAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1882-2623 |
1.45e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.74 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1882 AEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILK 1961
Cdd:pfam07111 7 SDIPLVQSPGHQDVLERRLDTQRPTVTMWEQDVSGDGQGPGRRGRSLELEGSQALSQQAELISRQLQELRRLEEEVRLLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1962 lnfekassgkldlelelnklkniaDETQQSKIRAEEEAEKLRKLAleeekrrreaeekvkkiaaaeeeaaRQRKAALEEL 2041
Cdd:pfam07111 87 ------------------------ETSLQQKMRLEAQAMELDALA-------------------------VAEKAGQAEA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2042 ERLRKK---AEEARKQKDEAD-KEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDsiTQKKLKEeyekakklakeaeaa 2117
Cdd:pfam07111 118 EGLRAAlagAEMVRKNLEEGSqRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEG--LEKSLNS--------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2118 kekaereaaLLRQQAEEAERqktaaeeeaanQAKAQEDAERLRKEaefeaakraqaeaaalMQKQQADTEmakhkklAEQ 2197
Cdd:pfam07111 181 ---------LETKRAGEAKQ-----------LAEAQKEAELLRKQ----------------LSKTQEELE-------AQV 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2198 TLKQ---KFQVEQELTKVKLKLDETDKQKsvLDEELQRLKDEVDDAvkqrgQVEEELFKVKVQmeellklknkieeenqr 2274
Cdd:pfam07111 218 TLVEslrKYVGEQVPPEVHSQTWELERQE--LLDTMQHLQEDRADL-----QATVELLQVRVQ----------------- 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2275 likkdkDSTQKLLAEEAENMRKLAEDAarlSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQ 2354
Cdd:pfam07111 274 ------SLTHMLALQEEELTRKIQPSD---SLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQ 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2355 KQ-KDLAQEQA--QKLLEDK--QLMQQRLEEET--EEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKF 2427
Cdd:pfam07111 345 EQvTSQSQEQAilQRALQDKaaEVEVERMSAKGlqMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRV 424
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2428 KKQADKVATRLHETEIATQEKMTV---------VERLEFERLNTSKEA----DDLRKAIADLENEKARLKKE----AEEL 2490
Cdd:pfam07111 425 EQAVARIPSLSNRLSYAVRKVHTIkglmarkvaLAQLRQESCPPPPPAppvdADLSLELEQLREERNRLDAElqlsAHLI 504
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2491 QN---KSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKK 2567
Cdd:pfam07111 505 QQevgRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVA 584
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774676 2568 TLQATMDAALSKQKEAEEEMLRKQ------------KEMQELERQ---RLEQERILAEENQKLREKLQQLE 2623
Cdd:pfam07111 585 EVETRLREQLSDTKRRLNEARREQakavvslrqiqhRATQEKERNqelRRLQDEARKEEGQRLARRVQELE 655
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1399-1555 |
1.46e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 42.61 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1399 LDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQEL---KNLSEQQIKDKSQQVDEAlh 1475
Cdd:pfam08614 13 LDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELyrsRGELAQRLVDLNEELQEL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1476 srtkiEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEE--------L 1547
Cdd:pfam08614 91 -----EKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKEnrelverwM 165
|
....*....
gi 1988774676 1548 KRKS-EAEK 1555
Cdd:pfam08614 166 KRKGqEAEA 174
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1732-1835 |
1.48e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.94 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1732 ESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEmdiLIQLKTKAEKETMSN 1811
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQ---LEQLQEKAAETSQER 214
|
90 100
....*....|....*....|....
gi 1988774676 1812 TEKSKQLLEaEAAKMKDLAEEASR 1835
Cdd:PRK11448 215 KQKRKEITD-QAAKRLELSEEETR 237
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1525-1654 |
1.49e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 43.82 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1525 EAEKLRKQVSEETQK--KRQAEEELKR-KSEAEKEAakqkqkaleDLEKLRMQA--EEAERQVKQAEIEKEkqikvAHEA 1599
Cdd:cd03406 172 EAEKTKLLIAEQHQKvvEKEAETERKRaVIEAEKDA---------EVAKIQMQQkiMEKEAEKKISEIEDE-----MHLA 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774676 1600 AQKSAAAelqskhmsfAEKTSKleesLKQEHGAVLQLQQEAERLKKQQEDAENSR 1654
Cdd:cd03406 238 REKARAD---------AEYYRA----LREAEANKLKLTPEYLELKKYQAIANNTK 279
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3826-3859 |
1.51e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.51e-03
10 20 30
....*....|....*....|....*....|....
gi 1988774676 3826 LEAQTATGGIIDPEFQFHLPTDVAMQRGYINKET 3859
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2450-2629 |
1.52e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.48 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2450 TVVERLEFERLNTSKE----------ADDLRK--------AIADLENEK-----------ARLKKEAEELQN---KSKEM 2497
Cdd:COG2268 135 AVAAQMTVEELNEDREkfaekvqevaGTDLAKnglelesvAITDLEDENnyldalgrrkiAEIIRDARIAEAeaeRETEI 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2498 ADAQQKKIEHEKTVLQQTfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAK---ALKDEQERQKQQMEQEKKTLQATMD 2574
Cdd:COG2268 215 AIAQANREAEEAELEQER---EIETARIAEAEAELAKKKAEERREAETARAEaeaAYEIAEANAEREVQRQLEIAERERE 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2575 AALsKQKEAEEEMLRKQKEMQ---ELERQRLEQE------------RILAEENQKLREKLQQLEDAQKDQ 2629
Cdd:COG2268 292 IEL-QEKEAEREEAELEADVRkpaEAEKQAAEAEaeaeaeairakgLAEAEGKRALAEAWNKLGDAAILL 360
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2260-2413 |
1.61e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.62 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2260 ELLKLKNKIEEENQRlikkdkdstQKLLAEEAENmrklaedaarLSVEAQEAARlrqiaeddlnqqrALAEkmlkekmqA 2339
Cdd:PTZ00491 684 ERQKMHDKAKAEEQR---------TKLLELQAES----------AAVESSGQSR-------------AEAL--------A 723
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774676 2340 IQEASRLKAEAEMLQKQkdlAQEQAQKLLEDKQLMQQRLEEETE-EYHKS---LEVERKRQLEiMAEAERLRLQVSQL 2413
Cdd:PTZ00491 724 EAEARLIEAEAEVEQAE---LRAKALRIEAEAELEKLRKRQELElEYEQAqneLEIAKAKELA-DIEATKFERIVEAL 797
|
|
| Mcm10 |
pfam09332 |
Mcm10 replication factor; Mcm10 is a eukaryotic DNA replication factor that regulates the ... |
1513-1627 |
1.64e-03 |
|
Mcm10 replication factor; Mcm10 is a eukaryotic DNA replication factor that regulates the stability and chromatin association of DNA polymerase alpha.
Pssm-ID: 462760 Cd Length: 349 Bit Score: 43.98 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1513 AEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQ 1592
Cdd:pfam09332 133 AEAAKLAAIAKLKAKGGVLEKEDPNAVKRKRSDSGEIKERVEKNLESSSSSSPDEEEPALKKRREQLAYLKSEEFQKILN 212
|
90 100 110
....*....|....*....|....*....|....*
gi 1988774676 1593 IKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLK 1627
Cdd:pfam09332 213 AKSKHTGELKEAEAEMQERYFEPLVKKEQMEEKMR 247
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1709-2053 |
1.64e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.47 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1709 AEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQ---QQRKQLED 1785
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREerrQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1786 ELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEAS---RLRAISEEAKHQ--RQIAE--EEAARQR 1858
Cdd:pfam02029 84 ERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEEteiREKEYQENKWSTevRQAEEegEEEEDKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1859 AEAERILKE-------KLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKS 1931
Cdd:pfam02029 164 EEAEEVPTEnfakeevKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1932 SEAEMERQKaivddtLKQRRVVEEEirilkLNFEKASSGKLDLELELNKLKNIADEtqQSKIRAEEEaeklrklaleeek 2011
Cdd:pfam02029 244 LEAEQKLEE------LRRRRQEKES-----EEFEKLRQKQQEAELELEELKKKREE--RRKLLEEEE------------- 297
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1988774676 2012 RRREAEEKVKKIaaAEEEAARQRKaalEELERLRKKAEEARK 2053
Cdd:pfam02029 298 QRRKQEEAERKL--REEEEKRRMK---EEIERRRAEAAEKRQ 334
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2178-2342 |
1.69e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2178 LMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQ 2257
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2258 MEELLKLKNKIEEENQRLIKKDKDSTQKLlaEEAENMRK---LAEDAARLSVEAQE--AARLRQIAEDDLNQQRALAEKM 2332
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDNEL--YRVAGLTPeqaRKLLLKLLDAELEEekAQRVKKIEEEADLEAERKAQNI 181
|
170
....*....|
gi 1988774676 2333 LKEKMQAIQE 2342
Cdd:PRK12705 182 LAQAMQRIAS 191
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1374-1672 |
1.71e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.85 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1374 LDDEEKAAEKLKAEERKKMAEMQAELDK-QKQLAEAHAKAIAKAEKEAQELKLKMQEEvskreiaaVDAEKQKTNIQLEL 1452
Cdd:PLN03229 413 VDPERKVNMKKREAVKTPVRELEGEVEKlKEQILKAKESSSKPSELALNEMIEKLKKE--------IDLEYTEAVIAMGL 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1453 QE-LKNLSEQQIKDKSQqvDEALHSRTKIEEEIRLIRIQLETTEKQKYTAeseLKQLRDRAAEAEKLRKLAQ--DEAEKL 1529
Cdd:PLN03229 485 QErLENLREEFSKANSQ--DQLMHPVLMEKIEKLKDEFNKRLSRAPNYLS---LKYKLDMLNEFSRAKALSEkkSKAEKL 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1530 RKQVSEETqKKRQAEEELKRKSEAEK-EAAKQKQKALEDLEKlrMQAEEAERQVKQAEIEKEKQIKVAH----EAAQKSA 1604
Cdd:PLN03229 560 KAEINKKF-KEVMDRPEIKEKMEALKaEVASSGASSGDELDD--DLKEKVEKMKKEIELELAGVLKSMGleviGVTKKNK 636
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 1605 AAELQSKHMSFAEKTSKLEESLKQEHGAVLQ---LQQEAERLKKQQEDAENSREEAEKE-LEKWRQKANEAL 1672
Cdd:PLN03229 637 DTAEQTPPPNLQEKIESLNEEINKKIERVIRssdLKSKIELLKLEVAKASKTPDVTEKEkIEALEQQIKQKI 708
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3378-3416 |
1.77e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.85 E-value: 1.77e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1988774676 3378 YLQGSSSIAGLYLEPTKEKLSIYQAMKKKLLRHNTGLSL 3416
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1721-1941 |
1.77e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.56 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1721 EEELERQRKIAESTAQQKLTAEQELI-RLRADfdNAEQQRslLEDELYRLKNEVAAAQQQRKQLEDElaKVRSEMDILIQ 1799
Cdd:pfam15709 310 ESEEERSEEDPSKALLEKREQEKASRdRLRAE--RAEMRR--LEVERKRREQEEQRRLQQEQLERAE--KMREELELEQQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1800 LKTKAEKETMSNTEKSKQLLEAEAAKmKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKlaaiseatRLK 1879
Cdd:pfam15709 384 RRFEEIRLRKQRLEEERQRQEEEERK-QRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEK--------QRQ 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774676 1880 TEAEIALKEkeaENERLRRQAEDE--AYQRKaledqasqhKQEIEEKIVQlkkssEAEMERQKA 1941
Cdd:pfam15709 455 KELEMQLAE---EQKRLMEMAEEErlEYQRQ---------KQEAEEKARL-----EAEERRQKE 501
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2530-2611 |
1.83e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 41.06 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2530 IEDEKKRLES---QFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEM--LRKQKEMQELERQRLEQ 2604
Cdd:pfam20492 4 AEREKQELEErlkQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKerLEESAEMEAEEKEQLEA 83
|
....*..
gi 1988774676 2605 ERILAEE 2611
Cdd:pfam20492 84 ELAEAQE 90
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
2133-2301 |
1.86e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 44.75 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2133 EEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQ-KQQADTEMAKHKKLAEQT---LKQKFQVEQE 2208
Cdd:COG1193 521 EELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKaREEAEEILREARKEAEELireLREAQAEEEE 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2209 LTKVKLKLDETDKQksvLDEELQRLKD-----------EVDDAVK-----QRGQVEEE-----------LFKVKVQMEEL 2261
Cdd:COG1193 601 LKEARKKLEELKQE---LEEKLEKPKKkakpakppeelKVGDRVRvlslgQKGEVLEIpkggeaevqvgILKMTVKLSDL 677
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1988774676 2262 LKLKNKIEEENQRLIKKDKDSTQKLLAEEAE-NMR-KLAEDA 2301
Cdd:COG1193 678 EKVEKKKPKKPKKRPAGVSVSVSKASTVSPElDLRgMRVEEA 719
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1429-1586 |
1.86e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1429 EEVSKREIAAVDAEKQKTNIQLELQELKNLS--EQQIKDKSQQVDEalhsrtkIEEEIRLIRIQLETTEKQKYTAESELK 1506
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHEERELTeeEEEIRRLEEQVER-------LEAEVEELEAELEEKDERIERLERELS 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1507 QLRDRA-AEAEKLRKLA--QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQA-EEAERQV 1582
Cdd:COG2433 452 EARSEErREIRKDREISrlDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEAiRRLEEEY 531
|
....
gi 1988774676 1583 KQAE 1586
Cdd:COG2433 532 GLKE 535
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1427-1680 |
1.88e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1427 MQEEVSKREIAAVDAEKQKTniqleLQELKNLSEQQIKDKSQQVD-----EALHSRTKIEEEIRLIRiQLETTEKqkyTA 1501
Cdd:PRK05771 2 APVRMKKVLIVTLKSYKDEV-----LEALHELGVVHIEDLKEELSnerlrKLRSLLTKLSEALDKLR-SYLPKLN---PL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1502 ESELKQLRDRaaEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKsEAEKEAAKqKQKALE-DLEKLRM------- 1573
Cdd:PRK05771 73 REEKKKVSVK--SLEELIKDVEEELEKIEKEIKELEEEISELENEIKEL-EQEIERLE-PWGNFDlDLSLLLGfkyvsvf 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1574 -------QAEEAERQVKQAEIEKEKQIK-------VAHEAAQKSAAAELQSkhMSFAEKTSKLEESLKQehgAVLQLQQE 1639
Cdd:PRK05771 149 vgtvpedKLEELKLESDVENVEYISTDKgyvyvvvVVLKELSDEVEEELKK--LGFERLELEEEGTPSE---LIREIKEE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1988774676 1640 AERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAED 1680
Cdd:PRK05771 224 LEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAE 264
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
1510-1594 |
1.90e-03 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 43.71 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1510 DRAAEAEKLRKLAQDEAEKLRKQVSEETQKkrQAEEElkrKSEAEKEAAKQKQKALEDLEKLRMQAEEaerQVKQAEIEK 1589
Cdd:pfam07946 246 DKLAKRAKLRPEALKKAKKTREEEIEKIKK--AAEEE---RAEEAQEKKEEAKKKEREEKLAKLSPEE---QRKYEEKER 317
|
....*
gi 1988774676 1590 EKQIK 1594
Cdd:pfam07946 318 KKEQR 322
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1623-1857 |
1.95e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.17 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1623 EESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQaedeahkktlaqeeaekqkeeaere 1702
Cdd:pfam15709 340 AERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQ------------------------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1703 akkraKAEESALKQkemaeEELERQRKIAESTAQQKLTAEQELIRLRAdfdnAEQQRSLLEDELYRlkneVAAAQQQRKQ 1782
Cdd:pfam15709 395 -----RLEEERQRQ-----EEEERKQRLQLQAAQERARQQQEEFRRKL----QELQRKKQQEEAER----AEAEKQRQKE 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774676 1783 LEDELA---KVRSEMDILIQLKTKAEKEtmsnTEKSKQLLEAEAAKMKdlAEEASRLraISEEAKHQRQiaeeEAARQ 1857
Cdd:pfam15709 457 LEMQLAeeqKRLMEMAEEERLEYQRQKQ----EAEEKARLEAEERRQK--EEEAARL--ALEEAMKQAQ----EQARQ 522
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
552-646 |
1.98e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.39 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 552 LRYVQDLLAWVEENQRRIDNAEWGSDLPSMESQLGSHRGLHQTVEDFKSKIERAKADETQL---SPVSKGTYREYLGKLD 628
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1988774676 629 LQYGKLLNSSKSRLRNLE 646
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
1509-1586 |
2.04e-03 |
|
Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.
Pssm-ID: 459956 [Multi-domain] Cd Length: 136 Bit Score: 41.56 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1509 RDRAAEAEKLRKLA---QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALedLEKLRMQAEEAERQVKQA 1585
Cdd:pfam00836 57 RRKSLEAQKLKQLAekrEKEEEALQKADEENNNFSKMAEEKLKQKMEAYKENREAQIAAL--KEKLKEKEKHVEEVRKNK 134
|
.
gi 1988774676 1586 E 1586
Cdd:pfam00836 135 E 135
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2458-2635 |
2.15e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2458 ERLNTSKEADDLRKAIADLEN-----EKARLKKEA-EELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIE 2531
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERahealEDAREQIELlEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2532 DEkkrlesqfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEA-EEEMLRKQKEMQELERQRLEQER---- 2606
Cdd:COG4913 299 EL--------RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEAllaa 370
|
170 180 190
....*....|....*....|....*....|....*....
gi 1988774676 2607 ----------ILAEENQKLREKLQQLEDAQKDQHTRETD 2635
Cdd:COG4913 371 lglplpasaeEFAALRAEAAALLEALEEELEALEEALAE 409
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1628-1891 |
2.16e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1628 QEHGAVLQLQQEAER--LKKQQEDAENSREEAEKELEKWRQKANEAlrlRLQAEDEAHKKtlaqeeaekqkeeaerEAKK 1705
Cdd:PRK05035 433 QAKAEIRAIEQEKKKaeEAKARFEARQARLEREKAAREARHKKAAE---ARAAKDKDAVA----------------AALA 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1706 RAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQ----RK 1781
Cdd:PRK05035 494 RVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAAnaeaEE 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1782 QLEDELAKVRSEMdiliqLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEA-SRLRAISEEAKHQRQIAEEEAARQRAE 1860
Cdd:PRK05035 574 EVDPKKAAVAAAI-----ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKAAV 648
|
250 260 270
....*....|....*....|....*....|.
gi 1988774676 1861 AERILKEKlAAISEATRLKTEAEIALKEKEA 1891
Cdd:PRK05035 649 AAAIARAK-ARKAAQQQANAEPEEAEDPKKA 678
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2162-2481 |
2.30e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.90 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2162 EAEFEAAKRAQAEAAALMQKQQADTE-----MAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDE 2236
Cdd:pfam19220 82 EGELEELVARLAKLEAALREAEAAKEelrieLRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2237 VDDAVKQRGQVEEELFKVKVQMEE----LLKLKNKIEEENQRLikkdkdstqkllaeeAENMRKLAEDAARLSVEAQEAA 2312
Cdd:pfam19220 162 LATARERLALLEQENRRLQALSEEqaaeLAELTRRLAELETQL---------------DATRARLRALEGQLAAEQAERE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2313 RLRQIAEDDLNQQRAlAEKMLKEKMQAIQE----ASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEyhks 2388
Cdd:pfam19220 227 RAEAQLEEAVEAHRA-ERASLRMKLEALTAraaaTEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAG---- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2389 LEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLhETEIATQEKMTVVERLEFERLNtskeadd 2468
Cdd:pfam19220 302 LEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASL-SDRIAELTKRFEVERAALEQAN------- 373
|
330
....*....|...
gi 1988774676 2469 lRKAIADLENEKA 2481
Cdd:pfam19220 374 -RRLKEELQRERA 385
|
|
| V-ATPase_G_2 |
pfam16999 |
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ... |
1829-1927 |
2.32e-03 |
|
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex
Pssm-ID: 339878 [Multi-domain] Cd Length: 104 Bit Score: 40.50 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1829 LAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKE---KLAAISEATRLKTEAEIALKEKEAenerlRRQAEDEAy 1905
Cdd:pfam16999 7 LSELAEREAALDQQIEAARKEAEREVEAAEAEAARILREaeaKAKALQAEYRQELAAETARIREEA-----RARAEAEA- 80
|
90 100
....*....|....*....|..
gi 1988774676 1906 qrKALEDQASQHKQEIEEKIVQ 1927
Cdd:pfam16999 81 --QAVRTRAEGRLQQAVELILR 100
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2348-2586 |
2.38e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2348 AEAEMLQKQKDL--AQEQAQKLLEDKQLMQQRLEEETEEYhKSLEVERKrqlEIMAEAERLRLQVSQLSeaqaraeeeaK 2425
Cdd:COG3883 14 ADPQIQAKQKELseLQAELEAAQAELDALQAELEELNEEY-NELQAELE---ALQAEIDKLQAEIAEAE----------A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2426 KFKKQADKVATRLHeteiATQEKMTVVERLEFerLNTSKEADDLRKAIADLENEKARLKKEAEELQnkskemadAQQKKI 2505
Cdd:COG3883 80 EIEERREELGERAR----ALYRSGGSVSYLDV--LLGSESFSDFLDRLSALSKIADADADLLEELK--------ADKAEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2506 EHEKTVLQQtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEE 2585
Cdd:COG3883 146 EAKKAELEA----KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
.
gi 1988774676 2586 E 2586
Cdd:COG3883 222 A 222
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4301-4334 |
2.47e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.47e-03
10 20 30
....*....|....*....|....*....|....
gi 1988774676 4301 EETGPVAGILDIDTLEKVSVTEAIHRNLVDNITG 4334
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1617-1729 |
2.54e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1617 EKTSKLEESLKQEHGAVLQLQQEAERLKKQQED-AENSREEAEKELEKWRQKANEALRlrlQAEDEAHK--KTLAQEEAE 1693
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEkKEKLQEEEDKLLEEAEKEAQQAIK---EAKKEADEiiKELRQLQKG 599
|
90 100 110
....*....|....*....|....*....|....*.
gi 1988774676 1694 KQKEEAEREAKKRAKAEESALKQKEMAEEELERQRK 1729
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
1461-1572 |
2.54e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.
Pssm-ID: 214019 [Multi-domain] Cd Length: 161 Bit Score: 41.61 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1461 QQIKDKSQQVDEALHSRTKIEEEIRL-----------IRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQdeAEKL 1529
Cdd:cd12926 15 QQYQDKSREYDQLYEEYTRTSQELQMkrtaieafnetIKIFEEQGQTQEKCSKEYLERFRREGNEKEMQRILLN--SERL 92
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1988774676 1530 RKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLR 1572
Cdd:cd12926 93 KSRIAEIHESRTKLEQDLRAQASDNREIDKRMNSLKPDLMQLR 135
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1420-1871 |
2.56e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1420 AQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKY 1499
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1500 TAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEE--ELKRKSEAEKEAAKQKQKALEDLEKLRMQAEE 1577
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRkaEEEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1578 AERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEA 1657
Cdd:COG3064 162 AAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1658 EKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQ 1737
Cdd:COG3064 242 EAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1738 KLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQ 1817
Cdd:COG3064 322 AAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1988774676 1818 LLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAA 1871
Cdd:COG3064 402 GLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKAL 455
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
211-288 |
2.57e-03 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 39.98 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 211 DNFTTSWRDGKLFNAVIHK------HYPRLInmgkvyQQTNLENLEQAFSvAEKDLGVTRLLDPEDVDVPHPDEKSIITY 284
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNAlggsvpGWPNLD------PEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAY 92
|
....
gi 1988774676 285 VSSL 288
Cdd:cd21185 93 AAQL 96
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
2227-2382 |
2.63e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 44.21 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2227 DEELQRLKDEVDDAVkQRGQVEEELFKvkvQMEELlklknkieeenqrlikkdKDSTQKLLAEEAENMRKLAEDAARLSV 2306
Cdd:pfam13779 488 ERRLRAAQERLSEAL-ERGASDEEIAK---LMQEL------------------REALDDYMQALAEQAQQNPQDLQQPDD 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2307 EAQEAAR-------LRQIAEDDLNQQRALAEKMLKEkMQAIQEasRLKAeAEMlQKQKDLAQEQAQKLLEDKQLM---QQ 2376
Cdd:pfam13779 546 PNAQEMTqqdlqrmLDRIEELARSGRRAEAQQMLSQ-LQQMLE--NLQA-GQP-QQQQQQGQSEMQQAMDELGDLlreQQ 620
|
....*.
gi 1988774676 2377 RLEEET 2382
Cdd:pfam13779 621 QLLDET 626
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2199-2658 |
2.66e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2199 LKQKFQVEQ-ELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFkvkvQMEELLKLKNKIEEEnqrliK 2277
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN----ELSSLEDMKNRYESE-----I 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2278 KDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQK 2357
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2358 DlAQEQAQKLLEDkqLMQQRLEEETEE-----YHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKK--- 2429
Cdd:PRK01156 339 N-DYIKKKSRYDD--LNNQILELEGYEmdynsYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNein 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2430 -------------QADKVATRLHETEIatQEKMTVVE-RLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSK 2495
Cdd:PRK01156 416 vklqdisskvsslNQRIRALRENLDEL--SRNMEMLNgQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVK 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2496 EMAD--AQQKKIEH-------EKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQK------- 2559
Cdd:PRK01156 494 DIDEkiVDLKKRKEyleseeiNKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKrtswlna 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2560 --QQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHT-RETDK 2636
Cdd:PRK01156 574 laVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKlRGKID 653
|
490 500
....*....|....*....|..
gi 1988774676 2637 VLHKDIIHLTTIETTKTVYNGQ 2658
Cdd:PRK01156 654 NYKKQIAEIDSIIPDLKEITSR 675
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1399-1571 |
2.81e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1399 LDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNiqLELQELKNLSEQQIKDKSQQVDEAlhsrt 1478
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEAR--REREELQREEERLVQKEEQLDARA----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1479 kieEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEaeKLRKLAQDEAEKLRKQVSEETQKKrqAEEELKrkseaeKEAA 1558
Cdd:PRK12705 98 ---EKLDNLENQLEEREKALSARELELEELEKQLDN--ELYRVAGLTPEQARKLLLKLLDAE--LEEEKA------QRVK 164
|
170
....*....|...
gi 1988774676 1559 KQKQKALEDLEKL 1571
Cdd:PRK12705 165 KIEEEADLEAERK 177
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1587-1904 |
2.87e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.07 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1587 IEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEhgAVLQLQQEAERLKKQ--------------QEDAEN 1652
Cdd:PLN03229 413 VDPERKVNMKKREAVKTPVRELEGEVEKLKEQILKAKESSSKP--SELALNEMIEKLKKEidleyteaviamglQERLEN 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1653 SREEAEKELEKwRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEeSALKQKEMAEE-ELERQRKIA 1731
Cdd:PLN03229 491 LREEFSKANSQ-DQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAK-ALSEKKSKAEKlKAEINKKFK 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1732 ESTAQQKLTAEQELIRlradfDNAEQQRSLLEDELYR-LKNEVAAAqqqRKQLEDELAKVRSEMDILIQLKTKAEKETMS 1810
Cdd:PLN03229 569 EVMDRPEIKEKMEALK-----AEVASSGASSGDELDDdLKEKVEKM---KKEIELELAGVLKSMGLEVIGVTKKNKDTAE 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1811 NT------EKSKQLLEAEAAKMKDLAeEASRLRAISEEAKhqRQIAEEEAARQRAEAERI------LKEKLAAISEATRL 1878
Cdd:PLN03229 641 QTpppnlqEKIESLNEEINKKIERVI-RSSDLKSKIELLK--LEVAKASKTPDVTEKEKIealeqqIKQKIAEALNSSEL 717
|
330 340 350
....*....|....*....|....*....|...
gi 1988774676 1879 KT-----EAEIALKEK--EAENERLRRQAEDEA 1904
Cdd:PLN03229 718 KEkfeelEAELAAAREtaAESNGSLKNDDDKEE 750
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1539-1629 |
2.89e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.88 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1539 KKRQA--EEELKRKSEAEKEAAKQKQKALEDLEKLRmqaEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFA 1616
Cdd:cd06503 29 DEREEkiAESLEEAEKAKEEAEELLAEYEEKLAEAR---AEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIE 105
|
90
....*....|...
gi 1988774676 1617 EKTSKLEESLKQE 1629
Cdd:cd06503 106 QEKEKALAELRKE 118
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2154-2366 |
2.90e-03 |
|
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: 43.60 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2154 EDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRL 2233
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2234 KdevdDAVKQRGQVEEELFKVK----VQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAEnmrkLAEDAARLSVEAQ 2309
Cdd:COG4942 110 L----RALYRLGRQPPLALLLSpedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE----LEAERAELEALLA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774676 2310 EAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQK 2366
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2220-2405 |
2.93e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2220 DKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKL--KNKIEEENQRLIKKdkdstQKLLAEEAenmRKL 2297
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAqeQKKQAEEAAKQAAL-----KQKQAEEA---AAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2298 AEDAARLSVEAQE---AARLRQIAEDDLNQQRALAEKMLKEKMQAIQEA-SRLKAEAEMLQKQKDLAQEQAQKLLEDKQL 2373
Cdd:PRK09510 141 AAAAAKAKAEAEAkraAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAeAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|..
gi 1988774676 2374 MQQRLEEETEEYHKSLEVERKRQLEIMAEAER 2405
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| SH3_Eps8 |
cd11764 |
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ... |
848-883 |
2.93e-03 |
|
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar proteins; This group is composed of Eps8 and Eps8-like proteins including Eps8-like 1-3, among others. These proteins contain N-terminal Phosphotyrosine-binding (PTB), central SH3, and C-terminal effector domains. Eps8 binds either Abi1 (also called E3b1) or Rab5 GTPase activating protein RN-tre through its SH3 domain. With Abi1 and Sos1, it becomes part of a trimeric complex that is required to activate Rac. Together with RN-tre, it inhibits the internalization of EGFR. The SH3 domains of Eps8 and similar proteins recognize peptides containing a PxxDY motif, instead of the classical PxxP motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212698 [Multi-domain] Cd Length: 54 Bit Score: 38.78 E-value: 2.93e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1988774676 848 QEITVHKGDECALLNNSQPFkWKVLNRSGHEAMVPS 883
Cdd:cd11764 14 KELSVLKGEYLEVLDDSRQW-WKVRNSRGQVGYVPH 48
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2188-2571 |
3.07e-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: 44.17 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2188 MAKHKKLAEQtlkqkfqvEQELTKVKLKLDETDKQKSVLDEELQRLKDE---VDDAVKQRGQVEEelfkvkvQMEELLKL 2264
Cdd:COG3096 295 FGARRQLAEE--------QYRLVEMARELEELSARESDLEQDYQAASDHlnlVQTALRQQEKIER-------YQEDLEEL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2265 KNKIEEenqrlikkdkdstQKLLAEEAENMRKLAEDAARLSVEaqEAARLR-QIAED----DLNQQRALAekmLKEKMQA 2339
Cdd:COG3096 360 TERLEE-------------QEEVVEEAAEQLAEAEARLEAAEE--EVDSLKsQLADYqqalDVQQTRAIQ---YQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2340 IQEASRLKAEAEMLQKQKDLAQEQAQKllEDKQLMQQRLEEET---------EEYHKSL--------EVER----KRQLE 2398
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRA--KEQQATEEVLELEQklsvadaarRQFEKAYelvckiagEVERsqawQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2399 IMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADkvATRLHEtEIATQEKMTVVERLEFERLNTSKEA--DDLRKAIADL 2476
Cdd:COG3096 500 LLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQN--AERLLE-EFCQRIGQQLDAAEELEELLAELEAqlEELEEQAAEA 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2477 ENEKARLKKEAEELQNKSKEMAD------AQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKrlesqfeeevkkAKA 2550
Cdd:COG3096 577 VEQRSELRQQLEQLRARIKELAArapawlAAQDALERLREQSGEALADSQEVTAAMQQLLERERE------------ATV 644
|
410 420
....*....|....*....|.
gi 1988774676 2551 LKDEQERQKQQMEQEKKTLQA 2571
Cdd:COG3096 645 ERDELAARKQALESQIERLSQ 665
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2039-2629 |
3.19e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2039 EELERLRKKAEEARKQKDeadkeaekQIVVAQQAAQKCSAAEQQVQsvLAQQIEDSITQKKLKEEYEkakklakeaeaak 2118
Cdd:COG4913 235 DDLERAHEALEDAREQIE--------LLEPIRELAERYAAARERLA--ELEYLRAALRLWFAQRRLE------------- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2119 ekaereaaLLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALmQKQQADTEmakhKKLAEQT 2198
Cdd:COG4913 292 --------LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL-EREIERLE----RELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2199 LKQKfQVEQELTKVKLKLDETDKQksvLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLikk 2278
Cdd:COG4913 359 RRRA-RLEALLAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL--- 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2279 dkDSTQKLLAEEAENMRKLAEDAARLS-VEAQEAARLRQIAEDDLNQQRAlAEKML--------------KEKMQAIqEA 2343
Cdd:COG4913 432 --ERRKSNIPARLLALRDALAEALGLDeAELPFVGELIEVRPEEERWRGA-IERVLggfaltllvppehyAAALRWV-NR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2344 SRLKAEAEMLQKQKDLAQEQAQKLLED-----------------KQLMQQRL-------EEETEEYHKSL---------- 2389
Cdd:COG4913 508 LHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfrawlEAELGRRFdyvcvdsPEELRRHPRAItragqvkgng 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2390 ---------EVERKRQLEIMAEA--ERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLH---------ETEIATQEKM 2449
Cdd:COG4913 588 trhekddrrRIRSRYVLGFDNRAklAALEAELAELEEELAEAEERLEALEAELDALQERREalqrlaeysWDEIDVASAE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2450 TVVERLEFERLNTSKEADDLRKA---IADLENEKARLKKEAEELQNK----SKEMADAQQkKIEHEKTVLQQtfMTEKEM 2522
Cdd:COG4913 668 REIAELEAELERLDASSDDLAALeeqLEELEAELEELEEELDELKGEigrlEKELEQAEE-ELDELQDRLEA--AEDLAR 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2523 LLKKEKLieDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELER--Q 2600
Cdd:COG4913 745 LELRALL--EERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLAllD 822
|
650 660
....*....|....*....|....*....
gi 1988774676 2601 RLEQERiLAEENQKLREKLQQLEDAQKDQ 2629
Cdd:COG4913 823 RLEEDG-LPEYEERFKELLNENSIEFVAD 850
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1708-1875 |
3.21e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 42.66 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1708 KAEESALKQKEMAEEELerQRKIAESTAQQkltAEQELIRLRADfdnAEQQRSLLEDElyrlknevAAAQQQRKQLEDEL 1787
Cdd:pfam12037 46 KALELMKKQEQTRQAEL--QAKIKEYEAAQ---EQLKIERQRVE---YEERRKTLQEE--------TKQKQQRAQYQDEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1788 AKVRSEMDILIQLKTKAE-----------KETMSNTEKSKQLLEAEAakmkDLAEEASRLRAISE-EAK-HQRQIAEE-- 1852
Cdd:pfam12037 110 ARKRYQDQLEAQRRRNEEllrkqeesvakQEAMRIQAQRRQTEEHEA----ELRRETERAKAEAEaEARaKEERENEDln 185
|
170 180
....*....|....*....|....
gi 1988774676 1853 -EAARQRAEAERilKEKLAAISEA 1875
Cdd:pfam12037 186 lEQLREKANEER--ETVLESINTA 207
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2456-2638 |
3.26e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2456 EFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKskeMADAQQKKI-----EHEKTVLQQTFMTEKEMLLKKEKLI 2530
Cdd:COG3206 160 AYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAA---LEEFRQKNGlvdlsEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2531 EDEKKR--LESQFEEEVKKAKALKdeQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERIL 2608
Cdd:COG3206 237 EAEARLaaLRAQLGSGPDALPELL--QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
|
170 180 190
....*....|....*....|....*....|
gi 1988774676 2609 AEENQKLREKLQQLEDAQKDQHTRETDKVL 2638
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLA 344
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1637-1865 |
3.36e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1637 QQEAERLKKQQEDAENSREEAE----KELEKWRQKANEAlrlRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEES 1712
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQKQAAEqerlKQLEKERLAAQEQ---KKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1713 ALkqKEMAEEELERQRKIAESTAQQKLTAEQelirlradfdnaeqqrslledelyRLKNEVAAAQQQrkqleDELAKVRS 1792
Cdd:PRK09510 155 RA--AAAAKKAAAEAKKKAEAEAAKKAAAEA------------------------KKKAEAEAAAKA-----AAEAKKKA 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 1793 EMDIliqlKTKAEKEtmsntEKSKQLLEAEAAKMKDLAEEAsrlrAISEEAKHQRQIAEEEAARQRAEAERIL 1865
Cdd:PRK09510 204 EAEA----KKKAAAE-----AKKKAAAEAKAAAAKAAAEAK----AAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
1391-1624 |
3.40e-03 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 43.41 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1391 KMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIA---AVDAEKQKTNIQLELQELK----NLSEQQI 1463
Cdd:PRK15374 107 RLAVWQAMIESQKEMGIQVSKEFQTALGEAQEATDLYEASIKKTDTAksvYDAAEKKLTQAQNKLQSLDpadpGYAQAEA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1464 KdKSQQVDEALHSRTKIEeeirliriqlettekQKYTAESelKQLRDRAAEAEKlrklAQDEAEKLRKQVSEETQkkrqa 1543
Cdd:PRK15374 187 A-VEQAGKEATEAKEALD---------------KATDATV--KAGTDAKAKAEK----ADNILTKFQGTANAASQ----- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1544 eeelkrkseaeKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLE 1623
Cdd:PRK15374 240 -----------NQVSQGEQDNLSNVARLTMLMAMFIEIVGKNTEESLQNDLALFNALQEGRQAEMEKKSAEFQEETRKAE 308
|
.
gi 1988774676 1624 E 1624
Cdd:PRK15374 309 E 309
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1994-2490 |
3.42e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1994 RAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEK--QIVVAQQ 2071
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2072 AAQKCSAAEQQVQSvLAQQIEdsitqkKLKEEYEKAKKLAKEAEAAKEKAEReaalLRQQAEEAERQKTaaEEEAANQAK 2151
Cdd:COG4717 130 LYQELEALEAELAE-LPERLE------ELEERLEELRELEEELEELEAELAE----LQEELEELLEQLS--LATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2152 AQEDAERLRKE-AEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEEL 2230
Cdd:COG4717 197 LAEELEELQQRlAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2231 QRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKL--KNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEA 2308
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLGKEAEELQALpaLEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2309 QEAARLRQIAEDDLNQQRALA------EKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLmqQRLEEET 2382
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEEL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2383 EEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEaqaraeeeakkfkkqadkvATRLHETEIATQEKMTVVERLEFERLNT 2462
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEE-------------------DGELAELLQELEELKAELRELAEEWAAL 495
|
490 500
....*....|....*....|....*....
gi 1988774676 2463 SKEADDLRKAIADLENEKA-RLKKEAEEL 2490
Cdd:COG4717 496 KLALELLEEAREEYREERLpPVLERASEY 524
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
65-173 |
3.48e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 40.74 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 65 ERDRVQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 135
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1988774676 136 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQVS 173
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1801-1903 |
3.56e-03 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 43.76 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1801 KTKaeKETMSNT-EKSKqLLEAEAAKMKDLAEE------------ASRLRAISEEAKHQRQIAEEEAARQRAEAE--RIL 1865
Cdd:pfam04147 162 KSK--KEVMEEViAKSK-LHKYERQKAKEEDEElreeldkelkdlRSLLSGSKRPKPEQAKKPEEKPDRKKPDDDydKLV 238
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1988774676 1866 KE----KLAAISEatRLKTEAEIALKEKE----AENERLRR-QAEDE 1903
Cdd:pfam04147 239 RElafdKRAKPSD--RTKTEEELAEEEKErlekLEEERLRRmRGEED 283
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1355-1661 |
3.65e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1355 ELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELdkqKQLAEAHAKAIAKaEKEAQELKLKMQEEvsKR 1434
Cdd:pfam07888 45 ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEEL---RQSREKHEELEEK-YKELSASSEELSEE--KD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1435 EIAAVDAEKQktniqlelQELKNLsEQQIKDKSQQVDEalhsrtkIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAE 1514
Cdd:pfam07888 119 ALLAQRAAHE--------ARIREL-EEDIKTLTQRVLE-------RETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1515 AEK-LRKLAQD-------------EAEKLRKQVSEETQKKRQAEeelkrKSEAEKEAAKQKQKALEDLEKLRMQAEEA-E 1579
Cdd:pfam07888 183 TEEeLRSLSKEfqelrnslaqrdtQVLQLQDTITTLTQKLTTAH-----RKEAENEALLEELRSLQERLNASERKVEGlG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1580 RQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSK---------LEESLKQEHGAVLQLQQEAERLKKQQEDA 1650
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRarwaqeretLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
330
....*....|.
gi 1988774676 1651 ENSREEAEKEL 1661
Cdd:pfam07888 338 RMEREKLEVEL 348
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
2439-2559 |
3.73e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2439 HETEIATQEKMTVVERLEferlntsKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVlqQTFMT 2518
Cdd:COG2433 402 EHEERELTEEEEEIRRLE-------EQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREI--SRLDR 472
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1988774676 2519 EKEMLlkkEKLIEDEKKRLEsQFEEEVKKAKALKDEQERQK 2559
Cdd:COG2433 473 EIERL---ERELEEERERIE-ELKRKLERLKELWKLEHSGE 509
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1639-1915 |
3.77e-03 |
|
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: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1639 EAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEahkktlaqeeaekqkeeaEREAKKRAKAEESALKQke 1718
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE------------------LEALQAEIDKLQAEIAE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1719 mAEEELERQRKIAESTAQQKLTAEQELIRLRA-----DFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSE 1793
Cdd:COG3883 77 -AEAEIEERREELGERARALYRSGGSVSYLDVllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1794 MDILIQLKTKAEKETmsnTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAIS 1873
Cdd:COG3883 156 LAELEALKAELEAAK---AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1988774676 1874 EATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQAS 1915
Cdd:COG3883 233 AAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1351-1588 |
3.80e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.56 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1351 TRYSELMtltSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEahakaiaKAEKEAQELkLKMQEE 1430
Cdd:cd16269 44 AHYEEQM---EQRVQLPTETLQELLDLHAACEKEALEVFMKRSFKDEDQKFQKKLME-------QLEEKKEEF-CKQNEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1431 VSK-------REIAAVDAEKQKTNI-------QLELQELKNLSE--QQIKDKSQQVDEALH----SRTKIEEEIRLIRIQ 1490
Cdd:cd16269 113 ASSkrcqallQELSAPLEEKISQGSysvpggyQLYLEDREKLVEkyRQVPRKGVKAEEVLQeflqSKEAEAEAILQADQA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1491 LETTEKQKytaeselKQLRDRAAEAEKLRKLAQDEAEKLRKQVseETQKKRQAE--EELKRKSEAEKE-AAKQKQKALED 1567
Cdd:cd16269 193 LTEKEKEI-------EAERAKAEAAEQERKLLEEQQRELEQKL--EDQERSYEEhlRQLKEKMEEEREnLLKEQERALES 263
|
250 260
....*....|....*....|...
gi 1988774676 1568 L--EKLRMQAEEAERQVKQAEIE 1588
Cdd:cd16269 264 KlkEQEALLEEGFKEQAELLQEE 286
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
2527-2627 |
4.04e-03 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 43.50 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2527 EKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLqATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQER 2606
Cdd:pfam14817 65 DKGKAESRQSAAARRLELQKEIERLRAEISRLDKQLEARELEL-SREEAERERALDEISDSRHRQLLLEAYDQQCEEARK 143
|
90 100
....*....|....*....|.
gi 1988774676 2607 ILAEENQKLREKLQQLEDAQK 2627
Cdd:pfam14817 144 ILAEDHQRLQGQLQQLRDAAR 164
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2181-2409 |
4.19e-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: 42.98 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2181 KQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFK-VKVQME 2259
Cdd:pfam13868 58 EEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREeIDEFNE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2260 ELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARlsvEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQA 2339
Cdd:pfam13868 138 EQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEE---KEREIARLRAQQEKAQDEKAERDELRAKLYQEE 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 2340 IQEASRLKAEAEMLQKQK---DLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQ 2409
Cdd:pfam13868 215 QERKERQKEREEAEKKARqrqELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMK 287
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1480-1570 |
4.44e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.93 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1480 IEEEIRLIRIQLETTEKQKYTAESELKQLRDR----AAEAEKLRKLAQDEAEKLRKqvseetQKKRQAEEELKR-KSEAE 1554
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKlaeaRAEAAEIIAEARKEAEAIAE------EAKAEAEAEAERiIAQAE 102
|
90
....*....|....*.
gi 1988774676 1555 KEAAKQKQKALEDLEK 1570
Cdd:COG0711 103 AEIEQERAKALAELRA 118
|
|
| PRK01558 |
PRK01558 |
V-type ATP synthase subunit E; Provisional |
1516-1607 |
4.72e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 179302 Cd Length: 198 Bit Score: 41.67 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1516 EKLRKLAQDEAEKLRKQVSEETQKKRqaeEELKRKseAEKEAAKQKQKALEDLEKLRMQAEEAERQ-VKQAEIEKEKQIK 1594
Cdd:PRK01558 10 NKIKKDGLEEAERLANEIILEAKEEA---EEIIAK--AEEEAKELKAKAEKEANDYKRHALEASRQaGRDLLISFEKSIK 84
|
90
....*....|...
gi 1988774676 1595 VAHEAAQKSAAAE 1607
Cdd:PRK01558 85 SLFKAALKDEVAE 97
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1520-1938 |
4.77e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.25 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1520 KLAQDEAEKLRKQVS------EETQKkrQAEEELKRKSEAEKEAAKQKQKALEDLEKL------------RMQAEEAERQ 1581
Cdd:PRK10246 194 KSARTELEKLQAQASgvalltPEQVQ--SLTASLQVLTDEEKQLLTAQQQQQQSLNWLtrldelqqeasrRQQALQQALA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1582 VKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEK-- 1659
Cdd:PRK10246 272 AEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNtw 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1660 --ELEKWRQKANEALRLRL----QAEDEAHKKTLAQEEAEKQkeeaereaKKRAKAEESALkqkEMAEEELERQRkiAES 1733
Cdd:PRK10246 352 laEHDRFRQWNNELAGWRAqfsqQTSDREQLRQWQQQLTHAE--------QKLNALPAITL---TLTADEVAAAL--AQH 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1734 TAQQKLtaEQELIRLRAdfdnaeqQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEM----DILIQLKTKAEKE-T 1808
Cdd:PRK10246 419 AEQRPL--RQRLVALHG-------QIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYkektQQLADVKTICEQEaR 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1809 MSNTEKSKQLLEA---------------EAAKMKDLAEEASRLRAISEEAKhqrQIAEEEAA-------------RQRAE 1860
Cdd:PRK10246 490 IKDLEAQRAQLQAgqpcplcgstshpavEAYQALEPGVNQSRLDALEKEVK---KLGEEGAAlrgqldaltkqlqRDESE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1861 AERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAY-----QRKALEDQASQHKQEI---EEKIVQLKKSS 1932
Cdd:PRK10246 567 AQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQlrllsQRHELQGQIAAHNQQIiqyQQQIEQRQQQL 646
|
....*.
gi 1988774676 1933 EAEMER 1938
Cdd:PRK10246 647 LTALAG 652
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1827-1956 |
4.93e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1827 KDLAEEASRLRAISE-EAKHQRQIAEEEAARQRAEAErilKEKLAAISEATRLKTEAEIALK--EKEAENERLRRQAEDE 1903
Cdd:COG2268 191 RRKIAEIIRDARIAEaEAERETEIAIAQANREAEEAE---LEQEREIETARIAEAEAELAKKkaEERREAETARAEAEAA 267
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774676 1904 AYQRKALEDQASQHKQEIEEKIVQLK---KSSEAEMERQKAIVDDTLK-QRRVVEEE 1956
Cdd:COG2268 268 YEIAEANAEREVQRQLEIAEREREIElqeKEAEREEAELEADVRKPAEaEKQAAEAE 324
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
64-167 |
4.96e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 40.12 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 64 DERDRVQkktFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETL-------PREKGRM--RFHK 125
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIdervlnkPPRKNKPlnNFQM 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1988774676 126 LQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 167
Cdd:cd21294 81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
2453-2621 |
5.00e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.38 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2453 ERLEFERLN-TSKE------ADDLRkaiADLENEKARLKKEAEELQNKSK---EMADAQQKKIE-HEKTVLQQTFMTEKE 2521
Cdd:PLN03188 1047 KKLEQERLRwTEAEskwislAEELR---TELDASRALAEKQKHELDTEKRcaeELKEAMQMAMEgHARMLEQYADLEEKH 1123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2522 MLL-----KKEKLIEDEKKRL--------ESQFEEEVK-KAKALKDEQERQKQQMEQEKKTLQATM-DAA---------L 2577
Cdd:PLN03188 1124 IQLlarhrRIQEGIDDVKKAAaragvrgaESKFINALAaEISALKVEREKERRYLRDENKSLQAQLrDTAeavqaagelL 1203
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1988774676 2578 SKQKEAEEEMLRKQKEMQELERQrleqerilAEENQKLREKLQQ 2621
Cdd:PLN03188 1204 VRLKEAEEALTVAQKRAMDAEQE--------AAEAYKQIDKLKR 1239
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
70-167 |
5.32e-03 |
|
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409142 Cd Length: 116 Bit Score: 39.82 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 70 QKKTFTKWVNKHL---------IKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 135
Cdd:cd21293 2 EKGSYVDHINRYLgddpflkqfLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1988774676 136 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 167
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2357-2621 |
5.44e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2357 KDLAQEQAQKLLEDKQLMQQRleeeteeyhKSLEVERKRQLEIMAEAER-LRLQVSQLSeaqaraeeeakKFKKQADKVA 2435
Cdd:PRK11637 50 KSIQQDIAAKEKSVRQQQQQR---------ASLLAQLKKQEEAISQASRkLRETQNTLN-----------QLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2436 TRLH--ETEIATQEKMTvverleferlntskeADDLRKAIADLENEKARLKKEAEELQNKSKEMA------DAQQKKIEH 2507
Cdd:PRK11637 110 ASIAklEQQQAAQERLL---------------AAQLDAAFRQGEHTGLQLILSGEESQRGERILAyfgylnQARQETIAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2508 ektvLQQTfmtekemllkKEKLIEdEKKRLESQFEEEvkkaKALKDEQERQKQQMEQ----EKKTLqATMDAALSKQKE- 2582
Cdd:PRK11637 175 ----LKQT----------REELAA-QKAELEEKQSQQ----KTLLYEQQAQQQKLEQarneRKKTL-TGLESSLQKDQQq 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1988774676 2583 -----AEEEMLRKQKEMQELE-RQRLEQErilAEENQKLREKLQQ 2621
Cdd:PRK11637 235 lselrANESRLRDSIARAEREaKARAERE---AREAARVRDKQKQ 276
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2517-2632 |
5.58e-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: 42.21 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2517 MTEKEMLLKKEKlieDEKKRLESQFEEEVKKAKALKDEQERQ-KQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQ 2595
Cdd:pfam13868 28 IAEKKRIKAEEK---EEERRLDEMMEEERERALEEEEEKEEErKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMD 104
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774676 2596 ELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTR 2632
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAE 141
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1481-1588 |
5.58e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.41 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1481 EEEIRLIRIQLETTEKQKYTAESE----LKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKE 1556
Cdd:pfam05672 17 AEKRRQAREQREREEQERLEKEEEerlrKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQ 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1988774676 1557 AAKQKQK------ALEDLEKLR------MQAEEAERQVKQAEIE 1588
Cdd:pfam05672 97 ERLQKQKeeaeakAREEAERQRqerekiMQQEEQERLERKKRIE 140
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1517-1744 |
5.68e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1517 KLRKLAQDEAEKlRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVA 1596
Cdd:PRK11637 48 QLKSIQQDIAAK-EKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1597 heaAQKSAAAELQSKHmsfaektSKLEESLKQEHGavlqlqQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLrL 1676
Cdd:PRK11637 127 ---AAQLDAAFRQGEH-------TGLQLILSGEES------QRGERILAYFGYLNQARQETIAELKQTREELAAQKAE-L 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774676 1677 QAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAE-ESALKQK-----EMAEEELERQRKIAESTAQQKLTAEQE 1744
Cdd:PRK11637 190 EEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGlESSLQKDqqqlsELRANESRLRDSIARAEREAKARAERE 263
|
|
| MRP-S27 |
pfam10037 |
Mitochondrial 28S ribosomal protein S27; Members of this family of small ribosomal proteins ... |
1714-1867 |
5.70e-03 |
|
Mitochondrial 28S ribosomal protein S27; Members of this family of small ribosomal proteins possess one of three conserved blocks of sequence found in proteins that stimulate the dissociation of guanine nucleotides from G-proteins, leaving open the possibility that MRP-S27 might be a functional partner of GTP-binding ribosomal proteins.
Pssm-ID: 462947 [Multi-domain] Cd Length: 395 Bit Score: 42.43 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1714 LKQKEMAEEELERQRKIAESTAQQKLTAE--QELIRLRADFDNAEqqrsllEDELYRLKNEVAAAQQQRKQLEdELAKVR 1791
Cdd:pfam10037 259 LGKVGYLDRALSVMEKVASSPGDLKLHKEvlDVLQDILETLDELE------ESEQSKLPEYVKSFQELLSKLQ-SLGKVE 331
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774676 1792 SEmdILIQLKTKAEKETMSNTEKskQLLEAEAAKMKDLAEEasRLRAISEEAKHQrqiaeeEAARQRAEAERILKE 1867
Cdd:pfam10037 332 SE--SLLTLLENLVKESLPACEE--KDLANYEQLYQEWEEE--RRQLIQREKEMR------EKAEREDEARKALKE 395
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2263-2410 |
5.71e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.68 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2263 KLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQ---IAEDDLNQQRALAEKMLKEKMQA 2339
Cdd:pfam05262 181 KVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQkadFAQDNADKQRDEVRQKQQEAKNL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2340 ------------IQEASRLKAEAEMLQKQKDLAQEQAQKLLEDK--QLMQQRLEEETEEYHKSLEVERKRqLEIMAEAER 2405
Cdd:pfam05262 261 pkpadtsspkedKQVAENQKREIEKAQIEIKKNDEEALKAKDHKafDLKQESKASEKEAEDKELEAQKKR-EPVAEDLQK 339
|
....*
gi 1988774676 2406 LRLQV 2410
Cdd:pfam05262 340 TKPQV 344
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2305-2584 |
5.72e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 43.28 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2305 SVEAQEAARLRQIAEDDLNQQRALAEKmlkekmqAIQEASRLKAEAEMLQKQKDLAQEQAQklLEDKQlmQQRLEEETEE 2384
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK-------ERAEADRQRLEQEKQQQLAAISGSQSQ--LESTD--QNALETNGQA 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2385 YHKSLEVERKrqlEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQ-----ADKVATRLHETEIATQEKMTVVERLEFER 2459
Cdd:NF012221 1607 QRDAILEESR---AVTKELTTLAQGLDALDSQATYAGESGDQWRNPfagglLDRVQEQLDDAKKISGKQLADAKQRHVDN 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2460 LNTSKEAddLRKAIADLENEKaRLKKEAEelQNKSKEMADAQQKKiehektvlqqtfmteKEMLLKKEkliedEKKRLES 2539
Cdd:NF012221 1684 QQKVKDA--VAKSEAGVAQGE-QNQANAE--QDIDDAKADAEKRK---------------DDALAKQN-----EAQQAES 1738
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1988774676 2540 QFEEEVKKAKalkdeQERQKQQMEQEKKTLQATMDAALSKQKEAE 2584
Cdd:NF012221 1739 DANAAANDAQ-----SRGEQDASAAENKANQAQADAKGAKQDESD 1778
|
|
| iSH2_PIK3R1 |
cd12924 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
1461-1591 |
5.79e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 1, PIK3R1, also called p85alpha; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In addition, p85alpha, also called PIK3R1, contains N-terminal SH3 and GAP domains. p85alpha carry functions independent of its PI3K regulatory role. It can independently stimulate signaling pathways involved in cytoskeletal rearrangements. Insulin-sensitive tissues express splice variants of the PIK3R1 gene, p50alpha and p55alpha, which may play important roles in insulin signaling during lipid and glucose metabolism. Mice deficient with PIK3R1 die perinatally, indicating its importance in development.
Pssm-ID: 214017 [Multi-domain] Cd Length: 161 Bit Score: 40.83 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1461 QQIKDKSQQVDEALHSRTKIEEEIRLIRIQLET-TEKQKYTAESELKQLRDRAAEAEKLRKLAQDEA--------EKLRK 1531
Cdd:cd12924 15 TQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAfNETIKIFEEQCQTQERYSKEYIEKFKREGNEKEiqrimhnyEKLKS 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1532 QVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEK 1591
Cdd:cd12924 95 RISEIVDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKK 154
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3710-3746 |
5.81e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 5.81e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1988774676 3710 KQYLYGTGCVAGIT-TDSSSKLSIYQAMKRGFIKPEIG 3746
Cdd:smart00250 1 QRLLEAQSAIGGIIdPETGQKLSVEEALRRGLIDPETG 38
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
1389-1557 |
5.93e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 41.41 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1389 RKKMAEmqaeldkqKQLAEAHAKA---IAKAEKEAQELK----LKMQEEVSKREiaaVDAEKQKTNIQLELQELKNL--- 1458
Cdd:pfam12072 21 RKSIAE--------AKIGSAEELAkriIEEAKKEAETKKkealLEAKEEIHKLR---AEAERELKERRNELQRQERRllq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1459 SEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLEttEKQKYTAESELKQLrdraAEAEKLRKLAQDEAEK-LRKQVSEET 1537
Cdd:pfam12072 90 KEETLDRKDESLEKKEESLEKKEKELEAQQQQLE--EKEEELEELIEEQR----QELERISGLTSEEAKEiLLDEVEEEL 163
|
170 180
....*....|....*....|....*
gi 1988774676 1538 QKK-----RQAEEELKRksEAEKEA 1557
Cdd:pfam12072 164 RHEaavmiKEIEEEAKE--EADKKA 186
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1371-1639 |
6.04e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1371 QRRLDDEEKAAEKLKAEERKKMAEMQAELDK-----QKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQK 1445
Cdd:pfam15905 75 QKELEKEIRALVQERGEQDKRLQALEEELEKveaklNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGTQKKM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1446 TNIQLELQELKNLSEQQIKdksqqvdEALHSRTKIEeeirlirIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDE 1525
Cdd:pfam15905 155 SSLSMELMKLRNKLEAKMK-------EVMAKQEGME-------GKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1526 AEKLRKQVSEETQKKRQAeEELKRKSEAEKEAAKQKQKALEDL--------EKLRMQAEEAERQVKQAEIEKEKQIKVAH 1597
Cdd:pfam15905 221 TEKLLEYITELSCVSEQV-EKYKLDIAQLEELLKEKNDEIESLkqsleekeQELSKQIKDLNEKCKLLESEKEELLREYE 299
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1988774676 1598 EAAQkSAAAELQSkhmsfaektskLEESLKQEHGAVLQLQQE 1639
Cdd:pfam15905 300 EKEQ-TLNAELEE-----------LKEKLTLEEQEHQKLQQK 329
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1513-1592 |
6.28e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 39.73 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1513 AEAEKLRKlaqdEAEKLRKQVSEETQK-KRQAEEELKrksEAEKEAAKQKQKALEDLEklrmqaEEAERQVKQA--EIEK 1589
Cdd:cd06503 40 EEAEKAKE----EAEELLAEYEEKLAEaRAEAQEIIE---EARKEAEKIKEEILAEAK------EEAERILEQAkaEIEQ 106
|
...
gi 1988774676 1590 EKQ 1592
Cdd:cd06503 107 EKE 109
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2257-2404 |
6.37e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2257 QMEELLKLKNKIEEENQRLIKKdKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEK 2336
Cdd:COG2268 193 KIAEIIRDARIAEAEAERETEI-AIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIA 271
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774676 2337 MQAIQEASRLKAEAEMLQKQKDLAQEQAQKlledkqlmqqRLEEETEEYHKSLEVERKRQlEIMAEAE 2404
Cdd:COG2268 272 EANAEREVQRQLEIAEREREIELQEKEAER----------EEAELEADVRKPAEAEKQAA-EAEAEAE 328
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
1756-1921 |
6.49e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 40.42 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1756 EQQRSLLEDELYRLKNEVAaaqqqRKQLEDELAKVRSEMDILIQLKTKAEKETMsntekskqlleaeaakMKDLAEEASR 1835
Cdd:pfam15346 2 EAESKLLEEETARRVEEAV-----AKRVEEELEKRKDEIEAEVERRVEEARKIM----------------EKQVLEELER 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1836 LRAISEEAKHQRqiaEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEaenerlrRQAEDEAYQRKALEDQAS 1915
Cdd:pfam15346 61 EREAELEEERRK---EEEERKKREELERILEENNRKIEEAQRKEAEERLAMLEEQ-------RRMKEERQRREKEEEERE 130
|
....*.
gi 1988774676 1916 QHKQEI 1921
Cdd:pfam15346 131 KREQQK 136
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1705-1938 |
6.53e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 42.74 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1705 KRAKAEESALKQkemaeeELErqrkiaeSTAQQKLTAEQELIRLRADFDNAEQQ-RSLLEDELYRLKNEVAAAQQQ---- 1779
Cdd:pfam05911 20 EKAEAEALALKQ------QLE-------SVTLQKLTAEERAAHLDGALKECMQQlRNVKEEQEQKIHDVVLKKTKEweki 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1780 RKQLEDELAkvrsemdiliqlktkaeketmsntEKSKQLLEAEAakmkdlaeEASRL-RAISEEAKHQRQIAEEEAarqR 1858
Cdd:pfam05911 87 KAELEAKLV------------------------ETEQELLRAAA--------ENDALsRSLQERENLLMKLSEEKS---Q 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1859 AEAE-RILKEKLAAIS-EATRLKTEAEIALKEKEAENERL---RRQAEdeayqrkaledqaSQHKQEIE--EKIVQLkks 1931
Cdd:pfam05911 132 AEAEiEALKSRLESCEkEINSLKYELHVLSKELEIRNEEKnmsRRSAD-------------AAHKQHLEsvKKIAKL--- 195
|
....*..
gi 1988774676 1932 sEAEMER 1938
Cdd:pfam05911 196 -EAECQR 201
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
2496-2614 |
6.58e-03 |
|
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.
Pssm-ID: 434558 [Multi-domain] Cd Length: 154 Bit Score: 40.55 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2496 EMADAQQKKIEHEKTVLQQtfMTEKEmllkKEKLIEDEKKRLESQFEEEvkkakALKDEQERQKQQMEQEKKtlqatmda 2575
Cdd:pfam15236 46 ERERKRQKALEHQNAIKKQ--LEEKE----RQKKLEEERRRQEEQEEEE-----RLRREREEEQKQFEEERR-------- 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1988774676 2576 alsKQKEAEEEMLRKQKEM-QELER-----QRLEQERILAEENQK 2614
Cdd:pfam15236 107 ---KQKEKEEAMTRKTQALlQAMQKaqelaQRLKQEQRIRELAEK 148
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2476-2633 |
6.68e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.79 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2476 LENEKARLKKEAEELQNKSKEMADAQQKKIE-----HEKTVLQQTFMTEKEMLLKKEKLIEDE--KKRLESQ--FEEEVK 2546
Cdd:cd16269 108 KQNEEASSKRCQALLQELSAPLEEKISQGSYsvpggYQLYLEDREKLVEKYRQVPRKGVKAEEvlQEFLQSKeaEAEAIL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2547 KAKALKDEQERQKQqmEQEKKTLQATMDAALSKQKEAEEEMLRKQ-----KEMQELERQRLEQER--ILAEENQKLREKL 2619
Cdd:cd16269 188 QADQALTEKEKEIE--AERAKAEAAEQERKLLEEQQRELEQKLEDqersyEEHLRQLKEKMEEERenLLKEQERALESKL 265
|
170
....*....|....
gi 1988774676 2620 QQLEDAQKDQHTRE 2633
Cdd:cd16269 266 KEQEALLEEGFKEQ 279
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1376-1499 |
7.01e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1376 DEEKAAEKLKAEE-RKKMAEMQAeldkQKQLAEAHAKAIAKAEKEAQELKLKMQEEVskrEIAAVDAEKQKTNIQLELQE 1454
Cdd:PTZ00491 684 ERQKMHDKAKAEEqRTKLLELQA----ESAAVESSGQSRAEALAEAEARLIEAEAEV---EQAELRAKALRIEAEAELEK 756
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1988774676 1455 LKNLSEQQIKdksqqvdealHSRTKIEEEIRLIRiQLETTEKQKY 1499
Cdd:PTZ00491 757 LRKRQELELE----------YEQAQNELEIAKAK-ELADIEATKF 790
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1623-1972 |
7.09e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 42.40 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1623 EESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELekwrQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAERE 1702
Cdd:pfam03528 3 DEDLQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKEL----YLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1703 AKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIR--LRADFDNAE--QQRSLLEDELYRLKNEVAAAQQ 1778
Cdd:pfam03528 79 NIKAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVREYEVQfhRRLEQERAQwnQYRESAEREIADLRRRLSEGQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1779 QrKQLEDELAKVRSEMDILIQLKTKAEKETMS----NTEKSKQLLEAEAAKMKDL-----AEEASR--LRAISEEAKHQR 1847
Cdd:pfam03528 159 E-ENLEDEMKKAQEDAEKLRSVVMPMEKEIAAlkakLTEAEDKIKELEASKMKELnhyleAEKSCRtdLEMYVAVLNTQK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1848 QIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIAlKEKEAENERLRRQaedeAYQRKALEDQASQHKQEIEEKivq 1927
Cdd:pfam03528 238 SVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKA-NDQFLESQRLLMR----DMQRMESVLTSEQLRQVEEIK--- 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1988774676 1928 lKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKL 1972
Cdd:pfam03528 310 -KKDQEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVETSAPL 353
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2451-2556 |
7.13e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2451 VVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQN-KSKEMADAQQK--------KIEHEKTVLQQTFMTEKE 2521
Cdd:PRK00409 521 LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeEDKLLEEAEKEaqqaikeaKKEADEIIKELRQLQKGG 600
|
90 100 110
....*....|....*....|....*....|....*
gi 1988774676 2522 MLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQE 2556
Cdd:PRK00409 601 YASVKAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1495-1582 |
7.27e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 39.99 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1495 EKQKYTAESElKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEElkrksEAEKEAAKQKQKALEDLEKlrmQ 1574
Cdd:PRK07353 54 EAEKLEAQYE-QQLASARKQAQAVIAEAEAEADKLAAEALAEAQAEAQASKE-----KARREIEQQKQAALAQLEQ---Q 124
|
....*...
gi 1988774676 1575 AEEAERQV 1582
Cdd:PRK07353 125 VDALSRQI 132
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2368-2600 |
7.30e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2368 LEDKQLMQQRLEEETEEyHKSLEVERKRQleimAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRlheteiatqe 2447
Cdd:pfam15709 328 REQEKASRDRLRAERAE-MRRLEVERKRR----EQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLR---------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2448 kmtvVERLEFERLNTSKEAddlRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKiEHEKTVLQQTFMTEKEMLLKke 2527
Cdd:pfam15709 393 ----KQRLEEERQRQEEEE---RKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQE-EAERAEAEKQRQKELEMQLA-- 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 2528 klieDEKKRLESQFEEEvkkakalKDEQERQKQqmEQEKKTLQatmDAALSKQKEAEEEMLRKQKEMQELERQ 2600
Cdd:pfam15709 463 ----EEQKRLMEMAEEE-------RLEYQRQKQ--EAEEKARL---EAEERRQKEEEAARLALEEAMKQAQEQ 519
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1456-1738 |
7.31e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1456 KNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSE 1535
Cdd:pfam15905 54 RKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1536 ETQkkrqAEEELKRKSEAEKEAAKQKQKALEdLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAA--AELQSKHM 1613
Cdd:pfam15905 134 LTR----VNELLKAKFSEDGTQKKMSSLSME-LMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGkvAQLEEKLV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1614 SFA-EKTSKLEESLKQEHgAVLQLQQEAERLKKQQEDAENSREEAEKelekwRQKANEALRLRLQAEDEAHKKTLAQEEA 1692
Cdd:pfam15905 209 STEkEKIEEKSETEKLLE-YITELSCVSEQVEKYKLDIAQLEELLKE-----KNDEIESLKQSLEEKEQELSKQIKDLNE 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1988774676 1693 EKQKEEAEREAKKRAKAEESALKQKEMAE-EELERQRKIAESTAQQK 1738
Cdd:pfam15905 283 KCKLLESEKEELLREYEEKEQTLNAELEElKEKLTLEEQEHQKLQQK 329
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1933-2500 |
7.35e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1933 EAEMERQKAI---VDDTLKQRRVVEEEIRILKLNfeKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEE 2009
Cdd:pfam05557 1 RAELIESKARlsqLQNEKKQMELEHKRARIELEK--KASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2010 EKRRREAEEKVKKIAAAEEEAA-----------------RQRKAALEELERLRKKAEEARKQKDEADK---EAEKQIVVA 2069
Cdd:pfam05557 79 RLKKKYLEALNKKLNEKESQLAdarevisclknelselrRQIQRAELELQSTNSELEELQERLDLLKAkasEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2070 QQAAQKCSAAEQQVQSV---LAQQIEDSITQKKLKEEyekakklakeaeaaKEKAEREAALLRQQAEEAERQKTAAEEEA 2146
Cdd:pfam05557 159 EKQQSSLAEAEQRIKELefeIQSQEQDSEIVKNSKSE--------------LARIPELEKELERLREHNKHLNENIENKL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2147 ANQAKAQEDAERLRKEAEfeaakraqaeaaalMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVK-----LKLDETDK 2221
Cdd:pfam05557 225 LLKEEVEDLKRKLEREEK--------------YREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpedlsRRIEQLQQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2222 QKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQ-----KLLAEEAENMRK 2296
Cdd:pfam05557 291 REIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKerdgyRAILESYDKELT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2297 LAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQ--------EQAQKLL 2368
Cdd:pfam05557 371 MSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADpsyskeevDSLRRKL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2369 EDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEiATQEK 2448
Cdd:pfam05557 451 ETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLE-DDLEQ 529
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 2449 MTVVERLEFERLNtsKEADDLRKaiaDLENEKARLKKEAEELQNKSKEMADA 2500
Cdd:pfam05557 530 VLRLPETTSTMNF--KEVLDLRK---ELESAELKNQRLKEVFQAKIQEFRDV 576
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1523-1782 |
7.40e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1523 QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAeRQVKQAEIEKEKQIKvaheaAQK 1602
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQEL-REKRDELNEKVKELK-----EER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1603 SAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEA 1682
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1683 HKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAE--EELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRS 1760
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIElyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260
....*....|....*....|..
gi 1988774676 1761 LLEDELYRLKNEVAAAQQQRKQ 1782
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEK 262
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4307-4337 |
7.44e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.92 E-value: 7.44e-03
10 20 30
....*....|....*....|....*....|.
gi 1988774676 4307 AGILDIDTLEKVSVTEAIHRNLVDNITGQRL 4337
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
2211-2543 |
7.46e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.53 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2211 KVKLKLDETDKQKSV-LDEELQRLKDEVDDAVKQRGQVEEELFKvkvqmEELLKLKNKIEEENQRLIKKdKDSTQKLLAE 2289
Cdd:PLN03229 418 KVNMKKREAVKTPVReLEGEVEKLKEQILKAKESSSKPSELALN-----EMIEKLKKEIDLEYTEAVIA-MGLQERLENL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2290 EAENMRKLAEDAARLSVEAQEAARLRQiaEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLE 2369
Cdd:PLN03229 492 REEFSKANSQDQLMHPVLMEKIEKLKD--EFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKE 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2370 --DKQLMQQRLEEETEEYHKSleverkrqlEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQE 2447
Cdd:PLN03229 570 vmDRPEIKEKMEALKAEVASS---------GASSGDELDDDLKEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTAE 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2448 KMTVVE-RLEFERLN--TSKEADDLRKAiADLENEKARLKKeaeELQNKSKEMADAQQKKIEHEKTVLQQTF---MTEKE 2521
Cdd:PLN03229 641 QTPPPNlQEKIESLNeeINKKIERVIRS-SDLKSKIELLKL---EVAKASKTPDVTEKEKIEALEQQIKQKIaeaLNSSE 716
|
330 340
....*....|....*....|..
gi 1988774676 2522 MLLKKEKLIEDEKKRLESQFEE 2543
Cdd:PLN03229 717 LKEKFEELEAELAAARETAAES 738
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1721-1897 |
7.75e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1721 EEELER-QRKIAEST------AQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAkvrSE 1793
Cdd:PRK09039 52 DSALDRlNSQIAELAdllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELD---SE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1794 mdiliqlktkaeketmsnteksKQLLEAEAAKMKDLAEEASRLRaiseeakhqRQIAEEEAARQRAEAERilKEKLAAIS 1873
Cdd:PRK09039 129 ----------------------KQVSARALAQVELLNQQIAALR---------RQLAALEAALDASEKRD--RESQAKIA 175
|
170 180
....*....|....*....|....
gi 1988774676 1874 EatrLKTEAEIALKEKEAENERLR 1897
Cdd:PRK09039 176 D---LGRRLNVALAQRVQELNRYR 196
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
76-134 |
8.07e-03 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 38.76 E-value: 8.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774676 76 KWVNKHLikAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALD 134
Cdd:cd21184 8 EWVNSKI--PEYKVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPLENATKAMD 64
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2514-2634 |
8.09e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2514 QTFMTEKEMLLKKEKLIEDEKKRLESQFEEE--------VKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEE 2585
Cdd:pfam15709 301 QTFVVTGNMESEEERSEEDPSKALLEKREQEkasrdrlrAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELEL 380
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1988774676 2586 EMLRKQKEMQeLERQRLEQERILAEE---NQKLREKLQQLEDAQKDQHTRET 2634
Cdd:pfam15709 381 EQQRRFEEIR-LRKQRLEEERQRQEEeerKQRLQLQAAQERARQQQEEFRRK 431
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2458-2635 |
8.11e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.30 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2458 ERLNTSKEAD-DLRKAIADLeneKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQtfmteKEMLLKKEKLIEDEKKR 2536
Cdd:pfam05262 184 EALREDNEKGvNFRRDMTDL---KERESQEDAKRAQQLKEELDKKQIDADKAQQKADF-----AQDNADKQRDEVRQKQQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2537 LESQFEE--EVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERilaEENQK 2614
Cdd:pfam05262 256 EAKNLPKpaDTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQ---KKREP 332
|
170 180
....*....|....*....|.
gi 1988774676 2615 LREKLQQLEDAQKDQHTRETD 2635
Cdd:pfam05262 333 VAEDLQKTKPQVEAQPTSLNE 353
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1701-1792 |
8.18e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.54 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1701 REAKKRAKAEESALKQKE-MAEEELERQRKIAEsTAQQKLTAE--------QELIRLRADFDNAEQQRSLLEDELYRLKN 1771
Cdd:pfam07926 7 QSEIKRLKEEAADAEAQLqKLQEDLEKQAEIAR-EAQQNYERElvlhaediKALQALREELNELKAEIAELKAEAESAKA 85
|
90 100
....*....|....*....|....*
gi 1988774676 1772 EVAAAQ----QQRKQLEDELAKVRS 1792
Cdd:pfam07926 86 ELEESEesweEQKKELEKELSELEK 110
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
2371-2565 |
8.52e-03 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 41.86 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2371 KQLMQQRLEEETEEYHKSLEVERKRQLEI-MAEAERLRLQVSQLSeaqaraeeeakkfKKQADKVATRLHETEIATQEKM 2449
Cdd:COG4487 21 ADIVKQRRAEFEKELAERLADAAKREAALeLAEAKAKAQLQEQVA-------------EKDAEIAELRARLEAEERKKAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2450 TVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQ-QTFMTEKEMLLKKEK 2528
Cdd:COG4487 88 AVAEEKEKELAALQEALAEKDAKLAELQAKELELLKKERELEDAKREAELTVEKERDEELDELKeKLKKEEEEKQLAEKS 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1988774676 2529 LIEDEKkrlESQFEEEVKKAKALKDEQERQKQQMEQE 2565
Cdd:COG4487 168 LKVAEY---EKQLKDMQEQIEELKRKKEQGSTQLQGE 201
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
1491-1629 |
8.53e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 41.54 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1491 LETTEKQKYTAESELKQlrdraaeaEKLRKLAQDEAEKLRKQVSEETQKKRQAEEElkrksEAEKEAAKQKQKALEDLEK 1570
Cdd:PRK06669 30 LSIKEKERLREEEEEQV--------EQLREEANDEAKEIIEEAEEDAFEIVEAAEE-----EAKEELLKKTDEASSIIEK 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 1571 LRMQaeeAERQVKQAEIEKEKQIKVA----HEAAQKSAAAELQSKHMSFAEKTSKLEESLKQE 1629
Cdd:PRK06669 97 LQMQ---IEREQEEWEEELERLIEEAkaegYEEGYEKGREEGLEEVRELIEQLNKIIEKLIKK 156
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3987-4021 |
8.78e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 36.69 E-value: 8.78e-03
10 20 30
....*....|....*....|....*....|....*
gi 1988774676 3987 LLESQAATGYVIDPIKNLKLTVNEAVKMGIVGPEF 4021
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| SPFH_like_u4 |
cd03407 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1764-1912 |
9.01e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259805 [Multi-domain] Cd Length: 269 Bit Score: 41.42 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1764 DELYRLKNEVAaaqqqrKQLEDELAKVRSEMDILIqlktkaeketmsntekskqlleaEAAKMKDLAEEASRLRAISEEA 1843
Cdd:cd03407 106 DEVFESKDEIA------KAVKEELAKVMSEYGYEI-----------------------VKTLVTDIEPDASVKAAMNEIN 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774676 1844 KHQRqiaEEEAARQRAEAERILKEKLAaiseatrlkteaeialkekEAENERLRRQAEDEAYQRKALED 1912
Cdd:cd03407 157 AAQR---LREAAEEKAEAEKILQVKAA-------------------EAEAEAKRLQGVGIAEQRKAIVD 203
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2318-2628 |
9.58e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.98 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2318 AEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLledkqlmqQRLEEETEEYHKSLE--VERKR 2395
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKV--------KKLEATVETYKKKLEdlGDLRR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2396 QLEIMAEAERLRLQVSQLSEAQARAEEEAKK----FKKQADKVATRLheteiatQEKMTVVERLEFERLNTSKEADDLRK 2471
Cdd:pfam05622 153 QVKLLEERNAEYMQRTLQLEEELKKANALRGqletYKRQVQELHGKL-------SEESKKADKLEFEYKKLEEKLEALQK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2472 AIADLENEKARLKKEAEEL-----QNKSKEMADAQQKKIEHEKTVLQQTFMTekemLLKKEKLIedekkRLESQfeeevk 2546
Cdd:pfam05622 226 EKERLIIERDTLRETNEELrcaqlQQAELSQADALLSPSSDPGDNLAAEIMP----AEIREKLI-----RLQHE------ 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2547 kAKALKdeqERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEE----------NQKLR 2616
Cdd:pfam05622 291 -NKMLR---LGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQgskaedssllKQKLE 366
|
330
....*....|..
gi 1988774676 2617 EKLQQLEDAQKD 2628
Cdd:pfam05622 367 EHLEKLHEAQSE 378
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2427-2641 |
9.62e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2427 FKKQADKVATRLHETE--IATQEKMTVVERLEFERL--NTSKEADDLRKAiadLENEKARLKKEAEELQNKSKEMADAQQ 2502
Cdd:PTZ00121 1081 FDAKEDNRADEATEEAfgKAEEAKKTETGKAEEARKaeEAKKKAEDARKA---EEARKAEDARKAEEARKAEDAKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 2503 KKIEHEKTVlqqtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKE 2582
Cdd:PTZ00121 1158 RKAEDARKA-------EEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK 1230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774676 2583 AEEEMLRKQKEMQELERQRLEQERILAEENQ----KLREKLQQLEDAQKDQHTRETDKVLHKD 2641
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEIRKFEEARmahfARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1898-2100 |
9.70e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1898 RQAEDEAYQRKALEDQASQHKQEIEEkivqLKKSSEAEMERQKAivddtLKQRRVVEEEIRIlklnfEKASSGKLDLELE 1977
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEE----LQQKQAAEQERLKQ-----LEKERLAAQEQKK-----QAEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1978 LNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAAR-----QRKAALEELERLRKKAEEAR 2052
Cdd:PRK09510 132 KQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKaeaeaAAKAAAEAKKKAEAEAKKKA 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1988774676 2053 KQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKL 2100
Cdd:PRK09510 212 AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1640-1738 |
9.97e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 39.76 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774676 1640 AERLKKQQEDAEnsrEEAEKELEKWRQKANEalrLRLQAEDEAHKktlaqeeaekqkeeAEREAKKRAKAEesALKQKEM 1719
Cdd:PRK05759 47 AERAKKELELAQ---AKYEAQLAEARAEAAE---IIEQAKKRAAQ--------------IIEEAKAEAEAE--AARIKAQ 104
|
90
....*....|....*....
gi 1988774676 1720 AEEELERQRKIAESTAQQK 1738
Cdd:PRK05759 105 AQAEIEQERKRAREELRKQ 123
|
|
| |
