|
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 ... |
19-123 |
8.51e-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: 8.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 19 DRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKLVNI 98
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1988774686 99 RNDDIADGNPKLTLGLIWTIILHFQ 123
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
16-138 |
3.61e-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: 231.84 E-value: 3.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 16 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKL 95
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1988774686 96 VNIRNDDIADGNPKLTLGLIWTIILHFQvsssISDIQVNGQSE 138
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQ----ISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
15-136 |
5.93e-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: 5.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 15 KDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVK 94
Cdd:cd21236 11 KDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVK 90
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1988774686 95 LVNIRNDDIADGNPKLTLGLIWTIILHFQvsssISDIQVNGQ 136
Cdd:cd21236 91 LVNIRNDDITDGNPKLTLGLIWTIILHFQ----ISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
140-245 |
3.24e-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: 3.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 140 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 219
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1988774686 220 PEDVDVPHPDEKSIITYVSSLYDAMP 245
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
141-245 |
6.53e-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: 6.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 141 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 220
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1988774686 221 EDVDVPHPDEKSIITYVSSLYDAMP 245
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
16-137 |
1.23e-58 |
|
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: 198.72 E-value: 1.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 16 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKL 95
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1988774686 96 VNIRNDDIADGNPKLTLGLIWTIILHFQvsssISDIQVNGQS 137
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQ----ISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
141-245 |
3.41e-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: 3.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 141 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 220
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1988774686 221 EDVDVPHPDEKSIITYVSSLYDAMP 245
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
21-124 |
9.87e-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: 175.65 E-value: 9.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 21 VQKKTFTKWVNKHLIKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKLVNIR 99
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1988774686 100 NDDIADGNPKLTLGLIWTIILHFQV 124
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 ... |
11-120 |
3.81e-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: 171.78 E-value: 3.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 11 ITSLKDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLR 89
Cdd:cd21246 6 IKALADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLK 85
|
90 100 110
....*....|....*....|....*....|.
gi 1988774686 90 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21246 86 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
139-245 |
9.77e-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: 9.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 139 DMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLL 218
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1988774686 219 DPEDVDVPHPDEKSIITYVSSLYDAMP 245
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
141-241 |
1.25e-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: 1.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 141 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 220
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1988774686 221 EDVDVPHPDEKSIITYVSSLY 241
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
11-120 |
2.43e-45 |
|
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: 160.54 E-value: 2.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 11 ITSLKDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLr 89
Cdd:cd21193 6 IRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL- 84
|
90 100 110
....*....|....*....|....*....|.
gi 1988774686 90 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21193 85 KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
141-241 |
3.62e-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: 3.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 141 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 220
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1988774686 221 EDVDVPHPDEKSIITYVSSLY 241
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
17-124 |
6.12e-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: 156.38 E-value: 6.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 17 ERDRVQKKTFTKWVNKHLIKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLRHRQ 92
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1988774686 93 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 124
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
11-120 |
1.97e-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: 153.26 E-value: 1.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 11 ITSLKDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLR 89
Cdd:cd21318 28 IKALADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLK 107
|
90 100 110
....*....|....*....|....*....|.
gi 1988774686 90 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21318 108 EQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
8-120 |
2.24e-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: 150.20 E-value: 2.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 8 QKEITSLKDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALD 86
Cdd:cd21317 18 RSRIKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQ 97
|
90 100 110
....*....|....*....|....*....|....
gi 1988774686 87 FLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21317 98 FLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
17-124 |
1.03e-40 |
|
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: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 17 ERDRVQKKTFTKWVNKHLIKAQRH--VTDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLRHRQ 92
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 1988774686 93 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 124
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
876-953 |
1.64e-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: 142.36 E-value: 1.64e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774686 876 LSWQYLMRDFTQIRSWNITMLKTMKPEEYRLIMRNLELHYQDFMRDSQDSQLFGPDDRMQVEDDYTKSTQHFDNLLRS 953
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
20-241 |
2.23e-39 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 158.57 E-value: 2.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 20 RVQKKTFTKWVNKHLIKA-QRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLRHRQVKLV 96
Cdd:COG5069 8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 97 NIRNDDIADGNPKLTLGLIWTIILhfqvSSSISDIQvngQSEDMTAKEKLLLWSQRMTDGYQ-GIRCDNFTTSWRDGKLF 175
Cdd:COG5069 88 NIGPQDIVDGNPKLILGLIWSLIS----RLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774686 176 NAVIHKHYPRLINMGKVYQQTNLE--NLEQAFSVAEKDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLY 241
Cdd:COG5069 161 SALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
128-243 |
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 1988774686 128 ISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 207
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774686 208 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 243
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
137-241 |
5.03e-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: 5.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 137 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTR 216
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1988774686 217 LLDPEDVDVPHPDEKSIITYVSSLY 241
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
140-245 |
8.27e-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: 8.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 140 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 219
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1988774686 220 PEDVDVPHPDEKSIITYVSSLYDAMP 245
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
21-122 |
9.87e-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: 9.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 21 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLRHRQVKLVNI 98
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1988774686 99 RNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
19-120 |
1.20e-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: 138.29 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 19 DRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLRHRQVKLVN 97
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1988774686 98 IRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
17-124 |
1.93e-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: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 17 ERDRVQKKTFTKWVNKHLIKAQ--RHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVK 94
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1988774686 95 LVNIRNDDIADGNPKLTLGLIWTIILHFQV 124
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
140-241 |
4.55e-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: 4.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 140 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 219
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1988774686 220 PEDVDVPHPDEKSIITYVSSLY 241
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1296-1875 |
1.60e-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: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1296 QEYVTLRTRYSEL-MTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQlaeahakAIAKAEKEAQE 1374
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL-------ELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1375 LKLKMQEEVSKreiaavdAEKQKTNIQLELQELKNLSEQQIKDKSQqvdealhsRTKIEEEIRLIRIQLETTEKQKYTAE 1454
Cdd:COG1196 286 AQAEEYELLAE-------LARLEQDIARLEERRRELEERLEELEEE--------LAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1455 SELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQV 1534
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1535 KQAEIEKEKQIkvAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELE 1614
Cdd:COG1196 431 AELEEEEEEEE--EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1615 KWRQKANEALR------LRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQ 1688
Cdd:COG1196 509 GVKAALLLAGLrglagaVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1689 QKLTAEQELIRLRA-------DFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtm 1761
Cdd:COG1196 589 AAALARGAIGAAVDlvasdlrEADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS-- 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1762 snTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEK 1841
Cdd:COG1196 667 --RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
570 580 590
....*....|....*....|....*....|....
gi 1988774686 1842 EAENERLRRQAEDEAYQRKALEDQASQHKQEIEE 1875
Cdd:COG1196 745 EELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1320-2562 |
4.86e-36 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 151.90 E-value: 4.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1320 TDTQRRLDDEEKAAEKLKAEERKKMAEMQAELdkqkqlaeaHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEkqktn 1399
Cdd:NF041483 90 ADAERELRDARAQTQRILQEHAEHQARLQAEL---------HTEAVQRRQQLDQELAERRQTVESHVNENVAWAE----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1400 iqlelqELKNLSEQQIKdksQQVDEalhSRTKIEEEIRLIRIQLE--TTE-KQKYTAESELKQlrdraAEAEKLRKLAQD 1476
Cdd:NF041483 156 ------QLRARTESQAR---RLLDE---SRAEAEQALAAARAEAErlAEEaRQRLGSEAESAR-----AEAEAILRRARK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1477 EAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQaeEAERQVKQAEIEKEKQIKVAHEAAQKS- 1555
Cdd:NF041483 219 DAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAAAKQl 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1556 AAAELQSKHMSfaeKTSKLEeslkqehgaVLQLQQEAERlkkqqeDAENSREEAEKELEKWRQkanEALRLRLQAEDEAh 1635
Cdd:NF041483 297 ASAESANEQRT---RTAKEE---------IARLVGEATK------EAEALKAEAEQALADARA---EAEKLVAEAAEKA- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1636 kKTLAQEEAEKQKEEAEREAKK-RAKAEESALKQKEMAEEELERQRKIAESTAQqkltaeqeliRLRAD-FDNAEQQRSL 1713
Cdd:NF041483 355 -RTVAAEDTAAQLAKAARTAEEvLTKASEDAKATTRAAAEEAERIRREAEAEAD----------RLRGEaADQAEQLKGA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1714 LEDELYRLKNEVAAAQQQRKQLEDELAKVRSE-MDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEAsrlrais 1792
Cdd:NF041483 424 AKDDTKEYRAKTVELQEEARRLRGEAEQLRAEaVAEGERIRGEARREAVQQIEEAARTAEELLTKAKADADEL------- 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1793 eeakhqRQIAEEEAARQRAEAerilkeklaaISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQE 1872
Cdd:NF041483 497 ------RSTATAESERVRTEA----------IERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1873 IEEKIVQLKKS----------------------------SEAEMERQKAiVDDTLKQRRVVEEEIRILKLNFEK------ 1918
Cdd:NF041483 561 ETERAIAARQAeaaeeltrlhteaeerltaaeealadarAEAERIRREA-AEETERLRTEAAERIRTLQAQAEQeaerlr 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1919 ------ASSGKLDLE-----------LELNKLKNIADETQQsKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEE 1981
Cdd:NF041483 640 teaaadASAARAEGEnvavrlrseaaAEAERLKSEAQESAD-RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEET 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1982 AARQRKAALEELERLRKKAEE----ARKQKDEADKEAEKQIVVA-QQAAQKCSAAEQQvqsvlAQQIEDSIT--QKKLKE 2054
Cdd:NF041483 719 LGSARAEADQERERAREQSEEllasARKRVEEAQAEAQRLVEEAdRRATELVSAAEQT-----AQQVRDSVAglQEQAEE 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2055 EYEKakklakeaeaakekaereaalLRQQAEE-AERQKTaaeeeaanqaKAQEDAERLRKEAeFEAAKRAQAEAAALMQK 2133
Cdd:NF041483 794 EIAG---------------------LRSAAEHaAERTRT----------EAQEEADRVRSDA-YAERERASEDANRLRRE 841
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2134 QQADTEMAkhKKLAEQTLKQKFQvEQEltkvKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVK----VQ 2209
Cdd:NF041483 842 AQEETEAA--KALAERTVSEAIA-EAE----RLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQ 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2210 MEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMR-KLAEDAARLSVEAQ-EAARLRQIAEDDLNQQRALAEKMLKE 2287
Cdd:NF041483 915 ADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRaDAAAQAEQLIAEATgEAERLRAEAAETVGSAQQHAERIRTE 994
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2288 KMQAIQEASrlkAEAEMLQKQkdlAQEQAQKLL-EDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSqls 2366
Cdd:NF041483 995 AERVKAEAA---AEAERLRTE---AREEADRTLdEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTT--- 1065
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2367 eaqARAEEEAKKFKKQADKVATRLHETeiATQEKMTVVERleferlnTSKEADDL-----RKAIA---DLENEKARLKKE 2438
Cdd:NF041483 1066 ---TEAEAQADTMVGAARKEAERIVAE--ATVEGNSLVEK-------ARTDADELlvgarRDATAireRAEELRDRITGE 1133
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2439 AEELQNKSK-EMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQE 2517
Cdd:NF041483 1134 IEELHERARrESAEQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKAELVRE 1213
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....*
gi 1988774686 2518 KKTLQATMDAalskqkEAEEEMLRKQKEMQELERQRleqERILAE 2562
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) ... |
137-241 |
1.32e-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: 132.87 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 137 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTR 216
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1988774686 217 LLDPEDVDVPHPDEKSIITYVSSLY 241
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
16-124 |
1.56e-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: 132.35 E-value: 1.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 16 DERDRVQKKTFTKWVNKHLIKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVK 94
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1988774686 95 LVNIRNDDIADGNPKLTLGLIWTIILHFQV 124
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
144-245 |
9.73e-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: 9.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 144 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 222
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1988774686 223 VDVPHPDEKSIITYVSSLYDAMP 245
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1381-1956 |
9.83e-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: 9.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1381 EEVSKR----EIAAVDAEKQKTnIQLELQELK-NLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAES 1455
Cdd:COG1196 196 GELERQleplERQAEKAERYRE-LKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1456 ELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVK 1535
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1536 QAEIEKEKQIKVAHEAAQKSAAAE-----LQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAE 1610
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEeeleeLAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1611 KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK 1690
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1691 LTAEQELIRLRAD---FDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKS 1767
Cdd:COG1196 515 LLAGLRGLAGAVAvliGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1768 KQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAE--EEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAEn 1845
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAArlEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA- 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1846 ERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEkassgKLD 1925
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE-----ELL 748
|
570 580 590
....*....|....*....|....*....|.
gi 1988774686 1926 LELELNKLKNIADETQQskiraEEEAEKLRK 1956
Cdd:COG1196 749 EEEALEELPEPPDLEEL-----ERELERLER 774
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1286-2041 |
5.13e-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: 5.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1286 KLDSASDNIIQEYVTLRTRYSELMTLTSQY---IKFitdtqRRLDDEEKAAEKL-----KAEERKKMAEMQAELDKQKQL 1357
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLERQAekaERY-----KELKAELRELELAllvlrLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1358 AEAHAKAIAKAEKEAQELKLKMQE------------EVSKREIAAVDAEKQKTNiqlelQELKNLsEQQIKDKSQQVDEA 1425
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSEleeeieelqkelYALANEISRLEQQKQILR-----ERLANL-ERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1426 LHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEA 1505
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1506 EKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHgav 1585
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA--- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1586 lQLQQEAERLKKQQEDAENsREEAEKELEKWRQKANEAL-----RLRLQAEDEAHKKTLAQEEAEKQKEeaerEAKKRAK 1660
Cdd:TIGR02168 486 -QLQARLDSLERLQENLEG-FSEGVKALLKNQSGLSGILgvlseLISVDEGYEAAIEAALGGRLQAVVV----ENLNAAK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1661 AEESALKQKE-----MAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLK--NEVAAAQQQRK 1733
Cdd:TIGR02168 560 KAIAFLKQNElgrvtFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvDDLDNALELAK 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1734 QLEDELAKVRSEMDIL----IQLKtKAEKETMSNTEKSKQLLEAEaAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQ 1809
Cdd:TIGR02168 640 KLRPGYRIVTLDGDLVrpggVITG-GSAKTNSSILERRREIEELE-EKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1810 RAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEdQASQHKQEIEEKIVQLkkssEAEME 1889
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEEL----EAQIE 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1890 RQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAE 1969
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 1970 EKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQ 2041
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
8-120 |
7.38e-34 |
|
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: 129.39 E-value: 7.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 8 QKEITSLKDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALD 86
Cdd:cd21316 40 RSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQ 119
|
90 100 110
....*....|....*....|....*....|....
gi 1988774686 87 FLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21316 120 FLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
131-241 |
8.04e-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: 8.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 131 IQVNGQSEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEK 210
Cdd:cd21322 7 IETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQ 86
|
90 100 110
....*....|....*....|....*....|.
gi 1988774686 211 DLGVTRLLDPEDVDVPHPDEKSIITYVSSLY 241
Cdd:cd21322 87 HLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1321-1956 |
9.27e-34 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 144.90 E-value: 9.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1321 DTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAiAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTni 1400
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD-- 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1401 qlELQELKNLSEQQIKDKSQQVDEALHSRTKIEEeirliriqlettekqKYTAESELKQLRDRAAEAEKLRKLAqdEAEK 1480
Cdd:PTZ00121 1358 --EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE---------------KKKADEAKKKAEEDKKKADELKKAA--AAKK 1418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1481 LRKQVSEETQKKRQAeEELKRKSEAEKEAAKQKQKALEdleklrmqAEEAERQVKQAEiEKEKQIKVAHEAAQKSAAAEL 1560
Cdd:PTZ00121 1419 KADEAKKKAEEKKKA-DEAKKKAEEAKKADEAKKKAEE--------AKKAEEAKKKAE-EAKKADEAKKKAEEAKKADEA 1488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1561 QSKhmsfAEKTSKLEESLKQEHGAvlqlQQEAERLKKQQE--DAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKT 1638
Cdd:PTZ00121 1489 KKK----AEEAKKKADEAKKAAEA----KKKADEAKKAEEakKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1639 LAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRaDFDNAEQQRSLLEDEL 1718
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLK 1639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1719 YRLKNEVAAAQQQRKqlEDELAKVRSEmdiliQLKTKAEKEtmsnTEKSKQLLEAEAAKMKdlAEEASRLRAisEEAKHQ 1798
Cdd:PTZ00121 1640 KKEAEEKKKAEELKK--AEEENKIKAA-----EEAKKAEED----KKKAEEAKKAEEDEKK--AAEALKKEA--EEAKKA 1704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1799 RQIAEEEAARQRaEAERILKEKLAAISEATRLKTEAEialkEKEAENERLRRQAEDeayqrkalEDQASQHKQEIEEKIV 1878
Cdd:PTZ00121 1705 EELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEAE----EDKKKAEEAKKDEEE--------KKKIAHLKKEEEKKAE 1771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1879 QLKKSSEAEMErqKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAD----ETQQSKIRAEEEAEKL 1954
Cdd:PTZ00121 1772 EIRKEKEAVIE--EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDsaikEVADSKNMQLEEADAF 1849
|
..
gi 1988774686 1955 RK 1956
Cdd:PTZ00121 1850 EK 1851
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
141-241 |
2.88e-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: 2.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 141 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 220
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1988774686 221 EDVDVPHPDEKSIITYVSSLY 241
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1751-2621 |
1.14e-32 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 141.43 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1751 QLKTKAEKETmsnTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAE---EEAARQRAEAERILKEKLAAISEA 1827
Cdd:PTZ00121 1083 AKEDNRADEA---TEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEarkAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1828 TRLKTEAEIALKEKEAENERLRRQAEDeayQRKALEDQASQHKQEIE-----EKIVQLKKSSEAEMERQKAIVDDTLKQR 1902
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEaarkaEEERKAEEARKAEDAKKAEAVKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1903 RVVEEEIRIlklnfEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEA 1982
Cdd:PTZ00121 1237 KDAEEAKKA-----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1983 ARQRKA---------ALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSV--LAQQIEDSITQKK 2051
Cdd:PTZ00121 1312 EEAKKAdeakkkaeeAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkKADAAKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2052 LKEEyekakklakeaeaakekaereaalLRQQAEEAERQktaaEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALM 2131
Cdd:PTZ00121 1392 KADE------------------------AKKKAEEDKKK----ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA 1443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2132 QKQQADTEMAKHKKLAEQtLKQKFQVEQELTKVKLKLDETDKQksvldEELQRLKDEVDDAVKQRGQVEEElfkvKVQME 2211
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEE-AKKKAEEAKKADEAKKKAEEAKKA-----DEAKKKAEEAKKKADEAKKAAEA----KKKAD 1513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2212 ELLKLKNKIEEENQRLIKKDKDSTQKLLAEE---AENMRKLAE----DAARLSVEAQEAARLRQIAEDDLNQQRALAEKM 2284
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEkkkADELKKAEElkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2285 LKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERkrqleimaEAERLRLQVSQ 2364
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK--------AEEENKIKAAE 1665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2365 LSEAQARAEEEAKKFKKqADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQN 2444
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKK-AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2445 KSKEMA--DAQQKKIEH---EKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQfeeevKKAKALKDEQERQKQQMEQEKK 2519
Cdd:PTZ00121 1745 KAEEAKkdEEEKKKIAHlkkEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD-----KKIKDIFDNFANIIEGGKEGNL 1819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2520 TLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQK----LREKLQQLEDAQKDQHTRETDKVLHKDIi 2595
Cdd:PTZ00121 1820 VINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKeadfNKEKDLKEDDEEEIEEADEIEKIDKDDI- 1898
|
890 900
....*....|....*....|....*.
gi 1988774686 2596 hltTIETTKTVYNGQNVGDVVDGIDK 2621
Cdd:PTZ00121 1899 ---EREIPNNNMAGKNNDIIDDKLDK 1921
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
20-125 |
1.70e-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: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 20 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLRHRQ-VKLV 96
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 1988774686 97 NIRNDDIADGNPKLTLGLIWTIILHFQVS 125
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
21-124 |
2.11e-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: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 21 VQKKTFTKWVNKHLIKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKLVNIR 99
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1988774686 100 NDDIADGNPKLTLGLIWTIILHFQV 124
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1474-2327 |
2.37e-31 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 136.81 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1474 AQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRmQAEEAERQVKQAEIEKEKQIKVAHEAAQ 1553
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEAR-KAEDAKRVEIARKAEDARKAEEARKAED 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1554 -KSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDaenSREEAEKELEKWRQKANEALRLRLQAED 1632
Cdd:PTZ00121 1175 aKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA---KKAEAVKKAEEAKKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1633 EAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEEL---ERQRKIAESTAQQKLTAEQELIRLRADFDNAEQ 1709
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1710 QRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDiliQLKTKAEKEtmsntekskqllEAEAAKMKdlAEEASRLR 1789
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA---EKKKEEAKK------------KADAAKKK--AEEKKKAD 1394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1790 AISEEAKHQRQIAEE----EAARQRAEAeriLKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQ 1865
Cdd:PTZ00121 1395 EAKKKAEEDKKKADElkkaAAAKKKADE---AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1866 ASQHKQEIEEKIVQLKKSSEAEMERQKAivdDTLKQRrvveEEIRILKLNFEKASSGKLDLELELNKLKNIADETQqski 1945
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKA---DEAKKA----AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK---- 1540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1946 RAEE--EAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQ----RKAALEELERLRKKAEEARKQKDEADKEAEKQIV 2019
Cdd:PTZ00121 1541 KAEEkkKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2020 VAQQAAQkcsaaEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAA 2099
Cdd:PTZ00121 1621 KAEELKK-----AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2100 NQAKAQEDAERLRKEAEFEAAkraqaeaaalmQKQQADTEMAKHKKLAEQTLKQKfqvEQELTKV-KLKLDETDKQKsvl 2178
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKK-----------KAEELKKAEEENKIKAEEAKKEA---EEDKKKAeEAKKDEEEKKK--- 1758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2179 deeLQRLKDEVDDAVKQRGQVEEELFKvkvqmEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSV 2258
Cdd:PTZ00121 1759 ---IAHLKKEEEKKAEEIRKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDS 1830
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774686 2259 EAQEAArlrqiaeDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQ 2327
Cdd:PTZ00121 1831 AIKEVA-------DSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEK 1892
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
140-238 |
2.87e-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: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 140 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 219
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1988774686 220 PEDVDVPHPDEKSIITYVS 238
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
21-124 |
1.27e-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: 118.16 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 21 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLRHRQVKLVNI 98
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1988774686 99 RNDDIADGNPKLTLGLIWTIILHFQV 124
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
128-243 |
1.31e-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: 118.40 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 128 ISDIQvngqSEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 207
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774686 208 AEKDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLYDA 243
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
140-238 |
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 1988774686 140 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 219
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1988774686 220 PEDVDVPHPDEKSIITYVS 238
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
144-246 |
3.37e-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: 3.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 144 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLGVTRLLDPE 221
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1988774686 222 DVDVPHPDEKSIITYVSSLYDAMPR 246
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
144-245 |
9.31e-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: 9.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 144 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 222
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1988774686 223 VDVPHPDEKSIITYVSSLYDAMP 245
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
17-124 |
9.49e-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: 9.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 17 ERDRVQKKTFTKWVNKHLIKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLRHRQ 92
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|..
gi 1988774686 93 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 124
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQI 112
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
20-122 |
2.48e-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: 114.50 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 20 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 96
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1988774686 97 NIRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
146-241 |
3.49e-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: 3.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 146 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED-VD 224
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1988774686 225 VPHPDEKSIITYVSSLY 241
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1480-2090 |
6.73e-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: 6.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1480 KLRKqvsEETQKK-RQAEEELKRKSEAEKEAAKQkqkaledLEKLRMQAEEAER--QVKQAEIEKEKQIKVAH------- 1549
Cdd:COG1196 171 KERK---EEAERKlEATEENLERLEDILGELERQ-------LEPLERQAEKAERyrELKEELKELEAELLLLKlreleae 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1550 EAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQ 1629
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1630 AEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQ 1709
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1710 QRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLR 1789
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1790 AISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQH 1869
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1870 KQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEE 1949
Cdd:COG1196 561 AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1950 EAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCS 2029
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 2030 AAEQQVQSVLAQQIEdsITQKKLKEEYEKAKKLAKEAEAAKEKAEReaalLRQQAEEAERQ 2090
Cdd:COG1196 721 LEEEALEEQLEAERE--ELLEELLEEEELLEEEALEELPEPPDLEE----LERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1465-2321 |
3.97e-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: 125.94 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1465 AEAEKLRKLAQDEAEKLR-KQVSEETQKK-RQAEEELKRKSEAEKEAAKQkqkaledLEKLRMQAEEAER------QVKQ 1536
Cdd:TIGR02168 152 AKPEERRAIFEEAAGISKyKERRKETERKlERTRENLDRLEDILNELERQ-------LKSLERQAEKAERykelkaELRE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1537 AEIE---KEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAEN--SREEAEK 1611
Cdd:TIGR02168 225 LELAllvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeiSRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1612 ELEKWRQKANEALRLRLQAEDEAHKKTLAQEEaekqkeeaeREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKL 1691
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELA---------EELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1692 TAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDiliqlkTKAEKETMSNTEKSKQLL 1771
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE------EAELKELQAELEELEEEL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1772 EAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEaerilKEKLAAISEATRLKTEAEIALKEKEAEN------ 1845
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR-----LDSLERLQENLEGFSEGVKALLKNQSGLsgilgv 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1846 --ERLRRQAEDE----AYQRKALEDQASQHKQEIEEKIVQLKKSS-------EAEMERQKAIVDDTLKQRRVVEEEIRIL 1912
Cdd:TIGR02168 525 lsELISVDEGYEaaieAALGGRLQAVVVENLNAAKKAIAFLKQNElgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1913 KLNFEKASSGKLDLELELNKL---KNIADETQQSKIRAEEE-------------------AEKLRKLALEEEKRRREAEE 1970
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYLLGGVlvvDDLDNALELAKKLRPGYrivtldgdlvrpggvitggSAKTNSSILERRREIEELEE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1971 KVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDeadkEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQiedSITQK 2050
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELE----ELSRQISALRKDLARLEAEVEQLEERIAQL---SKELT 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2051 KLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTaaeEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAAL 2130
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK---ALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2131 MQKQQADTEMAKHKKLAEQTLK---QKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVK 2207
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESlaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2208 vqmEELLKLKNKIEEENQRLikkdkdstQKLLAEEAENMRKLAEDAarlSVEAQEAARLRQIAEDDLNQQRALAEKmLKE 2287
Cdd:TIGR02168 915 ---RELEELREKLAQLELRL--------EGLEVRIDNLQERLSEEY---SLTLEEAEALENKIEDDEEEARRRLKR-LEN 979
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1988774686 2288 K--------MQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLE 2321
Cdd:TIGR02168 980 KikelgpvnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
128-243 |
5.55e-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: 5.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 128 ISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 207
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774686 208 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 243
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
11-124 |
7.91e-27 |
|
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: 108.31 E-value: 7.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 11 ITSLKDERDRVQKKTFTKWVNKHLIKAQRHV--TDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDF 87
Cdd:cd21247 10 IRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITF 89
|
90 100 110
....*....|....*....|....*....|....*...
gi 1988774686 88 LRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQV 124
Cdd:cd21247 90 LKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
20-122 |
8.86e-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: 107.19 E-value: 8.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 20 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 96
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1988774686 97 NIRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
127-243 |
1.37e-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: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 127 SISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFS 206
Cdd:cd21290 3 AIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFE 78
|
90 100 110
....*....|....*....|....*....|....*...
gi 1988774686 207 VAEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 243
Cdd:cd21290 79 VAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1323-1882 |
5.36e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 119.09 E-value: 5.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1323 QRRLDDEEKAAEKL--KAEERKKMAEMQAELDKQKQLAEAHAKAiAKAEKEAQELKlKMQEEVSKREIAAVDAEKQKTNI 1400
Cdd:PTZ00121 1370 EKKKEEAKKKADAAkkKAEEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAK-KKAEEKKKADEAKKKAEEAKKAD 1447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1401 QLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAE----SELKQLRDRAAEAEKLRKL--A 1474
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkaAEAKKKADEAKKAEEAKKAdeA 1527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1475 QDEAEKLRKQVSEETQKKRQAEEELK----RKSEaEKEAAKQKQKALEDLEKLRMQAEEAeRQVKQAEIEK-----EKQI 1545
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKaeelKKAE-EKKKAEEAKKAEEDKNMALRKAEEA-KKAEEARIEEvmklyEEEK 1605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1546 KVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGavlQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALR 1625
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA---EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1626 lrlqAEDEAHKKtlaqeeaekqKEEAEREAKKRAKAEEsaLKQKEmaEEELERQRKIAESTAQQKLTAEQELIRLRADFD 1705
Cdd:PTZ00121 1683 ----AEEDEKKA----------AEALKKEAEEAKKAEE--LKKKE--AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1706 NAEQQRSLLEDelyrlKNEVaaaQQQRKQLEDELAKVRSEMDILIQ--LKTKAEKETMSNTEKSKQLL------------ 1771
Cdd:PTZ00121 1745 KAEEAKKDEEE-----KKKI---AHLKKEEEKKAEEIRKEKEAVIEeeLDEEDEKRRMEVDKKIKDIFdnfaniieggke 1816
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1772 ---------EAEAAKMKDLAEEASRLRAISEE-AKHQRQIAEEEAARQRAEA----ERILKEKLAAISEATRLKTEAEIA 1837
Cdd:PTZ00121 1817 gnlvindskEMEDSAIKEVADSKNMQLEEADAfEKHKFNKNNENGEDGNKEAdfnkEKDLKEDDEEEIEEADEIEKIDKD 1896
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1988774686 1838 LKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKK 1882
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 ... |
1654-2573 |
7.18e-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: 118.54 E-value: 7.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1654 EAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRadfDNAEQQRSLLEDELYRLKNEVAAAQQQRK 1733
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALE---YYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1734 QLEDELAKVRSEMDILIQLKTKAEKETmsntEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEA 1813
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKL----AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1814 ERILKEKLAAISEATRLKTEAEIALKEKEaENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKa 1893
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEIEELEKELK-ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1894 ivddtlKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIaDETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVK 1973
Cdd:pfam02463 395 ------EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI-LEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1974 KIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVaqqaaqkcsaaeQQVQSVLAQQIEDSITQKKLK 2053
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA------------LIKDGVGGRIISAHGRLGDLG 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2054 EEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQK 2133
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2134 QQADTEMAKHKKLAEQTLKQKFQveqelTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEEL 2213
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLK-----ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2214 lKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRklaedaarlsveaqeaARLRQIAEDDLNQQRALAEKMLKEKMQAIQ 2293
Cdd:pfam02463 691 -KEEILRRQLEIKKKEQREKEELKKLKLEAEELL----------------ADRVQEAQDKINEELKLLKQKIDEEEEEEE 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2294 EASRLKAEAEMLQKQkdlaQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAE 2373
Cdd:pfam02463 754 KSRLKKEEKEEEKSE----LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2374 EEAKKFKKQADKVATRLHETEIATQEKMTVverLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQ 2453
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAEEELERL---EEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEES 906
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2454 QKKIEHEKTVLQQTFMTEKEmlLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTL------------ 2521
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEE--AEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELgkvnlmaieefe 984
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 1988774686 2522 --QATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQ 2573
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 ... |
20-125 |
8.32e-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: 105.11 E-value: 8.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 20 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLRHRQVKLV 96
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1988774686 97 NIRNDDIADGNPKLTLGLIWTIILHFQVS 125
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1804-2587 |
1.45e-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: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1804 EEAA------RQRAEAERilkeKLAAISEA-TRLkteaEIALKEKEAENERLRRQAEdEAYQRKALEDQASQHK------ 1870
Cdd:TIGR02168 162 EEAAgiskykERRKETER----KLERTRENlDRL----EDILNELERQLKSLERQAE-KAERYKELKAELRELElallvl 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1871 --QEIEEKIVQLKkSSEAEMERQKAIVDDTLKqrrVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAE 1948
Cdd:TIGR02168 233 rlEELREELEELQ-EELKEAEEELEELTAELQ---ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1949 EEAEKLRKlaleeekrrreaeeKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKC 2028
Cdd:TIGR02168 309 ERLANLER--------------QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2029 SAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDA 2108
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2109 ERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQE----LTKVKLKLD----------ETDKQ 2174
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEgvkaLLKNQSGLSgilgvlseliSVDEG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2175 KS-----VLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKL 2249
Cdd:TIGR02168 535 YEaaieaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2250 A----------------EDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAI---QEASRLKAEAEMLQKQKD 2310
Cdd:TIGR02168 615 RkalsyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILerrREIEELEEKIEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2311 LAQEQAQKLLEDkqlmQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRL 2390
Cdd:TIGR02168 695 ELEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2391 HETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKsKEMADAQQKKIEHEKTVLQQTFMT 2470
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-LESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2471 EKEMLLKKEKLIEDEKKRLEsQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQ--E 2548
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIE-ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAqlE 928
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1988774686 2549 LERQRLEQEriLAEENQKLREKLQ-QLEDAQKDQHTRETD 2587
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 ... |
144-243 |
1.75e-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: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 144 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED- 222
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1988774686 223 VDVPHPDEKSIITYVSSLYDA 243
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1606-2240 |
2.49e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 116.19 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1606 REEAEKELEKWRQKANEALR-LRLQAEDEAHKKTLAQEEAekqkeeaeREAKKRAKAEESALKQKEMAEEELERQRKIAE 1684
Cdd:COG1196 195 LGELERQLEPLERQAEKAERyRELKEELKELEAELLLLKL--------RELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1685 STAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNT 1764
Cdd:COG1196 267 AELEE---LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1765 EKSKQLLEAEAAKMKDLAEEASRL----RAISEEAKHQRQIAEEEAARQRAEAErILKEKLAAISEATRLKTEAEIALKE 1840
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALleaeAELAEAEEELEELAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1841 KEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRI-LKLNFEKA 1919
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLlLLLEAEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1920 SSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKK 1999
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKI 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2000 AEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAqqiEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAAL 2079
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL---GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2080 LRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQ 2159
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2160 ELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQR---GQV----EEELFKVKVQMEELLKLKNKIEEENQRL---IK 2229
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIealGPVnllaIEEYEELEERYDFLSEQREDLEEARETLeeaIE 819
|
650
....*....|..
gi 1988774686 2230 K-DKDSTQKLLA 2240
Cdd:COG1196 820 EiDRETRERFLE 831
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1214-1883 |
3.18e-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: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1214 KIQAVPITDSKTLKEQLAQEKK--LLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVspLKKTKLDSAS 1291
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1292 DNIIQEYVTLRTRYSELmtltSQYIKFITDTQRRLDDEEKAAEKLKAEERKK-------MAEMQAELDKQKQLAEAHAKA 1364
Cdd:TIGR02168 284 EELQKELYALANEISRL----EQQKQILRERLANLERQLEELEAQLEELESKldelaeeLAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1365 IAKAEKEAQELKLKM---QEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEE-EIRLIR 1440
Cdd:TIGR02168 360 LEELEAELEELESRLeelEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1441 IQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAE---EELKRKSEAEKEAAKQK---- 1513
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLErlqENLEGFSEGVKALLKNQsgls 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1514 ----------------QKALEDLEKLRMQA---EEAERQVKQAEIEKEKQI-KVAHEAAQKSAAAELQSKHM-------- 1565
Cdd:TIGR02168 520 gilgvlselisvdegyEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELgRVTFLPLDSIKGTEIQGNDReilknieg 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1566 ---------SFAEKTSKLEESL--------------------------------------------KQEHGAVLQLQQEA 1592
Cdd:TIGR02168 600 flgvakdlvKFDPKLRKALSYLlggvlvvddldnalelakklrpgyrivtldgdlvrpggvitggsAKTNSSILERRREI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1593 ERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMA 1672
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1673 EEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSL-------LEDELYRLKNEVAAAQQQRKQLEDELAKVRSE 1745
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealdeLRAELTLLNEEAANLRERLESLERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1746 MDILIQlKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAIS 1825
Cdd:TIGR02168 840 LEDLEE-QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 1826 EATRLKTEAEIALKEKEAE----NERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKS 1883
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRidnlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
128-243 |
5.07e-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: 5.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 128 ISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 207
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774686 208 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 243
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
140-246 |
6.03e-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: 101.98 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 140 MTAKEKLLLWSQRMTDGY-QGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQT--NLENLEQAFSVAEKDLGVTR 216
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEfdKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1988774686 217 -LLDPEDVDvpHPDEKSIITYVSSLYDAMPR 246
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1323-2196 |
9.14e-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: 114.68 E-value: 9.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1323 QRRLDDEEKAAE----KLKAEERKKMAEMQAELDKQ---KQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEK 1395
Cdd:pfam02463 153 ERRLEIEEEAAGsrlkRKKKEALKKLIEETENLAELiidLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1396 QKTNIQLELQELKNLSEQQIKDKSQQVDEalhsrtKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQ 1475
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIE------KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1476 DEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKS 1555
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1556 AAA------ELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQ 1629
Cdd:pfam02463 387 SSAaklkeeELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1630 AEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQ-----QKLTAEQELIRLRADF 1704
Cdd:pfam02463 467 LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIIsahgrLGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1705 DNAEQQRSLLEDELYRLKNEVAA-------AQQQRKQLEDELAKVRS----EMDILIQLKTKAEKETMSNTEKSKQLLEA 1773
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRAltelplgARKLRLLIPKLKLPLKSiavlEIDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1774 EAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKlaaiseaTRLKTEAEIALKEKEAENERLRRQAE 1853
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTK-------ELLEIQELQEKAESELAKEEILRRQL 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1854 DEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRilklnfEKASSGKLDLELELNKL 1933
Cdd:pfam02463 700 EIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSR------LKKEEKEEEKSELSLKE 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1934 KNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKE 2013
Cdd:pfam02463 774 KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2014 AEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAErqkta 2093
Cdd:pfam02463 854 EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE----- 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2094 AEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMaKHKKLAEQTLKQKFQVEQELTKVKLKLDETDK 2173
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKV-NLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007
|
890 900
....*....|....*....|...
gi 1988774686 2174 QKSVLDEELQRLKDEVDDAVKQR 2196
Cdd:pfam02463 1008 IRAIIEETCQRLKEFLELFVSIN 1030
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
146-241 |
1.28e-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: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 146 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED-VD 224
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1988774686 225 VPHPDEKSIITYVSSLY 241
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1367-2297 |
2.79e-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: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1367 KAEKEAQELKL-KMQEEVSKREIAAVDAEKQKTNIQL------ELQELKN-LSEQQIKDKSQQVDEALHSRTKIEEEIRL 1438
Cdd:TIGR02168 171 KERRKETERKLeRTRENLDRLEDILNELERQLKSLERqaekaeRYKELKAeLRELELALLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1439 IRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALE 1518
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1519 DLEKLrmQAEEAERQVKQAEIEKEKQikvaheaAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQ 1598
Cdd:TIGR02168 331 KLDEL--AEELAELEEKLEELKEELE-------SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1599 QEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAqeeaekqkeeaereakKRAKAEESALKQKEMAEEELER 1678
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE----------------ELEEELEELQEELERLEEALEE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1679 QRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDeLYRLKNEVAAAQQQRKQLED---ELAKVRS--EMDILIQLK 1753
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEG-FSEGVKALLKNQSGLSGILGvlsELISVDEgyEAAIEAALG 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1754 TKAEKETMSNTEKSKQLLEA--EAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRA--------EAERILKEKLAA 1823
Cdd:TIGR02168 545 GRLQAVVVENLNAAKKAIAFlkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAkdlvkfdpKLRKALSYLLGG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1824 ISEATRLKTEAEIALKEKEAEN------ERLRRQAedeayqrkaledqasqhkqeieekiVQLKKSSEAEMERqkaivdd 1897
Cdd:TIGR02168 625 VLVVDDLDNALELAKKLRPGYRivtldgDLVRPGG-------------------------VITGGSAKTNSSI------- 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1898 tLKQRRvveeEIRILKLNFEKASSGKLDLELELNKLKNIADEtqqskirAEEEAEKLRKLALEEEKRRREAEEKVKKIAA 1977
Cdd:TIGR02168 673 -LERRR----EIEELEEKIEELEEKIAELEKALAELRKELEE-------LEEELEQLRKELEELSRQISALRKDLARLEA 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1978 AEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQqiedsitQKKLKEEYE 2057
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA-------LDELRAELT 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2058 KAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEaakraqaEAAALMQKQQAD 2137
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE-------LEALLNERASLE 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2138 TEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDdavKQRGQVEEElfkVKVQMEELLKLK 2217
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID---NLQERLSEE---YSLTLEEAEALE 960
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2218 NKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEdaarlsveaqeaarLRQIAE--DDLNQQRALAEKMLKEKMQAIQEA 2295
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKELGPVNLAAIEE--------------YEELKEryDFLTAQKEDLTEAKETLEEAIEEI 1026
|
..
gi 1988774686 2296 SR 2297
Cdd:TIGR02168 1027 DR 1028
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
24-121 |
3.40e-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: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 24 KTFTKWVNKHLIKA-QRHVTDLYEDLRDGHNLISLLEVLSGETLPREK---GRMRFHKLQNVQIALDFLRHRQVKLVNIR 99
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1988774686 100 NDDIADGnPKLTLGLIWTIILH 121
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1764-2439 |
3.67e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.34 E-value: 3.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1764 TEKSKQL--LEAEAAKmkdlaeeASRLRAISEEAKhQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEK 1841
Cdd:COG1196 196 GELERQLepLERQAEK-------AERYRELKEELK-ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1842 EAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAivdDTLKQRRVVEEEIRILKLNFEKASS 1921
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE---ELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1922 GKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLrkkaE 2001
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL----E 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2002 EARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLR 2081
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2082 QQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAaLMQKQQADTEMAKHKKLAEQTLKQKFQVEQEL 2161
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA-LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2162 TKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNK-IEEENQRLIKKDKDSTQKLLA 2240
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRrAVTLAGRLREVTLEGEGGSAG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2241 EEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLL 2320
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2321 EDKQLMQQRLEEETEEYHKSLEVErkrqlEIMAEAERLRLQVSQLSeaqaraeeeakkfkkqadKVATRlheteiATQEK 2400
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLE-----ELERELERLEREIEALG------------------PVNLL------AIEEY 790
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1988774686 2401 MTVVERLEF--ERLNT-SKEADDLRKAIADLENEKARLKKEA 2439
Cdd:COG1196 791 EELEERYDFlsEQREDlEEARETLEEAIEEIDRETRERFLET 832
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1591-2587 |
4.40e-24 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 112.61 E-value: 4.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1591 EAERLKKQQEDAENSREEAEKELEKWRQKANEALR------------LRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKR 1658
Cdd:NF041483 23 EMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRslasrpaydgadIGYQAEQLLRNAQIQADQLRADAERELRDARAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1659 AK------AEESALKQKEMAEEELERQRKIAESTAQQKLTAEQ---------ELIRLRADfdnaEQQRSLLEDELYRLKN 1723
Cdd:NF041483 103 TQrilqehAEHQARLQAELHTEAVQRRQQLDQELAERRQTVEShvnenvawaEQLRARTE----SQARRLLDESRAEAEQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1724 EVAAA--------QQQRKQLEDELAKVRSEMD-ILIQLKTKAEK----------ETMSNTEKSKQLLEAEAAKMKDLAEE 1784
Cdd:NF041483 179 ALAAAraeaerlaEEARQRLGSEAESARAEAEaILRRARKDAERllnaastqaqEATDHAEQLRSSTAAESDQARRQAAE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1785 ASR------------LRAISEEAKHQRQIAEEEAARQRAEAE-------RILKEKLA-----AISEATRLKTEAEIALKE 1840
Cdd:NF041483 259 LSRaaeqrmqeaeeaLREARAEAEKVVAEAKEAAAKQLASAEsaneqrtRTAKEEIArlvgeATKEAEALKAEAEQALAD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1841 KEAENERLRRQAEDEAyQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRilKLNFEKAS 1920
Cdd:NF041483 339 ARAEAEKLVAEAAEKA-RTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEAD--RLRGEAAD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1921 SGkldlelelNKLKNIA-DETQQSKIRA---EEEAEKLRKLAleeekrrreaeekvkkiaaaeeeaARQRKAALEELERL 1996
Cdd:NF041483 416 QA--------EQLKGAAkDDTKEYRAKTvelQEEARRLRGEA------------------------EQLRAEAVAEGERI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1997 RKKA-EEARKQKDEADKEAEKQIVVAQQAAQKC-SAAEQQVQSVLAQQIEDSITQKKLKEEyekakklakeaeaakekae 2074
Cdd:NF041483 464 RGEArREAVQQIEEAARTAEELLTKAKADADELrSTATAESERVRTEAIERATTLRRQAEE------------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2075 reaaLLRQQAEEAERQKTaaeeeaanqaKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQ-QADTEMAKHKKLAEQTLKq 2153
Cdd:NF041483 525 ----TLERTRAEAERLRA----------EAEEQAEEVRAAAERAARELREETERAIAARQaEAAEELTRLHTEAEERLT- 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2154 kfQVEQELTKVKlklDETDKQKSVLDEELQRLKDEVDDAVKQ-RGQVEEELFKVKVQMEE------------LLKLKNKI 2220
Cdd:NF041483 590 --AAEEALADAR---AEAERIRREAAEETERLRTEAAERIRTlQAQAEQEAERLRTEAAAdasaaraegenvAVRLRSEA 664
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2221 EEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQ-EAARLRQIAEDDLNQQRALAEkmlKEKMQAIQEASRLK 2299
Cdd:NF041483 665 AAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQeEAARRRREAEETLGSARAEAD---QERERAREQSEELL 741
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2300 AEAemlQKQKDLAQEQAQKLLED------------KQLMQQ------RLEEETEEYHKSLE------VERKRQlEIMAEA 2355
Cdd:NF041483 742 ASA---RKRVEEAQAEAQRLVEEadrratelvsaaEQTAQQvrdsvaGLQEQAEEEIAGLRsaaehaAERTRT-EAQEEA 817
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2356 ERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIAtqEKMTVVERLefeRLNTSKEADDLR----KAIADLENE 2431
Cdd:NF041483 818 DRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVS--EAIAEAERL---RSDASEYAQRVRteasDTLASAEQD 892
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2432 KARLKKEAEELQNKSKEMADAQQKKIEHEKTVlqqtfmtekemllkkekliEDEKKRLESQFEEEVKKAKALKDEQERQK 2511
Cdd:NF041483 893 AARTRADAREDANRIRSDAAAQADRLIGEATS-------------------EAERLTAEARAEAERLRDEARAEAERVRA 953
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2512 QQMEQEKKTLQATMDAALSKQKEAEEEMLRKQkemQELERQRLEQERILAE---ENQKLREKLQQ-----LEDAQKDQHT 2583
Cdd:NF041483 954 DAAAQAEQLIAEATGEAERLRAEAAETVGSAQ---QHAERIRTEAERVKAEaaaEAERLRTEAREeadrtLDEARKDANK 1030
|
....
gi 1988774686 2584 RETD 2587
Cdd:NF041483 1031 RRSE 1034
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
144-244 |
8.85e-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: 8.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 144 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPEDV 223
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1988774686 224 DVPHPDEKSIITYVSSLYDAM 244
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
141-241 |
1.13e-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: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 141 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 220
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1988774686 221 EDV---DVphPDEKSIITYVSSLY 241
Cdd:cd21198 80 ADMvllSV--PDKLSVMTYLHQIR 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1500-2442 |
1.18e-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: 110.92 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1500 KRKSEAEK--EAAKQKQKALED-LEKLRMQAEEAERQVKQAEieKEKQIKVAHEAAQKS-AAAELQSKHmsfaEKTSKLE 1575
Cdd:TIGR02168 172 ERRKETERklERTRENLDRLEDiLNELERQLKSLERQAEKAE--RYKELKAELRELELAlLVLRLEELR----EELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1576 ESLKQehgavlqLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREA 1655
Cdd:TIGR02168 246 EELKE-------AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1656 KKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQL 1735
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1736 EDELAKVRSEMDiliQLKTKAEKETmsnTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAER 1815
Cdd:TIGR02168 399 NNEIERLEARLE---RLEDRRERLQ---QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1816 ILKEKLAAISEATRLKTEAEIAlkekeaenERLRRQAEDEAYQRKALEDQASQHKQEIEE--KIVQLKKSSEAEME---- 1889
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSL--------ERLQENLEGFSEGVKALLKNQSGLSGILGVlsELISVDEGYEAAIEaalg 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1890 -RQKAIVDDTLKQrrvVEEEIRILKlnfeKASSGKLDLeLELNKLKniADETQQSKIRAEEEAEKLRKLALEEEKRRREA 1968
Cdd:TIGR02168 545 gRLQAVVVENLNA---AKKAIAFLK----QNELGRVTF-LPLDSIK--GTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1969 EEKVKKIAAAEEEAARQRKAaleeLERLRKKAEEARKQKDEADKEAEKQIVVAqqaaqkcsAAEQQVQSVLAQQIEdsit 2048
Cdd:TIGR02168 615 RKALSYLLGGVLVVDDLDNA----LELAKKLRPGYRIVTLDGDLVRPGGVITG--------GSAKTNSSILERRRE---- 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2049 qkkLKEeyekakklakeaeaakekaereaalLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAA 2128
Cdd:TIGR02168 679 ---IEE-------------------------LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2129 ALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKV 2208
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2209 QMEELLKLKNKIEEENQRLiKKDKDSTQKLLAEEAENMRKLAEDAARLSVEaqeaarlrqiaeddLNQQRALAEKM---- 2284
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESL-ERRIAATERRLEDLEEQIEELSEDIESLAAE--------------IEELEELIEELesel 875
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2285 ---LKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKsLEVERKRQLEIMAEAERLRLQ 2361
Cdd:TIGR02168 876 ealLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLE 954
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2362 -VSQLSEAQARAEEEAKKFKKQADKVATRLHETEI-ATQEKMTVVERLEFerlnTSKEADDLRKAIADLENEKARLKKEA 2439
Cdd:TIGR02168 955 eAEALENKIEDDEEEARRRLKRLENKIKELGPVNLaAIEEYEELKERYDF----LTAQKEDLTEAKETLEEAIEEIDREA 1030
|
...
gi 1988774686 2440 EEL 2442
Cdd:TIGR02168 1031 RER 1033
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
128-243 |
1.19e-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: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 128 ISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 207
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774686 208 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 243
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1226-1820 |
3.03e-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: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1226 LKEQLAQEKKLLEEIEQNKDKVDECQKyakayidTIKDYELQLVAYKAQVEplvsplkktKLDSASDNIIQEYVTLRTRY 1305
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEA-------ELAELEAELEELRLELE---------ELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1306 SELmtltSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSK 1385
Cdd:COG1196 298 ARL----EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1386 REiAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAA 1465
Cdd:COG1196 374 LA-EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1466 EA-EKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQ 1544
Cdd:COG1196 453 ELeEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1545 IKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKqehgavlqlQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAL 1624
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLK---------AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1625 RLRLQAEDEAHKKTLAQEEAEKQKEEAERE-AKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRAD 1703
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLEaALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1704 fdnAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAE 1783
Cdd:COG1196 684 ---LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1988774686 1784 EASRLRAISEEAKhqRQI---------AEEEAARQRAEAERILKEK 1820
Cdd:COG1196 761 DLEELERELERLE--REIealgpvnllAIEEYEELEERYDFLSEQR 804
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1653-2526 |
3.12e-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: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1653 REAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKltaeQELIRLRADFDNAEQQRSL-----LEDELYRLKNEVAA 1727
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKA----ERYKELKAELRELELALLVlrleeLREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1728 AQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtmsntekskqlLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAA 1807
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1808 RQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHkQEIEEKIVQLKKSSEAE 1887
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL-ETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1888 MERQKAIvDDTLKQ--RRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRR 1965
Cdd:TIGR02168 399 NNEIERL-EARLERleDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1966 REAEEKVKKIaaaeeeaaRQRKAALEEL-ERLRKKAEEARKQKDEADKEAEKQIVVAQQ--AAQKCSAAeqqVQSVLAQQ 2042
Cdd:TIGR02168 478 DAAERELAQL--------QARLDSLERLqENLEGFSEGVKALLKNQSGLSGILGVLSELisVDEGYEAA---IEAALGGR 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2043 IEDSITQKKlkeeyekAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKR 2122
Cdd:TIGR02168 547 LQAVVVENL-------NAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2123 AQAEAAALMQKQQADTEMAKHKK-------LAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQ 2195
Cdd:TIGR02168 620 YLLGGVLVVDDLDNALELAKKLRpgyrivtLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKA 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2196 RGQVEEELfkvkVQMEELLKLKNKIEEENQRLIkkdkDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLN 2275
Cdd:TIGR02168 700 LAELRKEL----EELEEELEQLRKELEELSRQI----SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2276 QQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKL---LEDKQLMQQRLEEETEEYHKSLEVERKRQLEIM 2352
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2353 AEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEK 2432
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2433 ARLKKEAEELQnkskemadaqqKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFE----------EEVKKAKA 2502
Cdd:TIGR02168 932 EGLEVRIDNLQ-----------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaiEEYEELKE 1000
|
890 900
....*....|....*....|....
gi 1988774686 2503 LKDEQERQKQQMEQEKKTLQATMD 2526
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEEAIE 1024
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
21-123 |
3.97e-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: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 21 VQKKTFTKWVNKHLIKAQRH--VTDLYEDLRDGHNLISLLEVLSGETLP-REKGRMRFHKLQNVQIALDFLRHRQ-VKLV 96
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*..
gi 1988774686 97 NIRNDDIADGNPKLTLGLIWTIILHFQ 123
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQ 108
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1748-2581 |
4.61e-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: 109.29 E-value: 4.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1748 ILIQLKtKAEKETMSNTEKSKQLLEAEA-AKMKDLAEEASR--LRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAI 1824
Cdd:pfam02463 137 FLVQGG-KIEIIAMMKPERRLEIEEEAAgSRLKRKKKEALKklIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1825 SEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKalEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIvddtlkqrrv 1904
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE--EIESSKQEIEKEEEKLAQVLKENKEEEKEKKL---------- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1905 VEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAAR 1984
Cdd:pfam02463 284 QEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1985 QRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAA--EQQVQSVLAQQIEDSITQKKLKEEYEKAKKL 2062
Cdd:pfam02463 364 LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLleLARQLEDLLKEEKKEELEILEEEEESIELKQ 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2063 AKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAK 2142
Cdd:pfam02463 444 GKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGR 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2143 HKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKvqmeeLLKLKNKIEE 2222
Cdd:pfam02463 524 IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLK-----LPLKSIAVLE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2223 ENQRLIKKDKDSTqKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEA 2302
Cdd:pfam02463 599 IDPILNLAQLDKA-TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2303 EMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERL--RLQVSQLSEAQARAEEEAKKFK 2380
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKinEELKLLKQKIDEEEEEEEKSRL 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2381 KQADKVATRLHETEiatQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHE 2460
Cdd:pfam02463 758 KKEEKEEEKSELSL---KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2461 KtvlqqtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKtLQATMDAALSKQKEAEEEML 2540
Cdd:pfam02463 835 L---------EELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKL-KDELESKEEKEKEEKKELEE 904
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1988774686 2541 RKQKEMQELERQRLEQERI--LAEENQKLREKLQQLEDAQKDQ 2581
Cdd:pfam02463 905 ESQKLNLLEEKENEIEERIkeEAEILLKYEEEPEELLLEEADE 947
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
141-245 |
4.80e-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: 4.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 141 TAKEKLLLWSQRMTDGYqGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 220
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1988774686 221 EDVDVPHPDEKSIITYVSSLYDAMP 245
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 ... |
1439-2335 |
3.80e-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: 106.21 E-value: 3.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1439 IRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRqaEEELKRKSEAEKEAAKQKQKALE 1518
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQ--ELKLKEQAKKALEYYQLKEKLEL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1519 DLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKsaaAELQSKHMSFAEKTSKLEESLKQEhgavlQLQQEAERLKKQ 1598
Cdd:pfam02463 222 EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSK---QEIEKEEEKLAQVLKENKEEEKEK-----KLQEEELKLLAK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1599 QEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELER 1678
Cdd:pfam02463 294 EEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1679 QRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEK 1758
Cdd:pfam02463 374 ELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1759 ETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKhqRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIAL 1838
Cdd:pfam02463 454 EKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS--RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1839 KEKEAENERLRRQ---AEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVE-EEIRILKL 1914
Cdd:pfam02463 532 GDLGVAVENYKVAistAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPIlNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1915 NFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKiaAAEEEAARQRKAALEELE 1994
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSEL--TKELLEIQELQEKAESEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1995 RLRKKAEEARKQKDEADKEAEKQIVVAQQaAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAE 2074
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLE-AEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2075 REAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQK 2154
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2155 FQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQrgQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDS 2234
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELE--SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2235 TQKLLAEEAENMRKLAEDAArlSVEAQEAARLRQIAEDDLNQQrALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQE 2314
Cdd:pfam02463 927 AEILLKYEEEPEELLLEEAD--EKEKEENNKEEEEERNKRLLL-AKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
890 900
....*....|....*....|.
gi 1988774686 2315 QAQKLLEDKQLMQQRLEEETE 2335
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 ... |
20-128 |
1.68e-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: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 20 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 96
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100 110
....*....|....*....|....*....|..
gi 1988774686 97 NIRNDDIADGNPKLTLGLIWTIILHFQVSSSI 128
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSISMPV 127
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
20-125 |
2.69e-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: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 20 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 96
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1988774686 97 NIRNDDIADGNPKLTLGLIWTIILHFQVS 125
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1104-1864 |
2.83e-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: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1104 VKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRE 1183
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1184 LEQLGRQLGYYRESYDWLIRWIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKD 1263
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1264 YELQLVAYKAQVEPLVSplKKTKLDSASDNIIQEYVTLRTRYSELMtltsqyikfITDTQRRLDDEEKAAEKLKAEErkk 1343
Cdd:TIGR02168 391 LELQIASLNNEIERLEA--RLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEELEELQEEL--- 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1344 mAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLK------MQEEVSKREIAAVDAEKQKTNIQLELQELKNL------- 1410
Cdd:TIGR02168 457 -ERLEEALEELREELEEAEQALDAAERELAQLQARldslerLQENLEGFSEGVKALLKNQSGLSGILGVLSELisvdegy 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1411 -------------------SEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLR 1471
Cdd:TIGR02168 536 eaaieaalggrlqavvvenLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1472 KLAQ------------DEAEKLRKQVSEE---------------------------TQKKRQAEEELKRKSEAEKEAAKQ 1512
Cdd:TIGR02168 616 KALSyllggvlvvddlDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEELEEKIAE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1513 KQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIkvaheaaqksaaaelqskhmsfaektSKLEESLKQEHGAVLQLQQEA 1592
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQI--------------------------SALRKDLARLEAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1593 ERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAhkktlaqeEAEKQKEEAEREAKKRAKAEESALKQK--- 1669
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI--------EQLKEELKALREALDELRAELTLLNEEaan 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1670 -----EMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRS 1744
Cdd:TIGR02168 822 lrerlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1745 EMDILIQLKTKAEKETMSNTEKSKQL-LEAEAAKMKdLAEEASRLRA----ISEEAKHQRQIAEEEAARQRAEAERiLKE 1819
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLeLRLEGLEVR-IDNLQERLSEeyslTLEEAEALENKIEDDEEEARRRLKR-LEN 979
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1988774686 1820 KLAAISEATRLkteaeiALKEKEAENER---LRRQAEDEAYQRKALED 1864
Cdd:TIGR02168 980 KIKELGPVNLA------AIEEYEELKERydfLTAQKEDLTEAKETLEE 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1206-1681 |
3.04e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 103.68 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1206 ADAKQRQEKIQAVPITDSKTLKE----QLAQEKKLLEEIE---QNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPL 1278
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEaaekKKEEAKKKADAAKkkaEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1279 VSPLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDD-EEKAAEKLKAEERKKMAE---MQAELDKQ 1354
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEaKKKAEEAKKADEAKKKAEeakKKADEAKK 1504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1355 KQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEE 1434
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1435 EIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSeetQKKRQAEEELKRKSEAEKEAAKQKQ 1514
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE---QLKKKEAEEKKKAEELKKAEEENKI 1661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1515 KAledlEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKsaaaelqskhmsfAEKTSKLEESLKQEHGAVlqlqQEAER 1594
Cdd:PTZ00121 1662 KA----AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-------------AEEAKKAEELKKKEAEEK----KKAEE 1720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1595 LKKQQEDAENSREEAEKELEKWRQKANEAlrlrlqAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEE 1674
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEA------KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
....*..
gi 1988774686 1675 ELERQRK 1681
Cdd:PTZ00121 1795 EVDKKIK 1801
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
775-841 |
3.09e-21 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 90.01 E-value: 3.09e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774686 775 QLKPRNptTSIKGKLPIQAVCDFKQQEITVHKGDECALLNNSQPFKWKVLNRSGHEAMVPSVCFIVP 841
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1984-2580 |
4.54e-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: 4.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1984 RQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSvLAQQIEDsitqkkLKEEYEKAKKLA 2063
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE-LELELEE------AQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2064 KEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKH 2143
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2144 KKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEE 2223
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2224 NQRLIKKDKDSTQKLLAEEAEnmrklaEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAE 2303
Cdd:COG1196 458 EEALLELLAELLEEAALLEAA------LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2304 MLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQA 2383
Cdd:COG1196 532 VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2384 DKVATRLHETEIATQEkmtVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTV 2463
Cdd:COG1196 612 DARYYVLGDTLLGRTL---VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2464 LQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLrkQ 2543
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL--E 766
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1988774686 2544 KEMQELERQR----------LEQERILAEENQKLREKLQQLEDAQKD 2580
Cdd:COG1196 767 RELERLEREIealgpvnllaIEEYEELEERYDFLSEQREDLEEARET 813
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
141-241 |
6.76e-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: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 141 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 220
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1988774686 221 EDVDV--PHPDEKSIITYVSSLY 241
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1804-2526 |
7.74e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.55 E-value: 7.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1804 EEAA------RQRAEAERilkeKLAAISEatRLkTEAEIALKEKEAENERLRRQAEDeayQRKALEDQASQHKQEIEEKI 1877
Cdd:COG1196 162 EEAAgiskykERKEEAER----KLEATEE--NL-ERLEDILGELERQLEPLERQAEK---AERYRELKEELKELEAELLL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1878 VQLKKSsEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKl 1957
Cdd:COG1196 232 LKLREL-EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1958 aleeekrrreaeekvkkiaaaeeeaarQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQS 2037
Cdd:COG1196 310 ---------------------------RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2038 VLAQQIEDSITQKKLKEEyekakklakeaeaakekaereaaLLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEF 2117
Cdd:COG1196 363 AEEALLEAEAELAEAEEE-----------------------LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2118 EAAKRAQAEaaalmQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRg 2197
Cdd:COG1196 420 EEELEELEE-----ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL- 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2198 qveeelfkvkvqmEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRkLAEDAARLSVEAQEAARLRQIAEDDLNQQ 2277
Cdd:COG1196 494 -------------LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI-GVEAAYEAALEAALAAALQNIVVEDDEVA 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2278 RALAEKMLKEKM--QAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEA 2355
Cdd:COG1196 560 AAAIEYLKAAKAgrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2356 ERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARL 2435
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2436 KKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLiEDEKKRLESQFE----------EEVKKAKALKD 2505
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL-ERELERLEREIEalgpvnllaiEEYEELEERYD 798
|
730 740
....*....|....*....|.
gi 1988774686 2506 EQERQKQQMEQEKKTLQATMD 2526
Cdd:COG1196 799 FLSEQREDLEEARETLEEAIE 819
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
142-241 |
9.91e-21 |
|
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: 9.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 142 AKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPE 221
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1988774686 222 D-VDVPHPDEKSIITYVSSLY 241
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
141-240 |
1.32e-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: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 141 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINmgkvYQQTNLENLE----QAFSVAEKdLGVTR 216
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVD----YESLDPLDIKennkKAFEAFAS-LGVPR 75
|
90 100
....*....|....*....|....*
gi 1988774686 217 LLDPED-VDVPHPDEKSIITYVSSL 240
Cdd:cd21255 76 LLEPADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
145-242 |
3.47e-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: 3.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 145 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD-PEDV 223
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1988774686 224 DVPHPDEKSIITYVSSLYD 242
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 ... |
1319-2335 |
1.13e-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: 97.94 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1319 ITDTQRRLDDEEKAAEKLKAE---------------------------ERKKMAEMQAELDKQKQLAEAHAKAIAKAEKE 1371
Cdd:pfam01576 105 IQDLEEQLDEEEAARQKLQLEkvtteakikkleedillledqnsklskERKLLEERISEFTSNLAEEEEKAKSLSKLKNK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1372 AQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKnlseQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKY 1451
Cdd:pfam01576 185 HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ----EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1452 TAESELKQLRDRAAEAEK---LRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKlrmqAE 1528
Cdd:pfam01576 261 NALKKIRELEAQISELQEdleSERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKK----AL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1529 EAERQVKQAEIEKEKQikvaheaAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREE 1608
Cdd:pfam01576 337 EEETRSHEAQLQEMRQ-------KHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1609 AEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQrkiaestAQ 1688
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE-------TR 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1689 QKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtmsnTEKSK 1768
Cdd:pfam01576 483 QKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE----LEALT 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1769 QLLEAEAAKMKDLAEEASRLRA----ISEEAKHQRQIAEEEAARQRaEAERILKEKLAAISEATRLKTEAEIALKEKEAE 1844
Cdd:pfam01576 559 QQLEEKAAAYDKLEKTKNRLQQelddLLVDLDHQRQLVSNLEKKQK-KFDQMLAEEKAISARYAEERDRAEAEAREKETR 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1845 NERLRRQAEDEAYQRKALEDQASQHKQEIEEkIVQLKKS---SEAEMERQKAIVDDTLKQRRVVEEEiriLKLNFEKASS 1921
Cdd:pfam01576 638 ALSLARALEEALEAKEELERTNKQLRAEMED-LVSSKDDvgkNVHELERSKRALEQQVEEMKTQLEE---LEDELQATED 713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1922 GKLDLELELNKLKNIADETQQSkiRAEEEAEKLRKLAleeekrrreaeEKVKKIAAAEEEAARQRKAALE-------ELE 1994
Cdd:pfam01576 714 AKLRLEVNMQALKAQFERDLQA--RDEQGEEKRRQLV-----------KQVRELEAELEDERKQRAQAVAakkklelDLK 780
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1995 RLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEdsiTQKKLKeeyekakklakeaeaakekae 2074
Cdd:pfam01576 781 ELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKE---SEKKLK--------------------- 836
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2075 reaallrqqAEEAErqktaaeeeaanQAKAQED---AERLRKEAEFEaakraqaeaaalmqKQQADTEMAKHKKLAEQTL 2151
Cdd:pfam01576 837 ---------NLEAE------------LLQLQEDlaaSERARRQAQQE--------------RDELADEIASGASGKSALQ 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2152 KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKV---KVQMEELLK-LKNKIEEENQRL 2227
Cdd:pfam01576 882 DEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSesaRQQLERQNKeLKAKLQEMEGTV 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2228 IKKDKDSTQKLLAeeaenmrKLAEDAARLSVEAQE---AARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEM 2304
Cdd:pfam01576 962 KSKFKSSIAALEA-------KIAQLEEQLEQESRErqaANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQ 1034
|
1050 1060 1070
....*....|....*....|....*....|.
gi 1988774686 2305 LQKQKDLAQEQAQKLLEDKQLMQQRLEEETE 2335
Cdd:pfam01576 1035 LKRQLEEAEEEASRANAARRKLQRELDDATE 1065
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
22-122 |
2.40e-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: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 22 QKKTFTKWVNKHLIKA--QRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLRHRQVKLVN 97
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1988774686 98 IRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1329-1950 |
4.09e-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: 96.29 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1329 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVS------KREIAAVDAEKQKT--NI 1400
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrvKEKIGELEAEIASLerSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1401 QLELQELKNLSEQQIKDKSQqVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEK 1480
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAE-IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1481 LRKQVSEETQKKRQAEEELKRKSE-------------AEKEAAKQKQKALED-LEKLRMQAEEAERQVKQ--AEIEKEKQ 1544
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEelqrlseeladlnAAIAGIEAKINELEEeKEDKALEIKKQEWKLEQlaADLSKYEQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1545 IKVA------------HEAAQKSAAAELQSKHMSFAEKTSK-----LEESLKQEHGAVLQLQQEAERLKKQQEDAENSR- 1606
Cdd:TIGR02169 470 ELYDlkeeydrvekelSKLQRELAEAEAQARASEERVRGGRaveevLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRl 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1607 --------EEAEKELEKWRQ-KANEA--LRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKA-------------E 1662
Cdd:TIGR02169 550 nnvvveddAVAKEAIELLKRrKAGRAtfLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAfkyvfgdtlvvedI 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1663 ESALKQK------EMAEEELERQRKI------AESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 1730
Cdd:TIGR02169 630 EAARRLMgkyrmvTLEGELFEKSGAMtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQ 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1731 QRKQLEDELAKVRSEMDILIQLKTKAE---KETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAisEEAKHQRQIAEEEAA 1807
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKerlEELEEDLSSLEQEIENVKSELKELEARIEELEE--DLHKLEEALNDLEAR 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1808 RQRAEAERI------LKEKLAAISEATRlktEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLK 1881
Cdd:TIGR02169 788 LSHSRIPEIqaelskLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774686 1882 KsSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEE 1950
Cdd:TIGR02169 865 E-LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
144-240 |
6.68e-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: 6.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 144 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN----LENLEQAFSVAEKDLGVTRLLD 219
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1988774686 220 PEDVDVPHPDEKSIITYVSSL 240
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 ... |
1331-2571 |
1.43e-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: 94.47 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1331 KAAEKLKAEERKKMAEMQ-AELD-KQKQLAE----------AHAKAIAKAEKEAQELKLKMQ--EEVSKREIAAVDAEKQ 1396
Cdd:pfam01576 10 KEEELQKVKERQQKAESElKELEkKHQQLCEeknalqeqlqAETELCAEAEEMRARLAARKQelEEILHELESRLEEEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1397 KTNiqlELQELKNLSEQQIKDKSQQVDEALHSRTK--------------IEEEIRLIRIQLETTEKQKYTAESELKQLRD 1462
Cdd:pfam01576 90 RSQ---QLQNEKKKMQQHIQDLEEQLDEEEAARQKlqlekvtteakikkLEEDILLLEDQNSKLSKERKLLEERISEFTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1463 RAAEAEKLRKLAQDEAEKLRKQVSE------ETQKKRQAEEELKRKSEAEKEAAKqkqkalEDLEKLRMQAEEAERQVKQ 1536
Cdd:pfam01576 167 NLAEEEEKAKSLSKLKNKHEAMISDleerlkKEEKGRQELEKAKRKLEGESTDLQ------EQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1537 AEIE-KEKQIKVAHEAAQKSAAaelQSKHMSFAEKTSKLEESLKQEHGAvlqlQQEAERLKKQ-QEDAENSREEAEKELE 1614
Cdd:pfam01576 241 KEEElQAALARLEEETAQKNNA---LKKIRELEAQISELQEDLESERAA----RNKAEKQRRDlGEELEALKTELEDTLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1615 KwrQKANEALRLRLQAEDEAHKKTLAqeeaekqkeeaerEAKKRAKAEESALKQK-----EMAEEELERQRKIAESTAQQ 1689
Cdd:pfam01576 314 T--TAAQQELRSKREQEVTELKKALE-------------EETRSHEAQLQEMRQKhtqalEELTEQLEQAKRNKANLEKA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1690 KLTAEQELIRLRADF-------DNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMS 1762
Cdd:pfam01576 379 KQALESENAELQAELrtlqqakQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1763 NTEKSKQLLEAEAAKMKDLAEE-------ASRLRAISEE-AKHQRQIAEEEAARQRAEaerilkeklaaiseatRLKTEA 1834
Cdd:pfam01576 459 LSKDVSSLESQLQDTQELLQEEtrqklnlSTRLRQLEDErNSLQEQLEEEEEAKRNVE----------------RQLSTL 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1835 EIALKEkeaenerLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEA--EMERQKAIVDDTLKQRRVVEEEIRIL 1912
Cdd:pfam01576 523 QAQLSD-------MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAydKLEKTKNRLQQELDDLLVDLDHQRQL 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1913 KLNFEKASSgKLDLELElnKLKNIADETQQSKIRAEEEAEKLRKLALEEEKrrreaeekvkkiaaaeeeaarqrkaALEE 1992
Cdd:pfam01576 596 VSNLEKKQK-KFDQMLA--EEKAISARYAEERDRAEAEAREKETRALSLAR-------------------------ALEE 647
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1993 LERLRKKAEEARKQKdEADKEaekQIVVAQQAAQKCSAAEQQVQSVLAQQIEDsitqkklkeeyekakklakeaeaakek 2072
Cdd:pfam01576 648 ALEAKEELERTNKQL-RAEME---DLVSSKDDVGKNVHELERSKRALEQQVEE--------------------------- 696
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2073 aereaalLRQQAEEAERQKTAAeeeaanqakaqEDAeRLRKEAEFEAAKRAQAeaaalmQKQQADTEMAKHKKlaEQTLK 2152
Cdd:pfam01576 697 -------MKTQLEELEDELQAT-----------EDA-KLRLEVNMQALKAQFE------RDLQARDEQGEEKR--RQLVK 749
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2153 QKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELlklknkieeenQRLIKKDK 2232
Cdd:pfam01576 750 QVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL-----------QRELEEAR 818
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2233 DSTQKLLAEEAENMRKLAedaarlSVEAQeaarLRQIAEDDLNQQRAlaekmlkeKMQAIQEASRLKAEAEMLQKQKDLA 2312
Cdd:pfam01576 819 ASRDEILAQSKESEKKLK------NLEAE----LLQLQEDLAASERA--------RRQAQQERDELADEIASGASGKSAL 880
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2313 QEQAQKLleDKQLMQqrLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHE 2392
Cdd:pfam01576 881 QDEKRRL--EARIAQ--LEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQE 956
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2393 TEIATQEKmtvverleferlntskeaddLRKAIADLEnekARLKKEAEELQNKSKEMADAQQKKIEHEKTVlqqtfmteK 2472
Cdd:pfam01576 957 MEGTVKSK--------------------FKSSIAALE---AKIAQLEEQLEQESRERQAANKLVRRTEKKL--------K 1005
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2473 EMLLkkekliedekkrlesQFEEEVKKAKALKDEQERQKQQMEQEKKTLQatmdaalskqkEAEEEMLRKQKEMQELERQ 2552
Cdd:pfam01576 1006 EVLL---------------QVEDERRHADQYKDQAEKGNSRMKQLKRQLE-----------EAEEEASRANAARRKLQRE 1059
|
1290 1300
....*....|....*....|..
gi 1988774686 2553 ---RLEQERILAEENQKLREKL 2571
Cdd:pfam01576 1060 lddATESNESMNREVSTLKSKL 1081
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1320-2016 |
2.13e-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: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1320 TDTQRRLDDEEKAAEK-LKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEvsKREIAAVDAEKQKT 1398
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKsLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQT--QQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1399 NIQLELQELknLSEQQIKDKSQQVDEALHSRTKIEEEIR-------LIRIQLETTEKQKYTAESELK-QLRDRAAEAEKL 1470
Cdd:TIGR00618 253 EEQLKKQQL--LKQLRARIEELRAQEAVLEETQERINRArkaaplaAHIKAVTQIEQQAQRIHTELQsKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1471 RKLAQDEAEKLRKQVSEETQkkRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHE 1550
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTL--HSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1551 AAQksAAAELQskhmsfaektsklEESLKQEHGAVLQLQQEAerlkkQQEDAENSREEAEKELEKWRQKANEALRLRLQA 1630
Cdd:TIGR00618 409 QAT--IDTRTS-------------AFRDLQGQLAHAKKQQEL-----QQRYAELCAAAITCTAQCEKLEKIHLQESAQSL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1631 EDEAHK-KTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRK-IAESTAQQKLTAEQELIRLRADFDNAE 1708
Cdd:TIGR00618 469 KEREQQlQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1709 QQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRL 1788
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1789 RAISEEAKHQRQIAEEEAARQRAE---AERILKEKLAAISEATRLKTEA-EIALKEKEAENERLRRQAEDEAYQRKALED 1864
Cdd:TIGR00618 629 DVRLHLQQCSQELALKLTALHALQltlTQERVREHALSIRVLPKELLASrQLALQKMQSEKEQLTYWKEMLAQCQTLLRE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1865 Q------ASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRvveEEIRILKLNFEKASSGKLDLELELNKLKNIAD 1938
Cdd:TIGR00618 709 LethieeYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR---TVLKARTEAHFNNNEEVTAALQTGAELSHLAA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1939 ETqQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQ--------RKAALEELERLRKKAEEARKQKDEA 2010
Cdd:TIGR00618 786 EI-QFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEqflsrleeKSATLGEITHQLLKYEECSKQLAQL 864
|
....*.
gi 1988774686 2011 DKEAEK 2016
Cdd:TIGR00618 865 TQEQAK 870
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1663-2576 |
2.95e-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: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1663 ESALKQKEMAEEELERQRKIAESTAQQkltaeqeLIRLRADFDNAEQQRSLL----EDELYRLKNEVAAAQQQRKQLEDE 1738
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQ-------LERLRREREKAERYQALLkekrEYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1739 LAKVRSEMDILIQLKTKAEKETmsntEKSKQLLEAEAAKMKDLAEEasrlraisEEAKHQRQIAEEEAarQRAEAERILK 1818
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRL----EEIEQLLEELNKKIKDLGEE--------EQLRVKEKIGELEA--EIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1819 EKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHK-------QEIEEKIVQLKKSSEAEMERQ 1891
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKeeledlrAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1892 KAIvDDTLKQRRVVEEEIRILKLNFEKASSGKLDLElelNKLKNIADETQQSKIRAEEEAEKLRKLaleeekrrreaEEK 1971
Cdd:TIGR02169 392 EKL-EKLKREINELKRELDRLQEELQRLSEELADLN---AAIAGIEAKINELEEEKEDKALEIKKQ-----------EWK 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1972 VKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEAdkEAEKQIVvaqQAAQKCSAAEQQVQSVLAQQIEDSITQ-K 2050
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA--EAQARAS---EERVRGGRAVEEVLKASIQGVHGTVAQlG 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2051 KLKEEYEKAKKLAKEAeaakekaereaallRQQAEEAErqktaaeeeaanqakAQEDAERLrkeaefeaakraqaeaaal 2130
Cdd:TIGR02169 532 SVGERYATAIEVAAGN--------------RLNNVVVE---------------DDAVAKEA------------------- 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2131 mqkqqadTEMAKHKKLAEQTLkqkfqveqeLTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKV-- 2208
Cdd:TIGR02169 564 -------IELLKRRKAGRATF---------LPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVve 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2209 QMEELLKLKNKIeeenqRLIKKDKDSTQK--LLAEEAENMRKLAEDAARLSVEAQE-AARLR--QIAEDDLNQQRALAEK 2283
Cdd:TIGR02169 628 DIEAARRLMGKY-----RMVTLEGELFEKsgAMTGGSRAPRGGILFSRSEPAELQRlRERLEglKRELSSLQSELRRIEN 702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2284 MLKEKMQAIQEASR----LKAEAEMLQKQkdlaQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLR 2359
Cdd:TIGR02169 703 RLDELSQELSDASRkigeIEKEIEQLEQE----EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2360 LQVSQLseAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEA 2439
Cdd:TIGR02169 779 EALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2440 EELQNKSKEMaDAQQKKIEhektvlqqtfmtekemllKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKK 2519
Cdd:TIGR02169 857 ENLNGKKEEL-EEELEELE------------------AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774686 2520 tLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERIlAEENQKLREKLQQLED 2576
Cdd:TIGR02169 918 -RLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV-QAELQRVEEEIRALEP 972
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1087-1834 |
3.58e-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: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1087 LKQYEDCLREVHTVPSDVKEVETYRAKLKKMRTEAEDE----QPVFDSLEEELKKAS-----AVSDKMVRVHSER---DV 1154
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRleeiEQLLEELNKKIKDLGeeeqlRVKEKIGELEAEIaslER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1155 ELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQLGRQLGYYRESYDWLIRWIADAKQRQEKIQAVPITDSKTLKEQLAQEK 1234
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1235 KLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSplKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQ 1314
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA--KINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1315 YIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQK------------------------QLAEAHAKAIAKAEK 1370
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRggraveevlkasiqgvhgtvaqlgSVGERYATAIEVAAG 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1371 EAQELKLKMQEEVSKREIAAVDAEKQK-------TNIQLELQELKNLSEQQIKD--------------------KSQQVD 1423
Cdd:TIGR02169 547 NRLNNVVVEDDAVAKEAIELLKRRKAGratflplNKMRDERRDLSILSEDGVIGfavdlvefdpkyepafkyvfGDTLVV 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1424 EALHSRTKIEEEIRLIRIQLETTEKQ----------------KYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSE 1487
Cdd:TIGR02169 627 EDIEAARRLMGKYRMVTLEGELFEKSgamtggsraprggilfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1488 ETQKKRQAEEELKRKSeaekeaaKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEkqikvAHEAAQKSAAAELQSKHmsf 1567
Cdd:TIGR02169 707 LSQELSDASRKIGEIE-------KEIEQLEQEEEKLKERLEELEEDLSSLEQEIE-----NVKSELKELEARIEELE--- 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1568 aEKTSKLEESL-----KQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELekwrqkaNEALRLRLQAEDEAHKKtlaqe 1642
Cdd:TIGR02169 772 -EDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL-------NRLTLEKEYLEKEIQEL----- 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1643 eAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAEstaqqkltAEQELIRLRADFDNAEQQRSLLEDELYRLK 1722
Cdd:TIGR02169 839 -QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD--------LESRLGDLKKERDELEAQLRELERKIEELE 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1723 NEVAAAQQQRKQLEDELAKVRSEMDILIQLKtKAEKETMSNT---EKSKQLLEAEAAKMKDLaeEASRLRAISEEAKHQR 1799
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIEDPK-GEDEEIPEEElslEDVQAELQRVEEEIRAL--EPVNMLAIQEYEEVLK 986
|
810 820 830
....*....|....*....|....*....|....*
gi 1988774686 1800 QIAEEEAARQRAEAERilKEKLAAISEATRLKTEA 1834
Cdd:TIGR02169 987 RLDELKEKRAKLEEER--KAILERIEEYEKKKREV 1019
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
141-240 |
5.14e-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: 5.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 141 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 220
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1988774686 221 ED-VDVPHPDEKSIITYVSSL 240
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1434-2192 |
6.39e-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: 6.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1434 EEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEaAKQK 1513
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ-TQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1514 QKALEDLEKLRMQAEEAERQVKQ--AEIEKEKQIKVAHEAAQKsaAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQ-Q 1590
Cdd:TIGR00618 242 HAYLTQKREAQEEQLKKQQLLKQlrARIEELRAQEAVLEETQE--RINRARKAAPLAAHIKAVTQIEQQAQRIHTELQsK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1591 EAERLKKQQEDAENSREEAekELEKWRQKANEALRLRLQAEDEAHKKTLaqeeaekqkeeaEREAKKRAKAEESALKQKE 1670
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQS--SIEEQRRLLQTLHSQEIHIRDAHEVATS------------IREISCQQHTLTQHIHTLQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1671 MAEEELERQRKIAeSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILI 1750
Cdd:TIGR00618 386 QQKTTLTQKLQSL-CKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1751 QLKTKAEKETMSNTEkskQLLEAEAAKMKdlaeeasrlraisEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEA-TR 1829
Cdd:TIGR00618 465 AQSLKEREQQLQTKE---QIHLQETRKKA-------------VVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPlTR 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1830 LKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEiEEKIVQLKKSSEAEMERQKAIVDDTLKQrrvVEEEI 1909
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITVRLQDL---TEKLS 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1910 RILKLNFEKASSGKLDLELELNKLKNIADETQQSKiraEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAA 1989
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQ---ELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLA 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1990 LEELERLRKKA---EEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIED-SITQKKLKEEYEKAKKLAKE 2065
Cdd:TIGR00618 682 LQKMQSEKEQLtywKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAlNQSLKELMHQARTVLKARTE 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2066 AEAAKEKAEREAALLRQQAEEAERQktaaeeEAANQAKAQEDAERLR-KEAEFEAAKRAQAEAAALMQKQQADTEMAKHK 2144
Cdd:TIGR00618 762 AHFNNNEEVTAALQTGAELSHLAAE------IQFFNRLREEDTHLLKtLEAEIGQEIPSDEDILNLQCETLVQEEEQFLS 835
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1988774686 2145 KLAEQTLKQkfqveQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDA 2192
Cdd:TIGR00618 836 RLEEKSATL-----GEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1224-1795 |
6.45e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 92.05 E-value: 6.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1224 KTLKEQLAQEKKLLEEIEQNKDKVDECQKYakayIDTIKDYELQLVAYKAQVEPLVSPLKKTKLDSASDNIIQEYVTLRT 1303
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLRE----INEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1304 R-YSELMTLTSQYIKFITDTQRRLDDEEKAAEKLK--AEERKKMAEMQAELDKQKQLAEahaKAIAKAEKEAQELKLKMq 1380
Cdd:PRK03918 255 RkLEEKIRELEERIEELKKEIEELEEKVKELKELKekAEEYIKLSEFYEEYLDELREIE---KRLSRLEEEINGIEERI- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1381 EEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQL 1460
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1461 RDRAAEAEKLRKLAQDEAEKLRK----------QVSEETQKKRQAE--EELKRKSEAEKEAAKQKQKALEDLEKLRMQAE 1528
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKakgkcpvcgrELTEEHRKELLEEytAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1529 EAERQVKQAEIEKekQIKVAHEAAQKSAAAELQSKhmsfAEKTSKLEESLKQEHGAVLQLQQEAERLK----------KQ 1598
Cdd:PRK03918 491 KESELIKLKELAE--QLKELEEKLKKYNLEELEKK----AEEYEKLKEKLIKLKGEIKSLKKELEKLEelkkklaeleKK 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1599 QEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEeaeREAKKRAKAEESAlkqkEMAEEELER 1678
Cdd:PRK03918 565 LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELE---REEKELKKLEEEL----DKAFEELAE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1679 QRKIAEStaqqkltAEQELIRLRADFDNAEQQRslLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDiliqlKTKAEK 1758
Cdd:PRK03918 638 TEKRLEE-------LRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLE-----KLKEEL 703
|
570 580 590
....*....|....*....|....*....|....*..
gi 1988774686 1759 ETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEA 1795
Cdd:PRK03918 704 EEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1301-2231 |
7.20e-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: 92.03 E-value: 7.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1301 LRTRYSELMTLTS-----QYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL 1375
Cdd:TIGR00606 171 LKQKFDEIFSATRyikalETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1376 KLKMQE-EVSKREIAAVDAE-KQKTNIQLELQELKNLSEQQIKDKSQQVDEAL------HSRTKIEEEIRLIRIQLETTE 1447
Cdd:TIGR00606 251 KNRLKEiEHNLSKIMKLDNEiKALKSRKKQMEKDNSELELKMEKVFQGTDEQLndlyhnHQRTVREKERELVDCQRELEK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1448 KQKytaeselkqlrdraaeaeKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEdleklrmQA 1527
Cdd:TIGR00606 331 LNK------------------ERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFE-------RG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1528 EEAERQVKQA-EIEKEKQIKVAHEAAQKsaAAELQSKHMSFAEKTSKLEESLKqehGAVLQLQQEAERLKKQQEDAENSR 1606
Cdd:TIGR00606 386 PFSERQIKNFhTLVIERQEDEAKTAAQL--CADLQSKERLKQEQADEIRDEKK---GLGRTIELKKEILEKKQEELKFVI 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1607 EEAE------KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEmaeeelERQR 1680
Cdd:TIGR00606 461 KELQqlegssDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH------TTTR 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1681 KIAESTAQQKLTAEQ-----------ELIRLRADFDNAEQqrslLEDELYRLKNEVaaaqqqrKQLEDELAKVRSEMDIL 1749
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEqirkiksrhsdELTSLLGYFPNKKQ----LEDWLHSKSKEI-------NQTRDRLAKLNKELASL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1750 IQLKTKAEKETMSNTEKSKQLLEA--EAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEA 1827
Cdd:TIGR00606 604 EQNKNHINNELESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVC 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1828 TR-LKTEAEIALKEKEAENerLRRQAEDEayqRKALEDQASQHKQEIEEKIVqLKKSSEAEMERQKAIVDDTLKQRRVVE 1906
Cdd:TIGR00606 684 QRvFQTEAELQEFISDLQS--KLRLAPDK---LKSTESELKKKEKRRDEMLG-LAPGRQSIIDLKEKEIPELRNKLQKVN 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1907 EEIRILKLNFEKASS--GKLDLELELNK--------LKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVK--- 1973
Cdd:TIGR00606 758 RDIQRLKNDIEEQETllGTIMPEEESAKvcltdvtiMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKqhe 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1974 --KIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKK 2051
Cdd:TIGR00606 838 ldTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETF 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2052 LKEEYEKAKKLAKEAEAAKEKAEREAALLRqqaeeaERQKTAAEEEAANQAKAQEDAERlrkeaefeaakraqaeaaalm 2131
Cdd:TIGR00606 918 LEKDQQEKEELISSKETSNKKAQDKVNDIK------EKVKNIHGYMKDIENKIQDGKDD--------------------- 970
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2132 QKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEvdDAVKqrgQVEEELFKVKVQME 2211
Cdd:TIGR00606 971 YLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRE--NELK---EVEEELKQHLKEMG 1045
|
970 980
....*....|....*....|....
gi 1988774686 2212 ELLKLKNKIE----EENQRLIKKD 2231
Cdd:TIGR00606 1046 QMQVLQMKQEhqklEENIDLIKRN 1069
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
141-239 |
7.43e-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: 81.51 E-value: 7.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 141 TAKEKLLLWSQRMTDGYqgiRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLGVTRLLD 219
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENpLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1988774686 220 PEDVDVPHPDEKSIITYVSS 239
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1528-2585 |
7.53e-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: 91.78 E-value: 7.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1528 EEAERQVKQAEIEKEKQIKVAHEAAQKsaaaELQSKHMSFAEKTSKLEESLKQEHgavlQLQQEAERLKKQQEDAENSRE 1607
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELK----ELEKKHQQLCEEKNALQEQLQAET----ELCAEAEEMRARLAARKQELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1608 EAEKELEKwrqkanealrlRLQAEDEAHKKTLAQeeaekqkeeaereaKKRAKAEESALKQkEMAEEELERQR-KIAEST 1686
Cdd:pfam01576 75 EILHELES-----------RLEEEEERSQQLQNE--------------KKKMQQHIQDLEE-QLDEEEAARQKlQLEKVT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1687 AQQKLTAEQELIRLRADFDNAEQ-QRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILiQLKTKAEKETMSNTE 1765
Cdd:pfam01576 129 TEAKIKKLEEDILLLEDQNSKLSkERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDL-EERLKKEEKGRQELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1766 KSKQLLEAEAAkmkDLAEEASRLRAISEEAKHQRQIAEEE----------AARQRAEAERILKEKLAAISEATR------ 1829
Cdd:pfam01576 208 KAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEElqaalarleeETAQKNNALKKIRELEAQISELQEdleser 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1830 -LKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEkivqLKKSSEAEMERQKAIVDD-TLKQRRVVE- 1906
Cdd:pfam01576 285 aARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTE----LKKALEEETRSHEAQLQEmRQKHTQALEe 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1907 -----EEIRILKLNFEKAssgKLDLELELNKLKNIADETQQSKIRAEEEAEKLrklaleeekrrreaEEKVKKIAAAEEE 1981
Cdd:pfam01576 361 lteqlEQAKRNKANLEKA---KQALESENAELQAELRTLQQAKQDSEHKRKKL--------------EGQLQELQARLSE 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1982 AARQRKAALEELERLRKKAEEARKQKDEADKEAEKqivvaqqAAQKCSAAEQQVQSvlAQQIEDSITQKKLKeeyekakk 2061
Cdd:pfam01576 424 SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK-------LSKDVSSLESQLQD--TQELLQEETRQKLN-------- 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2062 lakEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfeAAKRAQAEAAALMQKQQADTEMA 2141
Cdd:pfam01576 487 ---LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAG--TLEALEEGKKRLQRELEALTQQL 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2142 KHKKLAEQTL-KQKFQVEQELTKVKLKLDET--------DKQK---SVLDEE---LQRLKDEVDDAVKQRGQVEEELFKV 2206
Cdd:pfam01576 562 EEKAAAYDKLeKTKNRLQQELDDLLVDLDHQrqlvsnleKKQKkfdQMLAEEkaiSARYAEERDRAEAEAREKETRALSL 641
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2207 KVQMEELLKLKNKIEEENQRL------IKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDdlnqqral 2280
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQLraemedLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATED-------- 713
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2281 AEKMLKEKMQAiqeasrLKAEAEM-LQKQKDLAQEQAQKLLedKQLMQQRLEEETEEYHKSLEVERKRQLEImaEAERLR 2359
Cdd:pfam01576 714 AKLRLEVNMQA------LKAQFERdLQARDEQGEEKRRQLV--KQVRELEAELEDERKQRAQAVAAKKKLEL--DLKELE 783
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2360 LQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKmtvverleferLNTSKEADdlrKAIADLENEKARLKkea 2439
Cdd:pfam01576 784 AQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEI-----------LAQSKESE---KKLKNLEAELLQLQ--- 846
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2440 EELQNKSKEMADAQQKKIEHEKTVLQQTfmTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKK 2519
Cdd:pfam01576 847 EDLAASERARRQAQQERDELADEIASGA--SGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTT 924
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 2520 TLQATMDAAlSKQKEAEEEMLRKQKE----MQELERQ-RLEQERILAeenqKLREKLQQLEDaQKDQHTRE 2585
Cdd:pfam01576 925 ELAAERSTS-QKSESARQQLERQNKElkakLQEMEGTvKSKFKSSIA----ALEAKIAQLEE-QLEQESRE 989
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
143-253 |
1.21e-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: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 143 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 222
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|..
gi 1988774686 223 -VDVPHPDEKSIITYVSSLYdampRTDVHDGM 253
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 ... |
137-242 |
1.35e-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: 81.15 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 137 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTR 216
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1988774686 217 LLDPEDV-DVPHPDEKSIITYVSSLYD 242
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2241-2578 |
1.77e-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: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2241 EEAEnmRKLAEDAARLsveaqeaARLRQIAE------DDLNQQRALAEKMlkekmQAIQEASRLKaEAEMLQKQKDLAQE 2314
Cdd:COG1196 175 EEAE--RKLEATEENL-------ERLEDILGelerqlEPLERQAEKAERY-----RELKEELKEL-EAELLLLKLRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2315 QAQKLLEDKQLMQQRLEEETEEY---HKSLEVERKRQLEIMAEAERLRLQVSQLSEAQAraeeeakkfkkQADKVATRLH 2391
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELaelEAELEELRLELEELELELEEAQAEEYELLAELA-----------RLEQDIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2392 ETEIATQEKMtvvERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEmADAQQKKIEHEKTVLQQTFMTE 2471
Cdd:COG1196 309 ERRRELEERL---EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE-AEEALLEAEAELAEAEEELEEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2472 KEMLLKKEKLIEDEKKRLESQfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELER 2551
Cdd:COG1196 385 AEELLEALRAAAELAAQLEEL-EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340
....*....|....*....|....*..
gi 1988774686 2552 QRLEQERILAEENQKLREKLQQLEDAQ 2578
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAA 490
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
23-120 |
2.60e-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: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 23 KKTFTKWVNKHL-IKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLRHRQV-KLVNI 98
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1988774686 99 RNDDI-ADGNPKLTLGLIWTIIL 120
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
143-242 |
4.62e-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: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 143 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 222
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1988774686 223 VDV--PHPDEKSIITYVSSLYD 242
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2244-2555 |
5.82e-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: 88.64 E-value: 5.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2244 ENMRKLAEDAARLSVEAQEAARLRQIAED---DLNQQRALAEKMlKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLL 2320
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEkarEVERRRKLEEAE-KARQAEMDRQAAIYAEQERMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2321 EDKQLMQQRLEEETEEYHKSLEVERkRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEK 2400
Cdd:pfam17380 358 RKRELERIRQEEIAMEISRMRELER-LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2401 MtvvERLEFERlntSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKtvlQQTFMTEKEMLLKKEK 2480
Cdd:pfam17380 437 V---RRLEEER---AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE---QRRKILEKELEERKQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2481 LIEDEKKR--LESQFEEEVK----KAKALKDEQERQKQQMEQEKKTLQATMDAALSKQK-----EAEEEMLRKQKEmQEL 2549
Cdd:pfam17380 508 MIEEERKRklLEKEMEERQKaiyeEERRREAEEERRKQQEMEERRRIQEQMRKATEERSrleamEREREMMRQIVE-SEK 586
|
....*.
gi 1988774686 2550 ERQRLE 2555
Cdd:pfam17380 587 ARAEYE 592
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
143-249 |
7.73e-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: 7.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 143 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 222
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*....
gi 1988774686 223 VDV--PHPDEKSIITYVSSLYDAMPRTDV 249
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRRHEM 111
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1388-2204 |
1.01e-16 |
|
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: 88.20 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1388 IAAVDAEKQKTNIQLELQElKNLSEQQ--IKDKSQQVDEALHSRTKIEE--EIRLIRIQLETTE--KQKYTAESELKQLR 1461
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVE-ENIERLDliIDEKRQQLERLRREREKAERyqALLKEKREYEGYEllKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1462 DRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALE-DLEKLRMQAEEAERQVKQAEiE 1540
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERSIAEKERELEDAE-E 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1541 KEKQIKVAHEAaQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKA 1620
Cdd:TIGR02169 323 RLAKLEAEIDK-LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1621 NEALRLRLQAEDEAHKKTlaqeeaekQKEEAEREAKKRAKAEESALK-QKEMAEEELERQRKIAESTAQQKLTAEQELIR 1699
Cdd:TIGR02169 402 NELKRELDRLQEELQRLS--------EELADLNAAIAGIEAKINELEeEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1700 LRADFDNAEQQRSLLEDELYRLKNEVAAAQQ-------QRKQLEDELAKVRSEMDILIQLKTKAEK-------------- 1758
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEErvrggraVEEVLKASIQGVHGTVAQLGSVGERYATaievaagnrlnnvv 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1759 -ETMSNTEKSKQLLEAEAA---------KMKDLAEEASRLRA----------ISEEAKHQRQIA----------EEEAAR 1808
Cdd:TIGR02169 554 vEDDAVAKEAIELLKRRKAgratflplnKMRDERRDLSILSEdgvigfavdlVEFDPKYEPAFKyvfgdtlvveDIEAAR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1809 QRAEAERI------LKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKK 1882
Cdd:TIGR02169 634 RLMGKYRMvtlegeLFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1883 SSEAEMERQKAIvDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKL-RKLALEE 1961
Cdd:TIGR02169 714 ASRKIGEIEKEI-EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1962 EKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQ 2041
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2042 qiedsiTQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQED-AERLRKEAEFEAA 2120
Cdd:TIGR02169 873 ------LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEElSEIEDPKGEDEEI 946
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2121 KRAQAEAAALMQKQQADTEmakhkklAEQTLKQ-KFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQV 2199
Cdd:TIGR02169 947 PEEELSLEDVQAELQRVEE-------EIRALEPvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
....*
gi 1988774686 2200 EEELF 2204
Cdd:TIGR02169 1020 FMEAF 1024
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1329-1795 |
1.51e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.40 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1329 EEKAAEKLKAEERKKMA--------EMQAELDKQKQLAEAHAKAIAKAEKEAQELKlkmqEEVSKREIAAVDAEKQKTNI 1400
Cdd:PRK02224 223 ERYEEQREQARETRDEAdevleeheERREELETLEAEIEDLRETIAETEREREELA----EEVRDLRERLEELEEERDDL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1401 QLELQelknLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEK 1480
Cdd:PRK02224 299 LAEAG----LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1481 LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAEL 1560
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKC 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1561 --------QSKHMSFAEKTSKLEESLKQEhgaVLQLQQEAERLKKQQEDAENSReEAEKELEKWRQKANEALRLRLQAED 1632
Cdd:PRK02224 455 pecgqpveGSPHVETIEEDRERVEELEAE---LEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRE 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1633 EAHKKTLAQEEAEKQKEEAEREAK-KRAKAEESALKQKEMAE-------------EELERQRKIAESTAQQKlTAEQELI 1698
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEeKREAAAEAEEEAEEAREevaelnsklaelkERIESLERIRTLLAAIA-DAEDEIE 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1699 RL---RADFDNAEQQR-----------SLLEDELYrlKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtMSNT 1764
Cdd:PRK02224 610 RLrekREALAELNDERrerlaekrerkRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAE-IGAV 686
|
490 500 510
....*....|....*....|....*....|.
gi 1988774686 1765 EKSKQLLEAEAAKMKDLAEEASRLRAISEEA 1795
Cdd:PRK02224 687 ENELEELEELRERREALENRVEALEALYDEA 717
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
143-244 |
1.79e-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: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 143 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 222
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1988774686 223 -VDVPHPDEKSIITYVSSLYDAM 244
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1417-2051 |
5.12e-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: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1417 DKSQQVDEALHSRTKIEEEIRliriQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRqae 1496
Cdd:pfam12128 231 QAIAGIMKIRPEFTKLQQEFN----TLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKR--- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1497 EELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAeLQSKHMSFAEKTSKLEE 1576
Cdd:pfam12128 304 DELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LTGKHQDVTAKYNRRRS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1577 SLKQEHGAVLQLQQEaeRLKKQQEDAENSREEAEKELEK----WRQKANEALRlRLQAEDEAHKKTLAqeeaekqkeeae 1652
Cdd:pfam12128 383 KIKEQNNRDIAGIKD--KLAKIREARDRQLAVAEDDLQAleseLREQLEAGKL-EFNEEEYRLKSRLG------------ 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1653 rEAKKR---AKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQ 1729
Cdd:pfam12128 448 -ELKLRlnqATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1730 QQ------------RKQL---EDELAKVRSEmdiliQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEE 1794
Cdd:pfam12128 527 LQlfpqagtllhflRKEApdwEQSIGKVISP-----ELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEE 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1795 AKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIE 1874
Cdd:pfam12128 602 LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1875 EKIVQLKKSSEAEMERQKAIVDDTLKQRRvveeEIRILKLNFEKASSGKLDLELELNKlkniadetqqSKIRAEEEAEKL 1954
Cdd:pfam12128 682 ERLNSLEAQLKQLDKKHQAWLEEQKEQKR----EARTEKQAYWQVVEGALDAQLALLK----------AAIAARRSGAKA 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1955 RKLALEEEKRRREAEEKVKKIaaAEEEAARQRKAALEELERLRKKAEEARKQKD--EADKEAEKQIVVAQQAAQKCSAAE 2032
Cdd:pfam12128 748 ELKALETWYKRDLASLGVDPD--VIAKLKREIRTLERKIERIAVRRQEVLRYFDwyQETWLQRRPRLATQLSNIERAISE 825
|
650
....*....|....*....
gi 1988774686 2033 QQVQsvLAQQIEDSITQKK 2051
Cdd:pfam12128 826 LQQQ--LARLIADTKLRRA 842
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1105-1919 |
8.11e-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: 85.41 E-value: 8.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1105 KEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQREL 1184
Cdd:pfam02463 265 EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1185 EQLGRQLGYYRESydwlirwIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDY 1264
Cdd:pfam02463 345 KELEIKREAEEEE-------EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1265 ELQLVAYKAQVEPLVSPLKKTKLdsasdnIIQEYVTLRTRYSELMTLTSqyikfitdtQRRLDDEEKAAEKLKAEERKKM 1344
Cdd:pfam02463 418 EDLLKEEKKEELEILEEEEESIE------LKQGKLTEEKEELEKQELKL---------LKDELELKKSEDLLKETQLVKL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1345 AEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVskREIAAVDAEKQKTNIQLELQELKNLSeqqikdkSQQVDE 1424
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG--GRIISAHGRLGDLGVAVENYKVAIST-------AVIVEV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1425 ALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAeAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSE 1504
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSI-AVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1505 AEKEAAKQKQKALEDLEKLRMQAE-EAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHG 1583
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKGVSLEEgLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1584 AVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKtlaqeeaekqkeeAEREAKKRAKAEE 1663
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEK-------------SELSLKEKELAEE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1664 SALKQKEMAEEELERQRKIAESTaqqkLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEvaaAQQQRKQLEDELAKVR 1743
Cdd:pfam02463 780 REKTEKLKVEEEKEEKLKAQEEE----LRALEEELKEEAELLEEEQLLIEQEEKIKEEELE---ELALELKEEQKLEKLA 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1744 SEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAA 1823
Cdd:pfam02463 853 EEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLK 932
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1824 ISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEdqASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRR 1903
Cdd:pfam02463 933 YEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL--GKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRA 1010
|
810
....*....|....*.
gi 1988774686 1904 VVEEEIRILKLNFEKA 1919
Cdd:pfam02463 1011 IIEETCQRLKEFLELF 1026
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
146-241 |
1.09e-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: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 146 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEkDLGVTRLLDPED-VD 224
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1988774686 225 VPHPDEKSIITYVSSLY 241
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2238-2580 |
1.24e-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: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2238 LLAEEAENMRKLAEDAARlsveAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQ-EASRLKAEAEMLQKQkdlaQEQA 2316
Cdd:COG1196 194 ILGELERQLEPLERQAEK----AERYRELKEELKELEAELLLLKLRELEAELEELEaELEELEAELEELEAE----LAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2317 QKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIA 2396
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2397 TQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQqtfmtEKEMLL 2476
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-----RLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2477 KKEKLIEDEkkrlESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQ 2556
Cdd:COG1196 421 EELEELEEA----LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
330 340
....*....|....*....|....
gi 1988774686 2557 ERILAEENQKLREKLQQLEDAQKD 2580
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLR 520
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1429-2340 |
1.28e-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: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1429 RTKIEEEIRLIriqlETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKqvseETQKKRQAEEELKRKSEAE-K 1507
Cdd:TIGR02169 155 RRKIIDEIAGV----AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRR----EREKAERYQALLKEKREYEgY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1508 EAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKtskleeslkqehgavLQ 1587
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---------------LR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1588 LQQEAERLKKQQEDAENSREEAEKELEKW--RQKANEALRLRLQAEDEAHKKTLAqeeaekqkeeaeREAKKRAKAEESA 1665
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAeeRLAKLEAEIDKLLAEIEELEREIE------------EERKRRDKLTEEY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1666 LKQKEmaEEELERQRKIAESTAQQklTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSE 1745
Cdd:TIGR02169 360 AELKE--ELEDLRAELEEVDKEFA--ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1746 MDILIQLKTKAEKETMSNTEKSKQL---LEAEAAKMKDLAEEASRLRaiSEEAKHQRQIAEEEAARQRAE--------AE 1814
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQEWKLEQLaadLSKYEQELYDLKEEYDRVE--KELSKLQRELAEAEAQARASEervrggraVE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1815 RILKEKL----AAISEATRLKTEAEIALkEKEAENERLRRQAEDEAYQRKALEdQASQHK---------QEIEEKIVQLK 1881
Cdd:TIGR02169 514 EVLKASIqgvhGTVAQLGSVGERYATAI-EVAAGNRLNNVVVEDDAVAKEAIE-LLKRRKagratflplNKMRDERRDLS 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1882 KSSEA----------EMERQ-----KAIVDDTLkqrrVVE--EEIRILKLNFEKASsgkldLELEL-----------NKL 1933
Cdd:TIGR02169 592 ILSEDgvigfavdlvEFDPKyepafKYVFGDTL----VVEdiEAARRLMGKYRMVT-----LEGELfeksgamtggsRAP 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1934 KNIADETQQSKIRAEEEAEKLRKLaleeekrrreaeekvkkiaaaeeeaARQRKAALEELERLRKKAEEARkqkdEADKE 2013
Cdd:TIGR02169 663 RGGILFSRSEPAELQRLRERLEGL-------------------------KRELSSLQSELRRIENRLDELS----QELSD 713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2014 AEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDsitQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTA 2093
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEED---LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH 790
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2094 AEEEAANQAKAQEDAERLRKEAEFEaaKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDEtdk 2173
Cdd:TIGR02169 791 SRIPEIQAELSKLEEEVSRIEARLR--EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE--- 865
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2174 qksvLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKlLAEEAENMRKLAEDA 2253
Cdd:TIGR02169 866 ----LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEIEDPK 940
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2254 ARLSVEAQEAARLRQIAEDDLNQQRALaEKMLKEKMQAIQEAsrlkaeAEMLQKQKDLaQEQAQKLLEDKQLMQQRLEEE 2333
Cdd:TIGR02169 941 GEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEY------EEVLKRLDEL-KEKRAKLEEERKAILERIEEY 1012
|
....*..
gi 1988774686 2334 TEEYHKS 2340
Cdd:TIGR02169 1013 EKKKREV 1019
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1325-1956 |
1.79e-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: 84.00 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1325 RLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSK------------------R 1386
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdlikennatrhlcnllK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1387 EIAAVDAEK----------------------------------QKTNIQLEL-----------QELKNLSEQQIKDKSQQ 1421
Cdd:pfam05483 162 ETCARSAEKtkkyeyereetrqvymdlnnniekmilafeelrvQAENARLEMhfklkedhekiQHLEEEYKKEINDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1422 VDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKR 1501
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1502 KSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSaAAELQSKHMSFAEKTSKLEESLKQE 1581
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN-EDQLKIITMELQKKSSELEEMTKFK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1582 HGAVLQLqQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKK-RAK 1660
Cdd:pfam05483 401 NNKEVEL-EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDlKTE 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1661 AEESALKQKEM---AEEELERQRKIAESTAQQKLtaeqELIRLRADFDNAEQQRSlledelyRLKNEVAAAQQQRKQLED 1737
Cdd:pfam05483 480 LEKEKLKNIELtahCDKLLLENKELTQEASDMTL----ELKKHQEDIINCKKQEE-------RMLKQIENLEEKEMNLRD 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1738 ELAKVRSEM-DILIQLKTKAEKETMSNTEKSKQLLEAEaAKMKDLAEEASRLRA-ISEEAKHQRQIAEE-EAARQRAEAE 1814
Cdd:pfam05483 549 ELESVREEFiQKGDEVKCKLDKSEENARSIEYEVLKKE-KQMKILENKCNNLKKqIENKNKNIEELHQEnKALKKKGSAE 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1815 -------RILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQA-EDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEA 1886
Cdd:pfam05483 628 nkqlnayEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKlLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVA 707
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1887 EMERQKAIVDDTLKQRrvvEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRK 1956
Cdd:pfam05483 708 LMEKHKHQYDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKM 774
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
145-242 |
2.02e-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: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 145 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD-PEDV 223
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1988774686 224 DVPHPDEKSIITYVSSLYD 242
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1314-1934 |
3.28e-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: 83.24 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1314 QYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKaIAKAEKEAQElklkmqeevskreiaavDA 1393
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMAD-IRRRESQSQE-----------------DL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1394 EKQKTNIQLELQELKNLSEQQIKDKSQQVDE---ALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRdraaeaekL 1470
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLKEDMLEDSNTQIEQlrkMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMH--------F 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1471 RKLAQDEAEKLRKQVSEETQKKRQ---AEEELkrksEAEKEAAKQKQKALedlekLRMQAEEAERQVKQAEIEKEKQIKV 1547
Cdd:pfam15921 216 RSLGSAISKILRELDTEISYLKGRifpVEDQL----EALKSESQNKIELL-----LQQHQDRIEQLISEHEVEITGLTEK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1548 AHEAaqKSAAAELQSKhMSFAEKTSKLEESLKQEH-----GAVLQLQQEAERLKKQQEDaenSREEAEKELEKWRQKANE 1622
Cdd:pfam15921 287 ASSA--RSQANSIQSQ-LEIIQEQARNQNSMYMRQlsdleSTVSQLRSELREAKRMYED---KIEELEKQLVLANSELTE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1623 ALRLRLQAE------DEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESA-----------LKQKEMAEEELERQRKIAES 1685
Cdd:pfam15921 361 ARTERDQFSqesgnlDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGnsitidhlrreLDDRNMEVQRLEALLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1686 TAQQKLtaEQELIRLRADFDNAEQQRSL---LEDELYRLKNEVAAAQQQRKQLEDELAKVrSEMDILIQLKTKAEKETMS 1762
Cdd:pfam15921 441 ECQGQM--ERQMAAIQGKNESLEKVSSLtaqLESTKEMLRKVVEELTAKKMTLESSERTV-SDLTASLQEKERAIEATNA 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1763 NTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQR-QIAEEEAARQ--RAEAERILkeKLAAISEATRLKTEAEIALK 1839
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVIEilRQQIENMT--QLVGQHGRTAGAMQVEKAQL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1840 EKEAENERLRRQaedeayQRKALEDQASQHKQEIEEKIVQLK----KSSEAEMERQKAIVDdtLKQRR------------ 1903
Cdd:pfam15921 596 EKEINDRRLELQ------EFKILKDKKDAKIRELEARVSDLElekvKLVNAGSERLRAVKD--IKQERdqllnevktsrn 667
|
650 660 670
....*....|....*....|....*....|....
gi 1988774686 1904 ---VVEEEIRILKLNFEKASSgklDLELELNKLK 1934
Cdd:pfam15921 668 elnSLSEDYEVLKRNFRNKSE---EMETTTNKLK 698
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
22-122 |
3.35e-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: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 22 QKKTFTKWVNKHLIK--AQRHVTDLYEDLRDGHNLISLLEVLSGETL------PREKGRMRfhklQNVQIALDFLRHRQV 93
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1988774686 94 KLVNIRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
19-118 |
3.52e-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: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 19 DRVQKKTFTKWVNKHLIKAQ-RHVTDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLRHR-QV 93
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
|
90 100
....*....|....*....|....*
gi 1988774686 94 KLVNIRNDDIADGNPKLTLGLIWTI 118
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1653-1910 |
3.76e-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: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1653 REAKKRAKAEESALKQ-KEMAEEELERQRKIAES-TAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 1730
Cdd:pfam17380 288 QQQEKFEKMEQERLRQeKEEKAREVERRRKLEEAeKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1731 QRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKH-QRQIAEEEAARq 1809
Cdd:pfam17380 368 EEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQrEVRRLEEERAR- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1810 raEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQE-IEEKivQLKKSSEAEM 1888
Cdd:pfam17380 447 --EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAmIEEE--RKRKLLEKEM 522
|
250 260
....*....|....*....|...
gi 1988774686 1889 E-RQKAIVDDtlKQRRVVEEEIR 1910
Cdd:pfam17380 523 EeRQKAIYEE--ERRREAEEERR 543
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1404-1813 |
4.43e-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: 82.48 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1404 LQELKNLSEQQIKDKSQqvdealhsrtKIEEEirliRIQLETTEKQKytaesELKQlRDRAAEAEKLRKLAQDE-----A 1478
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE----------KMEQE----RLRQEKEEKAR-----EVER-RRKLEEAEKARQAEMDRqaaiyA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1479 EKLRKQVSEETQKKRQAEEELKRkseaEKEAAKQKQKALE-----DLEKLRMQAEEAERQVKQaEIEKEKQIKVAHEAAQ 1553
Cdd:pfam17380 338 EQERMAMERERELERIRQEERKR----ELERIRQEEIAMEisrmrELERLQMERQQKNERVRQ-ELEAARKVKILEEERQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1554 KSAaaelqSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENsreeaEKELEKWRQKANEALRLRLQAEde 1633
Cdd:pfam17380 413 RKI-----QQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQER-----QQQVERLRQQEEERKRKKLELE-- 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1634 ahkktlaqeeaekqkeeaeREAKKRAKAEEsaLKQKEMAEEELERQRKIAEStaqqkltaeqelirlradfdnaEQQRSL 1713
Cdd:pfam17380 481 -------------------KEKRDRKRAEE--QRRKILEKELEERKQAMIEE----------------------ERKRKL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1714 LEDELYRLKNEVAAAQQQRKQLEdelakvrsemdiliqlktkaEKETMSNTEKSKQLLEaeaaKMKDLAEEASRLRAISE 1793
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRREAEE--------------------ERRKQQEMEERRRIQE----QMRKATEERSRLEAMER 573
|
410 420
....*....|....*....|
gi 1988774686 1794 EAKHQRQIAEEEAARQRAEA 1813
Cdd:pfam17380 574 EREMMRQIVESEKARAEYEA 593
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2282-2581 |
6.78e-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: 81.71 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2282 EKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEdkQLMQQRLEEETEEyhKSLEVERKRQLEimaEAERLR-- 2359
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFE--KMEQERLRQEKEE--KAREVERRRKLE---EAEKARqa 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2360 -------LQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQ-EKMTVVERLEFERLNTS----KEADDLRKAIAD 2427
Cdd:pfam17380 328 emdrqaaIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEiSRMRELERLQMERQQKNervrQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2428 LENEKARLKKEAEELQNKSKEMADAQQKKIEhektVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQ 2507
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVR----RLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK 483
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774686 2508 ERQKQQMEQEKKTLQATMDAalSKQKEAEEEMLRKQKEMQELERQRL---EQERILAEENqklREKLQQLEDAQKDQ 2581
Cdd:pfam17380 484 RDRKRAEEQRRKILEKELEE--RKQAMIEEERKRKLLEKEMEERQKAiyeEERRREAEEE---RRKQQEMEERRRIQ 555
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1859-2582 |
6.97e-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: 82.33 E-value: 6.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1859 RKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKassgkLDLELELNKLKNIAD 1938
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQ-----LKEKLELEEEYLLYL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1939 ETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQI 2018
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2019 VVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAkekaereaaLLRQQAEEAERQKTAAEEEA 2098
Cdd:pfam02463 310 VDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEE---------LEKLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2099 ANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEqtlkqkfqveqeltkvKLKLDETDKQKSVL 2178
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELE----------------ILEEEEESIELKQG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2179 DEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRlIKKDKDSTQKLLAEEAENMRklaedaaRLSV 2258
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR-QKLEERSQKESKARSGLKVL-------LALI 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2259 EAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYH 2338
Cdd:pfam02463 517 KDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2339 KSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIAtQEKMTVVERLEFERLNTSKEA 2418
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSL-EEGLAEKSEVKASLSELTKEL 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2419 DDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVK 2498
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2499 KAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQErILAEENQKLREKLQQLEDAQ 2578
Cdd:pfam02463 756 RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA-ELLEEEQLLIEQEEKIKEEE 834
|
....
gi 1988774686 2579 KDQH 2582
Cdd:pfam02463 835 LEEL 838
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
955-1741 |
8.74e-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: 82.04 E-value: 8.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 955 EKGQQNETLC--KNYISELKDLRLRIEDCEAgtvarirkpveKEPLKEYIQKTTEQKKVQGELDGLKKDLDKVSVKTQEV 1032
Cdd:TIGR02169 195 EKRQQLERLRreREKAERYQALLKEKREYEG-----------YELLKEKEALERQKEAIERQLASLEEELEKLTEEISEL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1033 lasPQPSASAPVLRSELDLTVQKMDHAHMLSsvYLEKLKTVEMVIRNTQGAEGVLKQYEDCLREvhTVPSDVKEVETYRA 1112
Cdd:TIGR02169 264 ---EKRLEEIEQLLEELNKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1113 KLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQLGRQLG 1192
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1193 YYRESYDWLIRWIADAKQRQEKIQavpiTDSKTLKEQLAQEKKLLEEIEQNKDKVDEcQKYAK-----AYIDTIKDYELQ 1267
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELE----EEKEDKALEIKKQEWKLEQLAADLSKYEQ-ELYDLkeeydRVEKELSKLQRE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1268 LVAYKAQVEPLV--SPLKKTKLDSASDNIIQEYVTLRtrysELMTLTSQYIKFI-TDTQRRL-----DDEEKAAEKLK-A 1338
Cdd:TIGR02169 492 LAEAEAQARASEerVRGGRAVEEVLKASIQGVHGTVA----QLGSVGERYATAIeVAAGNRLnnvvvEDDAVAKEAIElL 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1339 EERK----------KMAEMQAELDKqkqLAEAHAKAIAK-----AEKEAQELKLKMQEEVSKREIAAvdAEKQKTNIQL- 1402
Cdd:TIGR02169 568 KRRKagratflplnKMRDERRDLSI---LSEDGVIGFAVdlvefDPKYEPAFKYVFGDTLVVEDIEA--ARRLMGKYRMv 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1403 ----ELQELK-------NLSEQQIKDKSQQVDEALHSRTKIEEeirlIRIQLETTEKQKYTAESELKQLRDRAAEAEKLR 1471
Cdd:TIGR02169 643 tlegELFEKSgamtggsRAPRGGILFSRSEPAELQRLRERLEG----LKRELSSLQSELRRIENRLDELSQELSDASRKI 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1472 KLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEaEKEAAKQKQKAL--------EDLEKLRMQAEEAER-------QVKQ 1536
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ-EIENVKSELKELearieeleEDLHKLEEALNDLEArlshsriPEIQ 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1537 AEIEKEKQIKVAHEAAQKSAAAELQSKHM--SFAEKTSKLEESLKQE---------------HGAVLQLQQEAERLKKQQ 1599
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLekEYLEKEIQELQEQRIDlkeqiksiekeienlNGKKEELEEELEELEAAL 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1600 EDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKtlaqeeaekQKEEAEREAKKRAKAEESALKQKEMAEEELERQ 1679
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK---------RKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 1680 RKIAESTAQQKLTAEQELIRLRADFDN-AEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAK 1741
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNMlAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1381-1864 |
9.02e-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: 81.21 E-value: 9.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1381 EEVSKREIAAVDAEKQKTNIQlELQELKNLSEQQIKDKSQQVDEALHSRTkIEEEIRLIRIqletteKQKYTAESELKQL 1460
Cdd:NF033838 38 EEVRGGNNPTVTSSGNESQKE-HAKEVESHLEKILSEIQKSLDKRKHTQN-VALNKKLSDI------KTEYLYELNVLKE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1461 RDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEeelKRKSEAEKEAAKQKQKALEDL-----EKLRMQAEEAERQVK 1535
Cdd:NF033838 110 KSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEAT---KKVEEAEKKAKDQKEEDRRNYptntyKTLELEIAESDVEVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1536 QAEIEKEKQikvaheaaqksaaaelqskhmsfAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEK 1615
Cdd:NF033838 187 KAELELVKE-----------------------EAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1616 WRQKANEALrlrlqaEDEAHKKTLAQEEAEKQKEEAEREAKKR--AKAEESALKQKEMAEEELERQRKIAEstAQQKLTA 1693
Cdd:NF033838 244 KLKEAVEKN------VATSEQDKPKRRAKRGVLGEPATPDKKEndAKSSDSSVGEETLPSPSLKPEKKVAE--AEKKVEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1694 EQElirlRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELakvrsemdiliqlkTKAEKETMSNTEKSKQLLEA 1773
Cdd:NF033838 316 AKK----KAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELEL--------------VKEEAKEPRNEEKIKQAKAK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1774 EAAKMKdlaeEASRLraisEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAEN---ERLRR 1850
Cdd:NF033838 378 VESKKA----EATRL----EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQpkaEKPAD 449
|
490
....*....|....
gi 1988774686 1851 QAEDEAYQRKALED 1864
Cdd:NF033838 450 QQAEEDYARRSEEE 463
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1357-1819 |
9.20e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 81.35 E-value: 9.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1357 LAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLsEQQIKDKSQQVDEALHSRTKIEEEI 1436
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEEL-EEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1437 RLIRIQLETTEkqkytAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKA 1516
Cdd:COG4717 126 QLLPLYQELEA-----LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1517 LEDLEKLRMQAEEAERQVKQ------AEIEKEKQIKVAHEAAQK-----------SAAAELQSKHMSFAEKTSKLEESLK 1579
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEeleeleEELEQLENELEAAALEERlkearlllliaAALLALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1580 QEHG----AVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKAnEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREA 1655
Cdd:COG4717 281 LVLGllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELL-AALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1656 KKRAKAEESALKQKEM-----AEEELERQRKIAESTAQQKLTAEQELI--RLRADFDNAEQQ-----RSLLEDELYRLKN 1723
Cdd:COG4717 360 EEELQLEELEQEIAALlaeagVEDEEELRAALEQAEEYQELKEELEELeeQLEELLGELEELlealdEEELEEELEELEE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1724 EVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtmsntekskQLLEAEAAKMKDLAEEASRLRAISEE-AKHQRQIA 1802
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEEDGELAELL---------QELEELKAELRELAEEWAALKLALELlEEAREEYR 510
|
490
....*....|....*..
gi 1988774686 1803 EEEAARQRAEAERILKE 1819
Cdd:COG4717 511 EERLPPVLERASEYFSR 527
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2314-2585 |
1.21e-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: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2314 EQAQKLLEDkqlMQQRLE------EETEEYHKSLEVERKRQL---EIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQAD 2384
Cdd:COG1196 175 EEAERKLEA---TEENLErledilGELERQLEPLERQAEKAEryrELKEELKELEAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2385 KVATRLHETEIATQEKMTVVERLEFERLNTSKEA--DDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKT 2462
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEaqAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2463 VLQQTfmTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRK 2542
Cdd:COG1196 332 LEELE--EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1988774686 2543 QKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRE 2585
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1511-1863 |
1.37e-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: 80.94 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1511 KQKQKALEDLEKLRMQAE------EAERQVKQAEIEKEKQIKVAHEAAqksaaaeLQSKHMSFAEKTSKLEESLKQEhga 1584
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEkeekarEVERRRKLEEAEKARQAEMDRQAA-------IYAEQERMAMERERELERIRQE--- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1585 vlQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAedeAHKKTLAQEEAEKQKEEAEREAKKRAKAEES 1664
Cdd:pfam17380 357 --ERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEA---ARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1665 AlKQKEMAEEELERQRKIaESTAQQKLTAEQELIRLRADfdnaeqqrslledelyrlknevaAAQQQRKQLEDElakvrs 1744
Cdd:pfam17380 432 A-RQREVRRLEEERAREM-ERVRLEEQERQQQVERLRQQ-----------------------EEERKRKKLELE------ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1745 emdiliqlktKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIA-EEEAARQRAEAER---ILKEK 1820
Cdd:pfam17380 481 ----------KEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAiYEEERRREAEEERrkqQEMEE 550
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1988774686 1821 LAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAyQRKALE 1863
Cdd:pfam17380 551 RRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4015-4053 |
1.57e-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: 1.57e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1988774686 4015 LLEAQIATGGIIDPEESHRLPVEVAYNRGFFDEEMNEIL 4053
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1091-1912 |
2.03e-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: 80.88 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1091 EDCLREVHTVPSDVKEVETY----RAKLKKMRTEAEDEQPvFDSLEEELkkasavsdkmvrvhseRDVELDHFRQQLSSL 1166
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIidekRQQLERLRREREKAER-YQALLKEK----------------REYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1167 QDRWKAVFTQIDLRQRELEQLGRQLGYYRESYDWLIRWIADAKQRQEKiqavpitdsKTLKEQLAQEKKLLE---EIEQN 1243
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD---------LGEEEQLRVKEKIGEleaEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1244 KDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKKTKLDSASdnIIQEYVTLRTRYSELmtltsqyikfitdtQ 1323
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK--LTEEYAELKEELEDL--------------R 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1324 RRLDDEEKAAeklkAEERKKMAEMQAELDKqkqlaeahakaiakaekeaqelkLKMQEEVSKREIAAVDAEKQKTNIQLE 1403
Cdd:TIGR02169 371 AELEEVDKEF----AETRDELKDYREKLEK-----------------------LKREINELKRELDRLQEELQRLSEELA 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1404 lqELKNlseqQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKL-- 1481
Cdd:TIGR02169 424 --DLNA----AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAea 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1482 RKQVSEETQKKRQAEEELKRKS--------EAEKEAAKQKQKALEDLEKLRMQA---EEAERQVKQAEIEKEKQI----- 1545
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASiqgvhgtvAQLGSVGERYATAIEVAAGNRLNNvvvEDDAVAKEAIELLKRRKAgratf 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1546 ----KVAHEAAQKSAAA-----------------------------------ELQSKHMSFAEKTSkLEESLKQEHGAV- 1585
Cdd:TIGR02169 578 lplnKMRDERRDLSILSedgvigfavdlvefdpkyepafkyvfgdtlvvediEAARRLMGKYRMVT-LEGELFEKSGAMt 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1586 -------------LQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRlqaeDEAHKKTlaqeeaekqkeeae 1652
Cdd:TIGR02169 657 ggsraprggilfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL----SDASRKI-------------- 718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1653 REAKKRAkaeESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQR 1732
Cdd:TIGR02169 719 GEIEKEI---EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPE 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1733 KQLE-DELAKVRSEMD-ILIQLKTKAEKETMSNT--EKSKQLLEAEAAKMKDlaEEASRLRAISEEAKHQRQIAEEEAAR 1808
Cdd:TIGR02169 796 IQAElSKLEEEVSRIEaRLREIEQKLNRLTLEKEylEKEIQELQEQRIDLKE--QIKSIEKEIENLNGKKEELEEELEEL 873
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1809 QRAEAERI--LKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASqhkqEIEEKIVQLKKSSEA 1886
Cdd:TIGR02169 874 EAALRDLEsrLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEE 949
|
890 900
....*....|....*....|....*.
gi 1988774686 1887 EMerqkaIVDDTLKQRRVVEEEIRIL 1912
Cdd:TIGR02169 950 EL-----SLEDVQAELQRVEEEIRAL 970
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
141-238 |
2.61e-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: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 141 TAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLGVTRLLD 219
Cdd:cd21230 1 TPKQRLLGWIQ---NKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1988774686 220 PEDVDVPHPDEKSIITYVS 238
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2239-2551 |
2.80e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2239 LAEEAENmrklAEDAARLSVEAQEA-ARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQ 2317
Cdd:COG1196 205 LERQAEK----AERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2318 KLLEDKQLMQQRLEEETEEYHKSLEVERKR-------QLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRL 2390
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERrreleerLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2391 HETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMT 2470
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2471 EKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELE 2550
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
.
gi 1988774686 2551 R 2551
Cdd:COG1196 521 G 521
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1200-1876 |
3.00e-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: 79.77 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1200 WLIRWIADAKQRQEKIQ---AVPITDSKTLKE-QLAQEK---KLLEEIEQNKDKVDE----------CQKYAKAYIDTIK 1262
Cdd:pfam05483 93 WKVSIEAELKQKENKLQenrKIIEAQRKAIQElQFENEKvslKLEEEIQENKDLIKEnnatrhlcnlLKETCARSAEKTK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1263 DYELQ-------LVAYKAQVEPLVSPLKKTKLdSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRL--------- 1326
Cdd:pfam05483 173 KYEYEreetrqvYMDLNNNIEKMILAFEELRV-QAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVsllliqite 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1327 -DDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQ 1405
Cdd:pfam05483 252 kENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1406 ELKNLSEQQIKDKSQQ---VDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLR 1482
Cdd:pfam05483 332 EKEAQMEELNKAKAAHsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1483 KQVSEETQ---KKRQAE---EELKRKSEAEKEAAKQKQKALEDLEkLRMQAEEAERQVKQAEIEKEKqikvaheaaqksa 1556
Cdd:pfam05483 412 KILAEDEKlldEKKQFEkiaEELKGKEQELIFLLQAREKEIHDLE-IQLTAIKTSEEHYLKEVEDLK------------- 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1557 aAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRlqAEDEAHK 1636
Cdd:pfam05483 478 -TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR--DELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1637 KTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMA--EEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLL 1714
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1715 EDELYRLKNEVAAAQQQRKQLEDELAKVrsemdilIQLKTKAEKETMSNTEKSKQLLEaEAAKM-----KDLAEEASRLR 1789
Cdd:pfam05483 635 EIKVNKLELELASAKQKFEEIIDNYQKE-------IEDKKISEEKLLEEVEKAKAIAD-EAVKLqkeidKRCQHKIAEMV 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1790 AISEEAKHQRQIAEEEaarqRAEAERILKEKLaaiSEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQH 1869
Cdd:pfam05483 707 ALMEKHKHQYDKIIEE----RDSELGLYKNKE---QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKEN 779
|
....*..
gi 1988774686 1870 KQEIEEK 1876
Cdd:pfam05483 780 TAILKDK 786
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
141-241 |
4.77e-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: 4.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 141 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 220
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1988774686 221 ED-VDVPHPDEKSIITYVSSLY 241
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1875-2558 |
5.44e-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: 79.00 E-value: 5.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1875 EKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASsgkLDLELELNKLKNIADETQQSKIRAEEEAEKL 1954
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVS---LKLEEEIQENKDLIKENNATRHLCNLLKETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1955 RKLAlEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELerlRKKAEEARKQKDEADKEAEKQIVVAQQAAQK-CSAAEQ 2033
Cdd:pfam05483 165 ARSA-EKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL---RVQAENARLEMHFKLKEDHEKIQHLEEEYKKeINDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2034 QVQSVLAQQIEDSITQKKLkeeyekakklakeaeaakekaereAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRK 2113
Cdd:pfam05483 241 QVSLLLIQITEKENKMKDL------------------------TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2114 EaeFEAAKRAQAEAAALMQKQQADTEMAKhKKLAEQTLKQKFQVEqELTKVK----LKLDETDKQKSVLDEELQRLKDEV 2189
Cdd:pfam05483 297 E--LEDIKMSLQRSMSTQKALEEDLQIAT-KTICQLTEEKEAQME-ELNKAKaahsFVVTEFEATTCSLEELLRTEQQRL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2190 DDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLiKKDKDSTQKLLaEEAENMRKLAEDaarLSVEAQEAARLRQI 2269
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEEL-KKILAEDEKLL-DEKKQFEKIAEE---LKGKEQELIFLLQA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2270 AEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQ-KQKDLAQEQAQKLLEDKQLMQQR--LEEETEEYHKSLEVERK 2346
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTAHCDKLLLENKELTQEAsdMTLELKKHQEDIINCKK 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2347 RQLEIMAEAERLRLQVSQLseaQARAEEEAKKFKKQADKVATRLHETE-------IATQEKMTVVERLEFERLNTSKEAD 2419
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNL---RDELESVREEFIQKGDEVKCKLDKSEenarsieYEVLKKEKQMKILENKCNNLKKQIE 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2420 DLRKAIADLENEKARLKKEAEElQNKSKEMADAQQKKIEHEKTVLQQTFmteKEMLLKKEKLIEDeKKRLESQFEEEVKK 2499
Cdd:pfam05483 605 NKNKNIEELHQENKALKKKGSA-ENKQLNAYEIKVNKLELELASAKQKF---EEIIDNYQKEIED-KKISEEKLLEEVEK 679
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774686 2500 AKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRlEQER 2558
Cdd:pfam05483 680 AKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNK-EQEQ 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1254-1880 |
5.73e-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: 5.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1254 AKAYIDTIKDYELQLVAYKAQVEPLvSPLKKTKldsasdniiQEYVTLRTRYSELMTLtsqyikfitDTQRRLDDEEKAA 1333
Cdd:COG4913 230 LVEHFDDLERAHEALEDAREQIELL-EPIRELA---------ERYAAARERLAELEYL---------RAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1334 EKLKAEERkkmaEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQE------EVSKREIAavDAEKQKTNIQLELQEL 1407
Cdd:COG4913 291 ELLEAELE----ELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrlEQLEREIE--RLERELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1408 KNL----------SEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQkytAESELKQLRDRAAEAEKLRKLAQDE 1477
Cdd:COG4913 365 EALlaalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIASLERRKSNIPAR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1478 AEKLRKQVSEETQKKrqaEEELK--------RKSEAEKEAA----------------KQKQKALEDLE----KLRMQAEE 1529
Cdd:COG4913 442 LLALRDALAEALGLD---EAELPfvgelievRPEEERWRGAiervlggfaltllvppEHYAAALRWVNrlhlRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1530 AERQVKQAEIEKEK------QIKVAHEAAQKSAAAELQsKHMSFAEKTSklEESLKQEHGAVL---QLQQEAERLKKQQE 1600
Cdd:COG4913 519 VRTGLPDPERPRLDpdslagKLDFKPHPFRAWLEAELG-RRFDYVCVDS--PEELRRHPRAITragQVKGNGTRHEKDDR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1601 DAENSR----EEAEKELEKWRQKANEalrlrLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEEL 1676
Cdd:COG4913 596 RRIRSRyvlgFDNRAKLAALEAELAE-----LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1677 ERqrkiaestaqqkltAEQELIRLRADFDNAEQqrslLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKA 1756
Cdd:COG4913 671 AE--------------LEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1757 EKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKE--------------KLA 1822
Cdd:COG4913 733 QDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldaDLE 812
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774686 1823 AISE-ATRLKTEAEIALKEKEAENERLRRQAEDEayQRKALEDQASQHKQEIEEKIVQL 1880
Cdd:COG4913 813 SLPEyLALLDRLEEDGLPEYEERFKELLNENSIE--FVADLLSKLRRAIREIKERIDPL 869
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1300-1944 |
6.56e-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: 78.64 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1300 TLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDkqkqlaeahakAIAKAEKEAQELKLKM 1379
Cdd:pfam07111 52 SLELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELD-----------ALAVAEKAGQAEAEGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1380 QEEVSKREIAAVDAEKQKtniQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTekqkytaeselkq 1459
Cdd:pfam07111 121 RAALAGAEMVRKNLEEGS---QRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETK------------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1460 lrdRAAEAEKLrKLAQDEAEKLRKQVSeETQKKRQAEEELkrkseaekeaakqkqkaLEDLEKLRMQAEEAERQVKQAEI 1539
Cdd:pfam07111 185 ---RAGEAKQL-AEAQKEAELLRKQLS-KTQEELEAQVTL-----------------VESLRKYVGEQVPPEVHSQTWEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1540 EKEKQIKVAHEAaqKSAAAELQSkhmsfaekTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSR--EEAEKELEKWR 1617
Cdd:pfam07111 243 ERQELLDTMQHL--QEDRADLQA--------TVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEfpKKCRSLLNRWR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1618 QKANeALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERqrkIAESTAQQKLTAEQEL 1697
Cdd:pfam07111 313 EKVF-ALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVER---MSAKGLQMELSRAQEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1698 -IRLRADFDNAEQQRSL-----------LEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAE--KETMSN 1763
Cdd:pfam07111 389 rRRQQQQTASAEEQLKFvvnamsstqiwLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQlrQESCPP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1764 TEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQiAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEA 1843
Cdd:pfam07111 469 PPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQ-QEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1844 ENERLRRQ--AEDEAYQRKALEDQASQHKQEIEEKIVQL------------KKSSEAEMERQKAIVDDTLKQRRVVEE-- 1907
Cdd:pfam07111 548 EVARQGQQesTEEAASLRQELTQQQEIYGQALQEKVAEVetrlreqlsdtkRRLNEARREQAKAVVSLRQIQHRATQEke 627
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1988774686 1908 ---EIRILKLNFEKASSGKLDLEL-ELNKLKNIADETQQSK 1944
Cdd:pfam07111 628 rnqELRRLQDEARKEEGQRLARRVqELERDKNLMLATLQQE 668
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
600-789 |
6.68e-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: 6.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 600 LHAFVSAATKELMWLNDKEEEEVNFDWSDRNTNMTAKKDNYSGLMRELELREKKVNDIQALGDRLVRDGHPGKKTVESFT 679
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 680 AALQTQWSWILQLCCCIEAHLKENTAYYQFFADVKEAQDKMKKMQENMKkkySCDRSTTATRLEDLLQDAAEEKEQLNEF 759
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|
gi 1988774686 760 KTVVAGLNKRSRSIIQLKPRNPTTSIKGKL 789
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3701-3739 |
8.00e-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: 8.00e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1988774686 3701 LLEAQAATGFIVDPLKNETLTVDEAVRKGVVGPEIHDKL 3739
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3368-3406 |
1.29e-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: 1.29e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1988774686 3368 LLEAQAASGFIVDPVRNQCLSVDEAVKSGVVGPELHEKL 3406
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1403-1882 |
1.56e-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: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1403 ELQELKNLsEQQIKDKSQQVD-----EALHSR-TKIEEEIRLIRIQLETTekQKYTAESELKQLRDRAAEAEKLRKLAQD 1476
Cdd:COG4913 233 HFDDLERA-HEALEDAREQIEllepiRELAERyAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1477 EAEKLRKQVSEETQKKRQAEEEL-----KRKSEAEKEAAkQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEA 1551
Cdd:COG4913 310 ELERLEARLDALREELDELEAQIrgnggDRLEQLEREIE-RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1552 AQkSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQ----EDAENSREEAEKEL-------------- 1613
Cdd:COG4913 389 AA-ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEALgldeaelpfvgeli 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1614 ------EKWRQKANEAL---RLRLQAEDEAHKK-------TLAQEEAEKQKEEAEREAKKRAKAEESALKQK-------- 1669
Cdd:COG4913 468 evrpeeERWRGAIERVLggfALTLLVPPEHYAAalrwvnrLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKldfkphpf 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1670 -EMAEEELERQRKIA--ESTAQQK-----LTAE------------QELIRLRAD----FDNAEQqRSLLEDELYRLKNEV 1725
Cdd:COG4913 548 rAWLEAELGRRFDYVcvDSPEELRrhpraITRAgqvkgngtrhekDDRRRIRSRyvlgFDNRAK-LAALEAELAELEEEL 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1726 AAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKE--------TMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKH 1797
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEidvasaerEIAELEAELERLDASSDDLAALEEQLEELEAELEELEE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1798 QRQIAEEEAARQRAEAERI------LKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAY-QRKALEDQASQHK 1870
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAeeeldeLQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEeRIDALRARLNRAE 786
|
570
....*....|..
gi 1988774686 1871 QEIEEKIVQLKK 1882
Cdd:COG4913 787 EELERAMRAFNR 798
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2322-2581 |
1.89e-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: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2322 DKQLmqQRLEEE---TEEYHKSLEVERKRQLEIMA-EAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIAT 2397
Cdd:COG1196 199 ERQL--EPLERQaekAERYRELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2398 QEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLK 2477
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2478 KEKLIEDEKKRLESqfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQE 2557
Cdd:COG1196 357 EAELAEAEEALLEA--EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260
....*....|....*....|....
gi 1988774686 2558 RILAEENQKLREKLQQLEDAQKDQ 2581
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEE 458
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
141-241 |
2.49e-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: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 141 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 220
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1988774686 221 ED-VDVPHPDEKSIITYVSSLY 241
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
16-121 |
3.28e-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: 68.85 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 16 DERDrvqKKTFTKWVNKHLIKAQRHvtDLYEDLRDGhnlISLLEVL--------SGETLPREKGRMRFHKLQNVQIALDF 87
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLDPLIN--NLYEDLRDG---LVLLQVLdkiqpgcvNWKKVNKPKPLNKFKKVENCNYAVDL 73
|
90 100 110
....*....|....*....|....*....|....
gi 1988774686 88 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 121
Cdd:cd21219 74 AKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1654-1886 |
3.75e-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: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1654 EAKKRAKAEESALKQK-EMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQR 1732
Cdd:COG4942 20 DAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1733 KQLEDELAKVRSEMdiliqlktkaekETMSNTEKSKQLLEAEaakmkDLAEEASRLRAISEEAKHQRQIAEE------EA 1806
Cdd:COG4942 100 EAQKEELAELLRAL------------YRLGRQPPLALLLSPE-----DFLDAVRRLQYLKYLAPARREQAEElradlaEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1807 ARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEA 1886
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1373-1932 |
4.06e-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: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1373 QELKlKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQ-QIKDKSQQVDEAlHSRTKIE-EEIRLIRIQLETTEKQK 1450
Cdd:pfam05701 42 LELE-KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEElKLNLERAQTEEA-QAKQDSElAKLRVEEMEQGIADEAS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1451 YTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQ----VSEETQKKRQAEEELKrkseaekeAAKQKQKALEDLEKLRMQ 1526
Cdd:pfam05701 120 VAAKAQLEVAKARHAAAVAELKSVKEELESLRKEyaslVSERDIAIKRAEEAVS--------ASKEIEKTVEELTIELIA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1527 AEEAERQVKQAEIEKEKqikvaheaaQKSAAAelqskhMSFAEKTSKLEESLKqehgavlQLQQEAERLKKQQedaeNSR 1606
Cdd:pfam05701 192 TKESLESAHAAHLEAEE---------HRIGAA------LAREQDKLNWEKELK-------QAEEELQRLNQQL----LSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1607 EEAEKELEkwrqkANEALRLRLQAEDEAHKktlaqeeaekqKEEAEREAKKRAKAEESALKQKEM---AEEELERQRKIA 1683
Cdd:pfam05701 246 KDLKSKLE-----TASALLLDLKAELAAYM-----------ESKLKEEADGEGNEKKTSTSIQAAlasAKKELEEVKANI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1684 EstaqqKLTAEQELIRLRAdfdnaeqqrSLLEDELYRLKNEVAAAQQQR-------KQLEDELAKVRSEMDiLIQLKTKA 1756
Cdd:pfam05701 310 E-----KAKDEVNCLRVAA---------ASLRSELEKEKAELASLRQREgmasiavSSLEAELNRTKSEIA-LVQAKEKE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1757 EKETMsnTEKSKQLLEA--EAAKMKDLAEEA-SRLRAISEEAKHQRqiAEEEAARQRAEAerILKEKLAAIsEATRLKTE 1833
Cdd:pfam05701 375 AREKM--VELPKQLQQAaqEAEEAKSLAQAArEELRKAKEEAEQAK--AAASTVESRLEA--VLKEIEAAK-ASEKLALA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1834 AEIALKEKEAENERLRRQA----------EDEAYQRKALEDQASQHKQeIEEKIVQLKKSSEAEMeRQKAIVDDTLKQRR 1903
Cdd:pfam05701 448 AIKALQESESSAESTNQEDsprgvtlsleEYYELSKRAHEAEELANKR-VAEAVSQIEEAKESEL-RSLEKLEEVNREME 525
|
570 580
....*....|....*....|....*....
gi 1988774686 1904 VVEEEIRILKLNFEKASSGKLDLELELNK 1932
Cdd:pfam05701 526 ERKEALKIALEKAEKAKEGKLAAEQELRK 554
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
40-119 |
4.45e-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: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 40 HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM----RFHKLQNVQIALDFLRHRQV----KLVNIRNDDIADGNPKLT 111
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1988774686 112 LGLIWTII 119
Cdd:cd21223 105 LALLWRII 112
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3037-3075 |
7.70e-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: 7.70e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1988774686 3037 LLEAQAGTGYLVDPVHNQKYTVDEAVKAGVVGPELHEKL 3075
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1567-2045 |
8.63e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.80 E-value: 8.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1567 FAEKTSKLEEsLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANealRLRLQAEDEAHKKTLAQEEAEK 1646
Cdd:COG4717 73 LKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ---LLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1647 qkeeaeREAKKRAKAEESALKQKEMAEEELER-QRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEV 1725
Cdd:COG4717 149 ------EELEERLEELRELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1726 AAAQQQRKQLEDELA------KVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKmkdLAEEASRLRAISEEAKHQR 1799
Cdd:COG4717 223 EELEEELEQLENELEaaaleeRLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF---LVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1800 QIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAyqrKALEDQASQhkQEIEEKIVQ 1879
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA---EELEEELQL--EELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1880 LKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLeLELNKLKNIADETQQSKIRAEEEAEKLRKLal 1959
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEELEEELEEL-- 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1960 eeekrrreaeekvkkiaAAEEEAARQRKAALE---ELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQ 2036
Cdd:COG4717 452 -----------------REELAELEAELEQLEedgELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
....*....
gi 1988774686 2037 SVLAQQIED 2045
Cdd:COG4717 515 PPVLERASE 523
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1102-1887 |
1.08e-12 |
|
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: 75.21 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1102 SDVKEVETYRAKLKKMRTEAEdeqPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRwkavftqidlrq 1181
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHE---AMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ------------ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1182 reLEQLGRQLGYYRESydwlirwIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQnkdkvdECQKYAKAYiDTI 1261
Cdd:pfam01576 231 --IAELRAQLAKKEEE-------LQAALARLEEETAQKNNALKKIRELEAQISELQEDLES------ERAARNKAE-KQR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1262 KDYELQLVAYKAQVEplvsplkkTKLDSAsdNIIQEyvtlrtryselmtLTSQYIKFITDTQRRLDDEEKAAEKLKAEER 1341
Cdd:pfam01576 295 RDLGEELEALKTELE--------DTLDTT--AAQQE-------------LRSKREQEVTELKKALEEETRSHEAQLQEMR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1342 KKMA----EMQAELDKQKQLAEAHAKAIAKAEKEAQELklkmQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKD 1417
Cdd:pfam01576 352 QKHTqaleELTEQLEQAKRNKANLEKAKQALESENAEL----QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQ 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1418 KSQQVDEAlhsrTKIEEEIRLIRIQLETTEKQKYTAESELKQL---------------RDRAAEAEKLRKLaQDEAEKLR 1482
Cdd:pfam01576 428 RAELAEKL----SKLQSELESVSSLLNEAEGKNIKLSKDVSSLesqlqdtqellqeetRQKLNLSTRLRQL-EDERNSLQ 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1483 KQVSEETQKKRQAEE----------ELKRKSEAEKEAAKQ----KQKALEDLEKLRMQAEEAERQVKQAEIEKEkqiKVA 1548
Cdd:pfam01576 503 EQLEEEEEAKRNVERqlstlqaqlsDMKKKLEEDAGTLEAleegKKRLQRELEALTQQLEEKAAAYDKLEKTKN---RLQ 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1549 HEAAQKSAAAELQSKHMSFAEKTS-KLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALR-- 1625
Cdd:pfam01576 580 QELDDLLVDLDHQRQLVSNLEKKQkKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERtn 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1626 --LRLQAEDEAHKKtlaqeeaeKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTaqqKLTAEQELIRLRAD 1703
Cdd:pfam01576 660 kqLRAEMEDLVSSK--------DDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDA---KLRLEVNMQALKAQ 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1704 FDN--------AEQQRSLLEDELYRLKNEVAAAQQQRKQLEDelAKVRSEMDiLIQLKTKAEKETMSNTEKSKQLLEAEa 1775
Cdd:pfam01576 729 FERdlqardeqGEEKRRQLVKQVRELEAELEDERKQRAQAVA--AKKKLELD-LKELEAQIDAANKGREEAVKQLKKLQ- 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1776 AKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERiLKEKLAAiseatrlkteAEIALKEKEAENERLRRQAEDE 1855
Cdd:pfam01576 805 AQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQ-LQEDLAA----------SERARRQAQQERDELADEIASG 873
|
810 820 830
....*....|....*....|....*....|..
gi 1988774686 1856 AYQRKALEDQasqhKQEIEEKIVQLKKSSEAE 1887
Cdd:pfam01576 874 ASGKSALQDE----KRRLEARIAQLEEELEEE 901
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1994-2589 |
1.28e-12 |
|
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: 75.01 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1994 ERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQsVLAQQIEDSITQKKLKEEyEKAKKLAKEAEAAKEKA 2073
Cdd:pfam02463 145 EIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAE-LIIDLEELKLQELKLKEQ-AKKALEYYQLKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2074 EREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQ 2153
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE-KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2154 KFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKD 2233
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2234 STQKLLAEEAENmRKLAEDAARLSVEAQEAARLRQIAEDDL---NQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKD 2310
Cdd:pfam02463 382 ESERLSSAAKLK-EEELELKSEEEKEAQLLLELARQLEDLLkeeKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2311 LAQEQAQKLLEDKqlmQQRLEEETEEYHKSLEVERK-----RQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADK 2385
Cdd:pfam02463 461 LKDELELKKSEDL---LKETQLVKLQEQLELLLSRQkleerSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2386 VATRLHETEIATQEKMTVVERLEFERLN----TSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEK 2461
Cdd:pfam02463 538 VENYKVAISTAVIVEVSATADEVEERQKlvraLTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2462 TVLQQTFMTEKEMLLKKEKLIE-------------------DEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQ 2522
Cdd:pfam02463 618 DDKRAKVVEGILKDTELTKLKEsakakesglrkgvsleeglAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774686 2523 ATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKV 2589
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1988-2586 |
1.29e-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: 74.62 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1988 AALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQ------KCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKK 2061
Cdd:TIGR00618 170 MNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLctpcmpDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2062 LAKEAEAAkekaereaalLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAAlmQKQQADTEMA 2141
Cdd:TIGR00618 250 EAQEEQLK----------KQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQ--QAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2142 KHKKLAEQTLKQKFQVEQEltkvklklDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIE 2221
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQ--------QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2222 EENQRLikkdKDSTQKLLAEEAENMRKLAEDAARlSVEAQEAARLR---QIAEDDLNQQRALAEKMLKEKMQAIQEASR- 2297
Cdd:TIGR00618 390 TLTQKL----QSLCKELDILQREQATIDTRTSAF-RDLQGQLAHAKkqqELQQRYAELCAAAITCTAQCEKLEKIHLQEs 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2298 ---LKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQ-----VSQLSEAQ 2369
Cdd:TIGR00618 465 aqsLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQrgeqtYAQLETSE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2370 ARAEEEAKKFKKQA----DKVATRLHETEIATQEKMTVVERLEferlNTSKEADDLRKAIADLENEKARLKKEAEELQNK 2445
Cdd:TIGR00618 545 EDVYHQLTSERKQRaslkEQMQEIQQSFSILTQCDNRSKEDIP----NLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2446 SKEMADAQQKKIE----HEKTVLQQTFMTEKEMLLKKEK------LIEDEKKRLESQFEEEVKKAKALKDEQERQKQQME 2515
Cdd:TIGR00618 621 LQPEQDLQDVRLHlqqcSQELALKLTALHALQLTLTQERvrehalSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 2516 QEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRET 2586
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2145-2577 |
1.56e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.03 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2145 KLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEeelfkvkvQMEELLKLKNKIEEEN 2224
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP--------LYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2225 QRLikkdkdstqKLLAEEAENMRKLAEDAARLSVEAQEAarlrqiaeddlnqQRALAEKMLKEKMQAIQEASRLKAEAEM 2304
Cdd:COG4717 146 ERL---------EELEERLEELRELEEELEELEAELAEL-------------QEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2305 LQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEE---------- 2374
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2375 ------------EAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEEL 2442
Cdd:COG4717 284 gllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2443 QNKSKEmadaqqkkiEHEKTVLQQTFMTEKEMLLKKEKL------IEDEKKRLESQFEEEVKKAKALKDEQErqKQQMEQ 2516
Cdd:COG4717 364 QLEELE---------QEIAALLAEAGVEDEEELRAALEQaeeyqeLKEELEELEEQLEELLGELEELLEALD--EEELEE 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 2517 EKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQEriLAEENQKLREKLQQLEDA 2577
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE--LLQELEELKAELRELAEE 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1893-2589 |
1.68e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.33 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1893 AIVDDTLKQRRVVEEEIRILKlnFEKASSGKLDLELELNKLKniadETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKV 1972
Cdd:PRK03918 139 AILESDESREKVVRQILGLDD--YENAYKNLGEVIKEIKRRI----ERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1973 KKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVqSVLAQQIEDSITQKKL 2052
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI-EELEEKVKELKELKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2053 KEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKE-AEFEAAKRAQaeaaalm 2131
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRlEELEERHELY------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2132 qkqqadtEMAKHKKLAEQTLKQKFQVEqELTKVKLKLDETDKQKSVLDEELQRLKDEvddavkqRGQVEEELFKVKVQME 2211
Cdd:PRK03918 365 -------EEAKAKKEELERLKKRLTGL-TPEKLEKELEELEKAKEEIEEEISKITAR-------IGELKKEIKELKKAIE 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2212 ELLKLKNKIEEENQRLIKKDKdstQKLLAEEAENMRKLAEDAARLsveaqeAARLRQIaeddlnqqralaEKMLKEKMQA 2291
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHR---KELLEEYTAELKRIEKELKEI------EEKERKL------------RKELRELEKV 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2292 IQEASRLKAEAEMLQKQKDLAQEQAQKLLEDkqlmqqrLEEETEEYHKSLEverkRQLEIMAEAERLRLQVSQLSEAQAR 2371
Cdd:PRK03918 489 LKKESELIKLKELAEQLKELEEKLKKYNLEE-------LEKKAEEYEKLKE----KLIKLKGEIKSLKKELEKLEELKKK 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2372 AEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMAD 2451
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAE 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2452 AQqKKIEhektvlqqtfMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQatmdaalsK 2531
Cdd:PRK03918 638 TE-KRLE----------ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE--------K 698
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774686 2532 QKEAEEEMLRKQKEMQELERQRleqerilaEENQKLREKLQQLEDAQKDQHTRETDKV 2589
Cdd:PRK03918 699 LKEELEEREKAKKELEKLEKAL--------ERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1729-2579 |
2.11e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 74.09 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1729 QQQRKQLEDELAKVRSEMDiliQLKTKAEKETMSNTEKSKQ-------LLEAEAAKMK-------DLAEEASR-LRAISE 1793
Cdd:NF041483 7 QESHRADDDHLSRFEAEMD---RLKTEREKAVQHAEDLGYQvevlrakLHEARRSLASrpaydgaDIGYQAEQlLRNAQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1794 EAKHQRQIAEEEAARQRAEAERILKEKlaaISEATRLKTEAeialkEKEAeNERLRRQAEDEAYQRKALEDQ-------A 1866
Cdd:NF041483 84 QADQLRADAERELRDARAQTQRILQEH---AEHQARLQAEL-----HTEA-VQRRQQLDQELAERRQTVESHvnenvawA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1867 SQHKQEIEEKIVQLKKSSEAEMErqKAIVDDTLKQRRVVEEEIRILKLNFEKASSgkldlelelnklkniadETQQSKIR 1946
Cdd:NF041483 155 EQLRARTESQARRLLDESRAEAE--QALAAARAEAERLAEEARQRLGSEAESARA-----------------EAEAILRR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1947 AEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAAL---------EELERLRKKAEEARKQKDEADKEAEKQ 2017
Cdd:NF041483 216 ARKDAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELsraaeqrmqEAEEALREARAEAEKVVAEAKEAAAKQ 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2018 IVVAQQA-AQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAAL-------LRQQAEEAER 2089
Cdd:NF041483 296 LASAESAnEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAaedtaaqLAKAARTAEE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2090 QKTAAEE-EAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQA---DTE--MAKHKKLAEQTLKQKFQVEQeltk 2163
Cdd:NF041483 376 VLTKASEdAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAakdDTKeyRAKTVELQEEARRLRGEAEQ---- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2164 vkLKLDETDKQKSVLDEELQRLKDEVDDAVKqrgQVEEELFKVKVQMEElLKLKNKIEEENQRLIKKDKDSTQKLLAEEA 2243
Cdd:NF041483 452 --LRAEAVAEGERIRGEARREAVQQIEEAAR---TAEELLTKAKADADE-LRSTATAESERVRTEAIERATTLRRQAEET 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2244 enMRKLAEDAARLSVEAQE-AARLRQIAEDDLNQQRALAEK-MLKEKMQAIQEASRLKAEAEmlqkQKDLAQEQAqklLE 2321
Cdd:NF041483 526 --LERTRAEAERLRAEAEEqAEEVRAAAERAARELREETERaIAARQAEAAEELTRLHTEAE----ERLTAAEEA---LA 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2322 DKQLMQQRLEEETEEYHKSLEV---ERKRQLEIMAEAERLRLQVSQLSEAQARaeeeakkfKKQADKVATRLHETEIATQ 2398
Cdd:NF041483 597 DARAEAERIRREAAEETERLRTeaaERIRTLQAQAEQEAERLRTEAAADASAA--------RAEGENVAVRLRSEAAAEA 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2399 EKMTVVERLEFERLNTSKEADDLR------KAIADLENEKARLKKEAEELQNKSKEMADAQQKKI-EHEKTVLQQTFMTE 2471
Cdd:NF041483 669 ERLKSEAQESADRVRAEAAAAAERvgteaaEALAAAQEEAARRRREAEETLGSARAEADQERERArEQSEELLASARKRV 748
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2472 KEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMD-AALSKQKEAEEEMLRKQKEMQElE 2550
Cdd:NF041483 749 EEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEhAAERTRTEAQEEADRVRSDAYA-E 827
|
890 900
....*....|....*....|....*....
gi 1988774686 2551 RQRleqeriLAEENQKLREKLQQLEDAQK 2579
Cdd:NF041483 828 RER------ASEDANRLRREAQEETEAAK 850
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1745-2519 |
2.57e-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: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1745 EMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAI 1824
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1825 SEATRLKTEAEIALKEKEAENERLRRQaedeayqrkaleDQASQHKQEIEEKIVQlkkssEAEMERQKAIVDDTLKQRRV 1904
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQ------------QLLKQLRARIEELRAQ-----EAVLEETQERINRARKAAPL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1905 VEEEIRILKLNFeKASSGKLDLELELNKLkniADETQQSKIRAEEEAEKLRKLALeeEKRRREAEEKVKKIAAAEEEAAR 1984
Cdd:TIGR00618 296 AAHIKAVTQIEQ-QAQRIHTELQSKMRSR---AKLLMKRAAHVKQQSSIEEQRRL--LQTLHSQEIHIRDAHEVATSIRE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1985 QRKAALEELERLRKKAEEarKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAK 2064
Cdd:TIGR00618 370 ISCQQHTLTQHIHTLQQQ--KTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2065 EAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHK 2144
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLT 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2145 KLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELlklknkieeen 2224
Cdd:TIGR00618 528 RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL----------- 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2225 qrlikkdkdstQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKML-KEKMQAIQEASRLKAEAE 2303
Cdd:TIGR00618 597 -----------QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTaLHALQLTLTQERVREHAL 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2304 MLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKrQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQA 2383
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRE-LETHIEEYDREFNEIENASSSLGSDLAAREDALNQS 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2384 DKVATRLHETEIATQEkmtvverLEFERLNTSKEADDLRKA-IADLENEKARLKKEAEELQNKSKEMADAQQKKIEH--- 2459
Cdd:TIGR00618 745 LKELMHQARTVLKART-------EAHFNNNEEVTAALQTGAeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSded 817
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2460 EKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKK 2519
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4289-4327 |
2.66e-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: 2.66e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1988774686 4289 LLEAQACTGGIIDPTSGEKYSIAEATEKGLVDKIMVDRL 4327
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1324-1863 |
2.84e-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: 73.24 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1324 RRLDDEEKAAEKLK---AEERKKMAEMQAELDK-QKQLAEAHAKAiaKAEKEAQELKLKMQEEVSK----REIAAVDAEK 1395
Cdd:pfam05557 27 RARIELEKKASALKrqlDRESDRNQELQKRIRLlEKREAEAEEAL--REQAELNRLKKKYLEALNKklneKESQLADARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1396 QKTNIQLELQELKnlseQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKL-RKLA 1474
Cdd:pfam05557 105 VISCLKNELSELR----RQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELeFEIQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1475 Q--DEAEKLRKQVSE-------ETQKKRQAEE-----ELKRKSEAEKEAAKQKQKALEDLEKlrMQAEEAERQVKQAEIE 1540
Cdd:pfam05557 181 SqeQDSEIVKNSKSElaripelEKELERLREHnkhlnENIENKLLLKEEVEDLKRKLEREEK--YREEAATLELEKEKLE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1541 KEKQ--IKVAHEA--------AQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAE 1610
Cdd:pfam05557 259 QELQswVKLAQDTglnlrspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1611 KELEKWRQKAnealrLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTA--- 1687
Cdd:pfam05557 339 ALVRRLQRRV-----LLLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELggy 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1688 -QQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQlktkaeketMSNTEK 1766
Cdd:pfam05557 414 kQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQG---------DYDPKK 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1767 SK--QLLEAEAAKMKD-LAEEASRLRaiseeakhqrqiAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEA 1843
Cdd:pfam05557 485 TKvlHLSMNPAAEAYQqRKNQLEKLQ------------AEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKEL 552
|
570 580
....*....|....*....|
gi 1988774686 1844 ENERLRRQAEDEAYQRKALE 1863
Cdd:pfam05557 553 ESAELKNQRLKEVFQAKIQE 572
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
24-118 |
2.85e-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: 66.10 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 24 KTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVL-------SGETLPREKGRMRFHKLQNVQIALDFLRHRQVKLV 96
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|..
gi 1988774686 97 NIRNDDIADGNPKLTLGLIWTI 118
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQL 108
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1475-1734 |
2.95e-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: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1475 QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKA-LEDLEKL--RMQAEEAERQVKQAEIEKEKQIKVAHEA 1551
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAeQARQKELeqRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1552 AQKSAaaelqskhmsfAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRlRLQAE 1631
Cdd:TIGR02794 125 KAKQA-----------AEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEA-KAKAE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1632 DEAHKKtlaqeeaekqkeeaeREAKKRAKAEESALKQKE-MAEEELERQRKIAESTAQQKLTAEQELirlradfdNAEQQ 1710
Cdd:TIGR02794 193 EAKAKA---------------EAAKAKAAAEAAAKAEAEaAAAAAAEAERKADEAELGDIFGLASGS--------NAEKQ 249
|
250 260
....*....|....*....|....
gi 1988774686 1711 RSLLEDELYRLKNEVAAAQQQRKQ 1734
Cdd:TIGR02794 250 GGARGAAAGSEVDKYAAIIQQAIQ 273
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1463-1677 |
3.73e-12 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 71.76 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1463 RAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKaledleklrmQAEEAERQVKQAEIEKE 1542
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK----------QAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1543 KQIKVAHEAAQKSAAAElqskHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDA-ENSREEAEKELEKWRQKan 1621
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAE----AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAaAKAAAEAKKKAEAEAKK-- 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774686 1622 ealrlrlQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELE 1677
Cdd:PRK09510 210 -------KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1358-1612 |
5.53e-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: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1358 AEAHAKAIAKAEKEAQELKLKMQEEVSKREiaavDAEKQKTNIQLELQELknlsEQQIKDKSQQVDEalhsrtkIEEEIR 1437
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELA----ALKKEEKALLKQLAAL----ERRIAALARRIRA-------LEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1438 LIRIQLETTEKQKYTAESELKQLRDRAAE-AEKLRKLAQDEAEKLRKQVSEETQKKRQAeEELKRKSEAEKEAAKQKQKA 1516
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLDAVRRL-QYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1517 LEDLEKLRmqaeeaerqvkqAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLK 1596
Cdd:COG4942 159 LAELAALR------------AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*.
gi 1988774686 1597 KQQEDAENSREEAEKE 1612
Cdd:COG4942 227 ALIARLEAEAAAAAER 242
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2710-2747 |
5.81e-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: 5.81e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1988774686 2710 LLEAQAATGYMLDPIKNQKLSVNAAVKEGLIGPELHNK 2747
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2134-2665 |
6.90e-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: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2134 QQADTEMAKHKKLAEQTlkQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQmeEL 2213
Cdd:COG4913 265 AAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD--RL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2214 LKLKNKIEEENQRLIKKDKDSTQklLAEEAENMR-KLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAI 2292
Cdd:COG4913 341 EQLEREIERLERELEERERRRAR--LEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2293 QEASRLKAEAEMLQKQK---DLAQEQAQKLLEDK------------QLMQQRLEEEteEYHKSLE-----------VERK 2346
Cdd:COG4913 419 RELRELEAEIASLERRKsniPARLLALRDALAEAlgldeaelpfvgELIEVRPEEE--RWRGAIErvlggfaltllVPPE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2347 RQLEIMA--EAERLRLQVSQLSEAQARAEEEAKKFKKQ--ADKVATRLH------ETEIATQEKMTVVERLE-FERLN-- 2413
Cdd:COG4913 497 HYAAALRwvNRLHLRGRLVYERVRTGLPDPERPRLDPDslAGKLDFKPHpfrawlEAELGRRFDYVCVDSPEeLRRHPra 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2414 -----------TSKEADDL-------------RKAIADLENEKARLKKEAEELQNKSKEMADAQQ--KKIEHEKTVLQQT 2467
Cdd:COG4913 577 itragqvkgngTRHEKDDRrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEY 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2468 FMTEKEMLLKKEKL--IEDEKKRLES------QFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEM 2539
Cdd:COG4913 657 SWDEIDVASAEREIaeLEAELERLDAssddlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2540 LRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKVlhkdiihlTTIETTKTVYNGQNVGDVVDGI 2619
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAE--------EELERAMRAFNREWPAETADLD 808
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1988774686 2620 DKKPDPLAFDGIRDKVPASRLHELgvlpKKEFDKLKNgETTVQELG 2665
Cdd:COG4913 809 ADLESLPEYLALLDRLEEDGLPEY----EERFKELLN-ENSIEFVA 849
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1804-2441 |
7.79e-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: 72.06 E-value: 7.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1804 EEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAL--EDQASQHKQEI--EEKIVQ 1879
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikENNATRHLCNLlkETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1880 LKKSSEAEMERQKAI-----VDDTLKQRRVVEEEIRIlklnfeKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKL 1954
Cdd:pfam05483 168 AEKTKKYEYEREETRqvymdLNNNIEKMILAFEELRV------QAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1955 RKLALEEEKRRREAEEKVKKIAAAEeeaaRQRKAALEELERLR-KKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQ 2033
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEES----RDKANQLEEKTKLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2034 QVQ---SVLAQQIEDSITQkkLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAER 2110
Cdd:pfam05483 318 DLQiatKTICQLTEEKEAQ--MEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2111 L-----RKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTL-----------------------------KQKFQ 2156
Cdd:pfam05483 396 MtkfknNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELifllqarekeihdleiqltaiktseehylKEVED 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2157 VEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLiKKDKDSTQ 2236
Cdd:pfam05483 476 LKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNL-RDELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2237 KLLAEEAENMR----KLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLA 2312
Cdd:pfam05483 555 EEFIQKGDEVKckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2313 QEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEE-----------AKKFKK 2381
Cdd:pfam05483 635 EIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRcqhkiaemvalMEKHKH 714
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774686 2382 QADKVA----TRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEE 2441
Cdd:pfam05483 715 QYDKIIeerdSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
143-242 |
1.05e-11 |
|
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: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 143 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN---LENLEQAFSVAEK-DLGVTRLL 218
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1988774686 219 DPEDVdVPHPDEKSIITYVSSLYD 242
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2786-2823 |
1.59e-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: 1.59e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1988774686 2786 VLEAQLATGGIIDPINSHRVPTETAYKQGHYDAEMNKI 2823
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
17-116 |
1.68e-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: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 17 ERDRvQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLE-VLSGE-------TLPREKGRMRFHKLQNVQIALDFL 88
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDkVIPGSvnwkkvnKAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1988774686 89 RHRQVKLVNIRNDDIADGNPKLTLGLIW 116
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3778-3815 |
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 1988774686 3778 LEAQTATGGIIDPEFQFHLPTDVAMQRGYINKETNEKL 3815
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
143-243 |
1.81e-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: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 143 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 222
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 1988774686 223 VdVPHPDEKSIITYVSSLYDA 243
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1568-2013 |
2.11e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.84 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1568 AEKTSK-LEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLR-----LQ---AEDEAHKKT 1638
Cdd:PRK02224 197 EEKEEKdLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEaeiedLRetiAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1639 LAQEEAEKQKEEAEREAKKRAKAEESAL----------------KQKEMAEEELERQR-----------------KIAES 1685
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLddadaeavearreeleDRDEELRDRLEECRvaaqahneeaeslredaDDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1686 TAQQKL----TAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQ--LKTKAEKE 1759
Cdd:PRK02224 357 RAEELReeaaELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREreAELEATLR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1760 TMSNT-EKSKQLLEA--------------EAAKMKDLAEEASRLRAISEEAKHQRQIAEE--EAARQRAEAERILKEKLA 1822
Cdd:PRK02224 437 TARERvEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEErlERAEDLVEAEDRIERLEE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1823 AISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLkksseAEMERQKAIVDDTLKQR 1902
Cdd:PRK02224 517 RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV-----AELNSKLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1903 RVVEEEirilklnFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLAleeekrrreaeekvKKIAAAEEEA 1982
Cdd:PRK02224 592 ERIRTL-------LAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELE--------------AEFDEARIEE 650
|
490 500 510
....*....|....*....|....*....|..
gi 1988774686 1983 ARQRKAALEE-LERLRKKAEEARKQKDEADKE 2013
Cdd:PRK02224 651 AREDKERAEEyLEQVEEKLDELREERDDLQAE 682
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2167-2580 |
2.16e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2167 KLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEE--------ENQRLIKKDKDSTQKL 2238
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDlretiaetEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2239 LAEEAENMRKLAEDAARLSVEAQEAARLRQiaeDDLNQQRALAEKMLKEKMQAIQEAsrlKAEAEMLQKQKDLAQEQAQK 2318
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDADAEAVEARR---EELEDRDEELRDRLEECRVAAQAH---NEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2319 LLEDKQlmqqRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQ 2398
Cdd:PRK02224 361 LREEAA----ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2399 EKMTVVERLEfERLNTSK---------------EADDLRKAIADLENEKARLKKEAEELQNKSKEMADAqqKKIEHEKTV 2463
Cdd:PRK02224 437 TARERVEEAE-ALLEAGKcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL--VEAEDRIER 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2464 LQQTFMTEKEMLLKKEKLIEDEKKRLESQFEE--------EVKKAKALKDEQERQKQQ-----MEQEKKTLQATMDA--- 2527
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERaaeleaeaEEKREAAAEAEEEAEEAReevaeLNSKLAELKERIESler 593
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 2528 ---ALSKQKEAEEEMLR---KQKEMQELERQRLEQ-----ERI--LAEEN-----QKLREKLQQLEDAQKD 2580
Cdd:PRK02224 594 irtLLAAIADAEDEIERlreKREALAELNDERRERlaekrERKreLEAEFdeariEEAREDKERAEEYLEQ 664
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1676-2557 |
2.57e-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: 70.46 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1676 LERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRslleDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTK 1755
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIR----DQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1756 AEK--ETMSNTEKSKQLLEAEAAKMKDLAEEAsrLRAISEEAK---HQRQIAEEEAARQRAEAERILKEKLAAISEATRL 1830
Cdd:TIGR00606 264 IMKldNEIKALKSRKKQMEKDNSELELKMEKV--FQGTDEQLNdlyHNHQRTVREKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1831 KTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQAS----QHKQEIEEKIVQLKKSSEAEMERQKAIV---------DD 1897
Cdd:TIGR00606 342 KTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfERGPFSERQIKNFHTLVIERQEDEAKTAaqlcadlqsKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1898 TLKQRRVVEEEIRILKLNfEKASSGKLDLELELNKLKNIADETQQ---SKIRAEEEAEKLRKLALEEEKRRREAEEKVKK 1974
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLG-RTIELKKEILEKKQEELKFVIKELQQlegSSDRILELDQELRKAERELSKAEKNSLTETLK 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1975 iaaaeeeaARQRKAALEELERLRKKAEEARKQKD-EADKEAEKQIvvaQQAAQKCSAAEQQVQSVLAQQIEDSITQ---- 2049
Cdd:TIGR00606 501 --------KEVKSLQNEKADLDRKLRKLDQEMEQlNHHTTTRTQM---EMLTKDKMDKDEQIRKIKSRHSDELTSLlgyf 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2050 ----------KKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQE---DAERLRKEAE 2116
Cdd:TIGR00606 570 pnkkqledwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDeesDLERLKEEIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2117 FEAAKRAQAEAAALMQKQQAdTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDET-----DKQKSvLDEELQRLKDEVDD 2191
Cdd:TIGR00606 650 KSSKQRAMLAGATAVYSQFI-TQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKlrlapDKLKS-TESELKKKEKRRDE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2192 AVkqrGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKD-STQKLLAEEAENMRKLAEDA-------ARLSVEAQEA 2263
Cdd:TIGR00606 728 ML---GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDiEEQETLLGTIMPEEESAKVCltdvtimERFQMELKDV 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2264 AR--LRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLledkqlmQQRLEE-ETEEYHKS 2340
Cdd:TIGR00606 805 ERkiAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL-------KSKTNElKSEKLQIG 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2341 LEVERKRQLE-----IMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERlefERLNTS 2415
Cdd:TIGR00606 878 TNLQRRQQFEeqlveLSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKE---KVKNIH 954
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2416 KEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEK--EMLLKKE---KLIEDEKKRLE 2490
Cdd:TIGR00606 955 GYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKiqERWLQDNltlRKRENELKEVE 1034
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2491 ---SQFEEEVKKAKALKDEQERQKqqMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQE 2557
Cdd:TIGR00606 1035 eelKQHLKEMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1325-1850 |
3.22e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1325 RLDDEEKAAEKLKaEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKlkmqEEVSKREIAAVDAEKQKTNIQLEL 1404
Cdd:PRK03918 156 GLDDYENAYKNLG-EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVL----REINEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1405 QELKNLSEQqIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKqkytaesELKQLRDRAAEAEKLRKLAqDEAEKLRKQ 1484
Cdd:PRK03918 231 KELEELKEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKK-------EIEELEEKVKELKELKEKA-EEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1485 VSEETQKKRQAEEELKRKSEAEKEAakqkQKALEDLEKLRMQAEEAERQVKqaEIEKEKqikvaheaaqksaaAELQSKH 1564
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGI----EERIKELEEKEERLEELKKKLK--ELEKRL--------------EELEERH 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1565 MSFAEKTSKLE--ESLKQEHGAvlqlqQEAERLKKQQEDAENSREEAEKELEKWRQK----ANEALRLRLQAE------- 1631
Cdd:PRK03918 362 ELYEEAKAKKEelERLKKRLTG-----LTPEKLEKELEELEKAKEEIEEEISKITARigelKKEIKELKKAIEelkkakg 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1632 ---------DEAHKKTLAQ---------EEAEKQKEEAEREAKKRAKAEESAL-------KQKEMAE------------- 1673
Cdd:PRK03918 437 kcpvcgrelTEEHRKELLEeytaelkriEKELKEIEEKERKLRKELRELEKVLkkeseliKLKELAEqlkeleeklkkyn 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1674 -EELERQRKIAESTAQQKLTAEQELIRLRADF-----------------DNAEQQRSLLEDELY---------------- 1719
Cdd:PRK03918 517 lEELEKKAEEYEKLKEKLIKLKGEIKSLKKELekleelkkklaelekklDELEEELAELLKELEelgfesveeleerlke 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1720 ---------RLKN---EVAAAQQQRKQLEDELAKVRSEMDiliQLKTKAEKETMSNTEKSKQLLEAEAAKMKD----LAE 1783
Cdd:PRK03918 597 lepfyneylELKDaekELEREEKELKKLEEELDKAFEELA---ETEKRLEELRKELEELEKKYSEEEYEELREeyleLSR 673
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774686 1784 EASRLRAISEEAKHQRQIAEEEAarqraeaeRILKEKLAAISEATRLKTEAEIALKEKEAENERLRR 1850
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTL--------EKLKEELEEREKAKKELEKLEKALERVEELREKVKK 732
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2424-2588 |
5.66e-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: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2424 AIADLENEKARLKKEAEELQNKSKEmADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLEsQFEEEVKKAKAL 2503
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEE-LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2504 KDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHT 2583
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
....*
gi 1988774686 2584 RETDK 2588
Cdd:COG1196 391 ALRAA 395
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2179-2553 |
5.79e-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: 69.33 E-value: 5.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2179 DEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKiEEENQRLIKKDKDSTQKLLAEEAENMRKLAE--DAARL 2256
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK-AERYQALLKEKREYEGYELLKEKEALERQKEaiERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2257 SVEAQEAARLRQIaeDDLNQQRALAEKMLKEKMQAIQEasrlKAEAEMLQKQKDLA-----QEQAQKLLEDKQLMQQRLE 2331
Cdd:TIGR02169 248 SLEEELEKLTEEI--SELEKRLEEIEQLLEELNKKIKD----LGEEEQLRVKEKIGeleaeIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2332 EETEEYhkslEVERKRQLEimaEAERLRLQVSQLseaqaraeeeakkfKKQADKVATRLHETEiatQEKMTVVERLEFEr 2411
Cdd:TIGR02169 322 ERLAKL----EAEIDKLLA---EIEELEREIEEE--------------RKRRDKLTEEYAELK---EELEDLRAELEEV- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2412 lntSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEhektvlqqtfmtEKEMLLKKEKLIEDEKKRLES 2491
Cdd:TIGR02169 377 ---DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE------------ELADLNAAIAGIEAKINELEE 441
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 2492 QFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMdaalSKQKEAEEEMLRKQKEMQELERQR 2553
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK----EEYDRVEKELSKLQRELAEAEAQA 499
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1672-1893 |
5.87e-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: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1672 AEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQ 1751
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1752 lktkAEKETMSNTEKSKQLLEAEaakmkDLAEEASRLRAISEEAKHQRQI------AEEEAARQRAEAERILKEKLAAIS 1825
Cdd:COG3883 94 ----ALYRSGGSVSYLDVLLGSE-----SFSDFLDRLSALSKIADADADLleelkaDKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774686 1826 EATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKA 1893
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1493-1896 |
5.97e-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: 5.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1493 RQAEEE---LKRKSEAEKE-AAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAeLQSKHMSFA 1568
Cdd:COG3096 275 RHANERrelSERALELRRElFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1569 EKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWrQKANEALRLR-------LQAEDEAhkKTLAQ 1641
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADY-QQALDVQQTRaiqyqqaVQALEKA--RALCG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1642 EEAEKQKEEAEREAKKRAKAEES-----ALKQK----EMA----EEELERQRKIA-ESTAQQKLTAEQELIRLRADFDNA 1707
Cdd:COG3096 431 LPDLTPENAEDYLAAFRAKEQQAteevlELEQKlsvaDAArrqfEKAYELVCKIAgEVERSQAWQTARELLRRYRSQQAL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1708 EQQRSLLEDELYRLKNEVAAAQQQRKQLEdELAKvrsemdiliqlktKAEKETMSNTEKSKQLLEAEAaKMKDLAEEASR 1787
Cdd:COG3096 511 AQRLQQLRAQLAELEQRLRQQQNAERLLE-EFCQ-------------RIGQQLDAAEELEELLAELEA-QLEELEEQAAE 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1788 LRAISEEAKHQRqiaeEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAyQRKALEDQAS 1867
Cdd:COG3096 576 AVEQRSELRQQL----EQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERER-EATVERDELA 650
|
410 420
....*....|....*....|....*....
gi 1988774686 1868 QHKQEIEEKIVQLKKSSEAEMERQKAIVD 1896
Cdd:COG3096 651 ARKQALESQIERLSQPGGAEDPRLLALAE 679
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3113-3151 |
6.06e-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: 6.06e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1988774686 3113 LLDAQMTTGGIIDPVKSHRIPHDVACKRNYFDDEMKQAL 3151
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3444-3482 |
6.24e-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: 6.24e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1988774686 3444 LLEAQIVSGGIIDPVKSHRVPTDVAYQKNILSRDIAKTL 3482
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1105-1598 |
7.79e-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: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1105 KEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQREL 1184
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1185 EQLGRQLGYYRESY-DWLIRWIADAKQRQEKIQAvpitdsktLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKD 1263
Cdd:COG1196 361 AEAEEALLEAEAELaEAEEELEELAEELLEALRA--------AAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1264 YELQLVAYKAQVEplvsplkktKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKK 1343
Cdd:COG1196 433 LEEEEEEEEEALE---------EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1344 MAEMQAELDKQKQLA---------------EAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQ--KTNIQLELQE 1406
Cdd:COG1196 504 EGFLEGVKAALLLAGlrglagavavligveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgrATFLPLDKIR 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1407 LKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEK-----QKYTAESELKQLRDRAAEAEKLRKLAQDEAEKL 1481
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRtlvaaRLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1482 RKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQ 1561
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
490 500 510
....*....|....*....|....*....|....*..
gi 1988774686 1562 SKHMSFAEKTSKLEESLKQEhgavlQLQQEAERLKKQ 1598
Cdd:COG1196 744 EEELLEEEALEELPEPPDLE-----ELERELERLERE 775
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2154-2579 |
8.47e-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: 68.71 E-value: 8.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2154 KFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEE-LFKVKVQMEELLKLKNKIEEENQR---LIK 2229
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERlkaLTG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2230 KDKDSTQKLLAEEA----ENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQ-RALAEKMLKEKMQAIQEASRLKAEAEM 2304
Cdd:pfam12128 369 KHQDVTAKYNRRRSkikeQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeSELREQLEAGKLEFNEEEYRLKSRLGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2305 LQKQKDLAQeqaqklLEDKQLMQQRLEEEteeyhkslEVERKRQLEIMAEAERLRLQvsqlseaqaraeEEAKKFKKQAD 2384
Cdd:pfam12128 449 LKLRLNQAT------ATPELLLQLENFDE--------RIERAREEQEAANAEVERLQ------------SELRQARKRRD 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2385 KVATRLHETEIATQEKMTVVERLEFERLNTSKEADD-LRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHE--- 2460
Cdd:pfam12128 503 QASEALRQASRRLEERQSALDELELQLFPQAGTLLHfLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNlyg 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2461 -KTVLQQTFMTEKEMLlkkekliEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEM 2539
Cdd:pfam12128 583 vKLDLKRIDVPEWAAS-------EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDL 655
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1988774686 2540 LRKQKEMQELERQRleqERILAEENQKLREKLQQLEDAQK 2579
Cdd:pfam12128 656 RRLFDEKQSEKDKK---NKALAERKDSANERLNSLEAQLK 692
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1453-1690 |
9.63e-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: 67.10 E-value: 9.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1453 AESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVseetqkkRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAER 1532
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1533 QVKQAEIEKEKQIKVAHEAAQKSAAAELQSkhmsfAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKE 1612
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1613 LEKWRQ--KANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK 1690
Cdd:COG4942 173 RAELEAllAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1501-1914 |
1.00e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1501 RKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQ 1580
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1581 EHGAVLQLQQEAERLKKQQEDaensREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAK 1660
Cdd:COG4717 144 LPERLEELEERLEELRELEEE----LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1661 AE----ESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQR---------SLLEDELYRLKNEVAA 1727
Cdd:COG4717 220 EEleelEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1728 AQQQRKQLEDELAKVRSEMDILIQLKtkaeKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAE---- 1803
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELL----AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaal 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1804 --------EEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAEN--ERLRRQAEDEAYQRKALEDQASQHKQEI 1873
Cdd:COG4717 376 laeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1988774686 1874 EEKIVQLKK-SSEAEMERQKAIVDDTLKQRRVVEEEIRILKL 1914
Cdd:COG4717 456 AELEAELEQlEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
143-238 |
1.01e-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: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 143 KEKLLLWSQRMtdgYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLI-NMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPE 221
Cdd:cd21229 5 KKLMLAWLQAV---LPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1988774686 222 DVDVPHPDEKSIITYVS 238
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
14-122 |
1.05e-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: 61.83 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 14 LKDERDRVQ--KKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLP----REKGRMRFHKLQNVQIALDF 87
Cdd:cd21222 7 FDEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALEL 86
|
90 100 110
....*....|....*....|....*....|....*
gi 1988774686 88 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21222 87 MEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3939-3977 |
1.16e-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: 1.16e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1988774686 3939 LLESQAATGYVIDPIKNLKLTVNEAVKMGIVGPEFKDKL 3977
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1333-1793 |
1.16e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 68.31 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1333 AEKLKAEERKKMAEMQAEldKQKQLAEAHAKA---IAKAEKEAQE-------LKLKMQEEVSK-REIAAVDAEKQKTNIQ 1401
Cdd:NF041483 737 SEELLASARKRVEEAQAE--AQRLVEEADRRAtelVSAAEQTAQQvrdsvagLQEQAEEEIAGlRSAAEHAAERTRTEAQ 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1402 LELQELKNlseqqikDKSQQVDEALHSRTKIEEEIRliriqlETTEKQKYTAEselKQLRDRAAEAEKLRKLAQDEAEKL 1481
Cdd:NF041483 815 EEADRVRS-------DAYAERERASEDANRLRREAQ------EETEAAKALAE---RTVSEAIAEAERLRSDASEYAQRV 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1482 RKQVSEetqkkrqaeeelkRKSEAEKEAAKQKQKALEDLEKLRMQA------------EEAERQVKQAEIEKEKQIKVAH 1549
Cdd:NF041483 879 RTEASD-------------TLASAEQDAARTRADAREDANRIRSDAaaqadrligeatSEAERLTAEARAEAERLRDEAR 945
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1550 EAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKqqeDAENSREEAEKELEKWRQKA-NEALRLRL 1628
Cdd:NF041483 946 AEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRT---EAERVKAEAAAEAERLRTEArEEADRTLD 1022
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1629 QAEDEAHKK-TLAQEEAEKQKEEAEREAKK-RAKAEESALKQKEMAEEEL---------ERQRKIAESTAQ--------- 1688
Cdd:NF041483 1023 EARKDANKRrSEAAEQADTLITEAAAEADQlTAKAQEEALRTTTEAEAQAdtmvgaarkEAERIVAEATVEgnslvekar 1102
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1689 -------------------------QKLTAEQELIRLRADFDNAEQQRSLLEdelyRLKNEVAAAQQQRKQLE------- 1736
Cdd:NF041483 1103 tdadellvgarrdataireraeelrDRITGEIEELHERARRESAEQMKSAGE----RCDALVKAAEEQLAEAEakakelv 1178
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1737 ----DELAKVR----SEMDILI---------------QLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISE 1793
Cdd:NF041483 1179 sdanSEASKVRiaavKKAEGLLkeaeqkkaelvreaeKIKAEAEAEAKRTVEEGKRELDVLVRRREDINAEISRVQDVLE 1258
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4287-4324 |
1.20e-10 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 59.03 E-value: 1.20e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1988774686 4287 QRLLEAQACTGGIIDPTSGEKYSIAEATEKGLVDKIMV 4324
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1323-1544 |
1.82e-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: 67.46 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1323 QRRLDDEEKAAEKLKAEERKK------MAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL----KLKMQEEVSKREIAAVD 1392
Cdd:pfam17380 340 ERMAMERERELERIRQEERKRelerirQEEIAMEISRMRELERLQMERQQKNERVRQELeaarKVKILEEERQRKIQQQK 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1393 AEKQKTNIQLE---LQELKNLSEQQIKDKSQQVDEALHSRTKIE------EEIRLIRIQLETTEKQKYTAESELKQLRDR 1463
Cdd:pfam17380 420 VEMEQIRAEQEearQREVRRLEEERAREMERVRLEEQERQQQVErlrqqeEERKRKKLELEKEKRDRKRAEEQRRKILEK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1464 AAEAeklRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQ------------KALEdlEKLRMQAEEAE 1531
Cdd:pfam17380 500 ELEE---RKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEmeerrriqeqmrKATE--ERSRLEAMERE 574
|
250
....*....|...
gi 1988774686 1532 RQVKQAEIEKEKQ 1544
Cdd:pfam17380 575 REMMRQIVESEKA 587
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1329-1562 |
1.83e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 66.37 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1329 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEahakaiakaekeAQELKlkmqeevskreiaavdaekqktniQLELQELK 1408
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAE------------QERLK------------------------QLEKERLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1409 nlSEQQIKDKSQQVDEALHSRTKIEEEirliriQLETTEKQKYTAESELKQLRDRAAEAE-KLRKLAQDEAEklrKQVSE 1487
Cdd:PRK09510 113 --AQEQKKQAEEAAKQAALKQKQAEEA------AAKAAAAAKAKAEAEAKRAAAAAKKAAaEAKKKAEAEAA---KKAAA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774686 1488 ETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQS 1562
Cdd:PRK09510 182 EAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2314-2604 |
2.15e-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: 67.39 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2314 EQAQKLLEDKQLMQQRLE---EETEEYHKSLEVERK---RQLEIMAEAERLRLQVSQLSEAQARAEEeaKKFKKQADKVA 2387
Cdd:TIGR02168 175 KETERKLERTRENLDRLEdilNELERQLKSLERQAEkaeRYKELKAELRELELALLVLRLEELREEL--EELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2388 TRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKA-------IADLENEKARLKKEAEELQNKSKEMADAQQKKIEHe 2460
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESK- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2461 ktvlqqtfmteKEMLLKKEKLIEDEKKRLESQFEEEVKKAKalkdEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEML 2540
Cdd:TIGR02168 332 -----------LDELAEELAELEEKLEELKEELESLEAELE----ELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774686 2541 RKQKEMQELERQ--RLEQER-ILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDIIHLTTIETTK 2604
Cdd:TIGR02168 397 SLNNEIERLEARleRLEDRReRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
504-693 |
2.21e-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: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 504 LRYVQDLLAWVEENQRRIDNAEWGSDLPSMESQLGSHRGLHQTVEDFKSKIERAKADETQL---SPVSKGTYREYLGKLD 580
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 581 LQYGKLLNSSKSRLRNLE---SLHAFVSAATKELMWLNDKEEEEVNFDWSDRNTNMTAKKDNYSGLMRELELREKKVNDI 657
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1988774686 658 QALGDRLVRDGHPGK-KTVESFTAALQTQWSWILQLC 693
Cdd:cd00176 166 NELAEELLEEGHPDAdEEIEEKLEELNERWEELLELA 202
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1412-1611 |
2.89e-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: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1412 EQQIKDKSQQVDEAlhsRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKlaqdeAEKLRKQVSEetqk 1491
Cdd:TIGR02794 49 AQQANRIQQQKKPA---AKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEE---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1492 KRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAElqskhmsfAEKT 1571
Cdd:TIGR02794 117 KQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAE--------AEAK 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1988774686 1572 SKLEESLKQEHGAVLQLQQEAERlKKQQEDAENSREEAEK 1611
Cdd:TIGR02794 189 AKAEEAKAKAEAAKAKAAAEAAA-KAEAEAAAAAAAEAER 227
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1814-2581 |
3.35e-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: 66.68 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1814 ERILKEKLAAISEATRLKTEAEiALKEKEAENER-----LRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEaEM 1888
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLNESN-ELHEKQKFYLRqsvidLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH-EL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1889 ERQKAIVDDTLKQ--------RRV------VEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAE-- 1952
Cdd:pfam15921 155 EAAKCLKEDMLEDsntqieqlRKMmlshegVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEis 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1953 --KLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALE---ELERLRKKAEEARKQKDEADKEAEkqiVVAQQAAQK 2027
Cdd:pfam15921 235 ylKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEhevEITGLTEKASSARSQANSIQSQLE---IIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2028 CSAAEQQVQsvlaqQIEDSITQkkLKEEYEKAKKlakeaeaakekaereaaLLRQQAEEAERQKTAAeeeaanqakaqeD 2107
Cdd:pfam15921 312 NSMYMRQLS-----DLESTVSQ--LRSELREAKR-----------------MYEDKIEELEKQLVLA------------N 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2108 AERLRKEAEFEAAKRAQAEAAALMQKQQADTemakHKKLAEQTLkqkfqvEQELTKvklKLDETDKQKSVLDEELQRlkd 2187
Cdd:pfam15921 356 SELTEARTERDQFSQESGNLDDQLQKLLADL----HKREKELSL------EKEQNK---RLWDRDTGNSITIDHLRR--- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2188 EVDDAVKQRGQVEEELFKVKV----QMEELLKlknKIEEENQRLIKKDKDSTQklLAEEAENMRKLAED--AARLSVEAQ 2261
Cdd:pfam15921 420 ELDDRNMEVQRLEALLKAMKSecqgQMERQMA---AIQGKNESLEKVSSLTAQ--LESTKEMLRKVVEEltAKKMTLESS 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2262 EaarlRQIAedDLNQQralaekmLKEKMQAIQEASrlkAEAEMLQKQKDLAQEQAQKL------LEDKQLMQQRLEEETE 2335
Cdd:pfam15921 495 E----RTVS--DLTAS-------LQEKERAIEATN---AEITKLRSRVDLKLQELQHLknegdhLRNVQTECEALKLQMA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2336 EYHKSLEVERKrQLEIMAE--------AERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQ----EKMTV 2403
Cdd:pfam15921 559 EKDKVIEILRQ-QIENMTQlvgqhgrtAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSdlelEKVKL 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2404 V----ERLEFERlNTSKEADDLRKAIADLENEKARLKKEAEELQ----NKSKEMADAQQK---KIEHEKTVLQQTFMTEK 2472
Cdd:pfam15921 638 VnagsERLRAVK-DIKQERDQLLNEVKTSRNELNSLSEDYEVLKrnfrNKSEEMETTTNKlkmQLKSAQSELEQTRNTLK 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2473 EM----------LLKKEKLIEDEKKRLES-----QFEEEV-----KKAKALKDEQERQKQQME---QEKKTLQATMDAAL 2529
Cdd:pfam15921 717 SMegsdghamkvAMGMQKQITAKRGQIDAlqskiQFLEEAmtnanKEKHFLKEEKNKLSQELStvaTEKNKMAGELEVLR 796
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 2530 SKQKEAEEEMLRKQKEMQELERQRLE-QERILAEENQKLREKLQQLEDAQKDQ 2581
Cdd:pfam15921 797 SQERRLKEKVANMEVALDKASLQFAEcQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1743-2464 |
3.37e-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: 66.79 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1743 RSEMDILIQLKTKAEKETMSNTEKSKQLL---EAEAAKMKDLAEEAS-------RLRAISEEAK-HQRQIAEEEAARQRA 1811
Cdd:pfam12128 205 ILEDDGVVPPKSRLNRQQVEHWIRDIQAIagiMKIRPEFTKLQQEFNtlesaelRLSHLHFGYKsDETLIASRQEERQET 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1812 EAEriLKEKLAA--------ISEATRLKTEAEIALKEKEAENERLRRQA----EDEAYQRKALEDQASQHKQEIEEKIVQ 1879
Cdd:pfam12128 285 SAE--LNQLLRTlddqwkekRDELNGELSAADAAVAKDRSELEALEDQHgaflDADIETAAADQEQLPSWQSELENLEER 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1880 LK------KSSEAEMERQKAIVDDTLKqrRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEK 1953
Cdd:pfam12128 363 LKaltgkhQDVTAKYNRRRSKIKEQNN--RDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEY 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1954 LRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKqivvAQQAAQKCSAAEQ 2033
Cdd:pfam12128 441 RLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQ----ASEALRQASRRLE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2034 QVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEaakekaereaalLRQQAEEAERQKTAAEEEAANQAKAQE------- 2106
Cdd:pfam12128 517 ERQSALDELELQLFPQAGTLLHFLRKEAPDWEQS------------IGKVISPELLHRTDLDPEVWDGSVGGElnlygvk 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2107 -DAERLRKEAEFEAAKRAQAEAAALmqKQQADTEMAKHKKLAEQTLKQKFQVEQ---ELTKVKLKLDETDKQKSVLDEEL 2182
Cdd:pfam12128 585 lDLKRIDVPEWAASEEELRERLDKA--EEALQSAREKQAAAEEQLVQANGELEKasrEETFARTALKNARLDLRRLFDEK 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2183 QRLKDEVDDAVKQR-GQVEEELFKVKVQMEELL-KLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAE-DAARLSVE 2259
Cdd:pfam12128 663 QSEKDKKNKALAERkDSANERLNSLEAQLKQLDkKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALlKAAIAARR 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2260 AQEAARLRQIAEDdlnQQRALAEKMLKEkmqaiQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHK 2339
Cdd:pfam12128 743 SGAKAELKALETW---YKRDLASLGVDP-----DVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLAT 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2340 SLEverkrqlEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLheteiatQEKMTVVeRLEFERLNTSKEAD 2419
Cdd:pfam12128 815 QLS-------NIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRL-------SENLRGL-RCEMSKLATLKEDA 879
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1988774686 2420 DlrkaIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVL 2464
Cdd:pfam12128 880 N----SEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVI 920
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1494-1897 |
4.27e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.52 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1494 QAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVkQAEIEKEKQIKVAHEAA----QKSAAAELQSKHM---- 1565
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMAREL-AELNEAESDLEQDYQAAsdhlNLVQTALRQQEKIeryq 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1566 -SFAEKTSKLEESLkqehgAVLQLQQEaerlkkQQEDAENSREEAEKELEKWR------QKANEALRLR-------LQAE 1631
Cdd:PRK04863 355 aDLEELEERLEEQN-----EVVEEADE------QQEENEARAEAAEEEVDELKsqladyQQALDVQQTRaiqyqqaVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1632 DEAhkKTLAQEEAEKQKEEAEREAKKRAKAEESALkqkemAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQ- 1710
Cdd:PRK04863 424 ERA--KQLCGLPDLTADNAEDWLEEFQAKEQEATE-----ELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWd 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1711 --RSLLED--ELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKeTMSNTEKSKQLLEAEAAKMKDLAEEAS 1786
Cdd:PRK04863 497 vaRELLRRlrEQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGK-NLDDEDELEQLQEELEARLESLSESVS 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1787 RLRAISEEAKHQRqiaeEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAlEDQA 1866
Cdd:PRK04863 576 EARERRMALRQQL----EQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVE-RDEL 650
|
410 420 430
....*....|....*....|....*....|.
gi 1988774686 1867 SQHKQEIEEKIVQLKKSSEAEMERQKAIVDD 1897
Cdd:PRK04863 651 AARKQALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1493-2006 |
5.93e-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: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1493 RQAEEELKRKSEAEKEA--AKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKqikVAHEAAQKsAAAELQskhmsfaek 1570
Cdd:COG4913 228 DALVEHFDDLERAHEALedAREQIELLEPIRELAERYAAARERLAELEYLRAA---LRLWFAQR-RLELLE--------- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1571 tsKLEESLKQEHGavlQLQQEAERLKKQQEDAENSREEAEkelEKWRQKANEALRlRLQAEDEAHKKTLaqeeaekqkee 1650
Cdd:COG4913 295 --AELEELRAELA---RLEAELERLEARLDALREELDELE---AQIRGNGGDRLE-QLEREIERLEREL----------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1651 aeREAKKRAKAEESALKQKEMA----EEELERQRKIAESTAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVA 1726
Cdd:COG4913 355 --EERERRRARLEALLAALGLPlpasAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1727 AAQQQ-----------RKQLEDELAKVRSEMDI---LIQLKTKAEKETMS--------------------------NTEK 1766
Cdd:COG4913 430 SLERRksniparllalRDALAEALGLDEAELPFvgeLIEVRPEEERWRGAiervlggfaltllvppehyaaalrwvNRLH 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1767 SKQLLEAEAAKMKDLAEEASRL-------------------------------------------RAISEE--AKH---- 1797
Cdd:COG4913 510 LRGRLVYERVRTGLPDPERPRLdpdslagkldfkphpfrawleaelgrrfdyvcvdspeelrrhpRAITRAgqVKGngtr 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1798 -----QRQIAEE-----EAARQRAEAERILKEKLAAISEATRLKTEaeiaLKEKEAENERLRRQAEDEAYQRKALEDQAS 1867
Cdd:COG4913 590 hekddRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1868 QHKQ--EIEEKIVQLKKSS------EAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEkassgklDLELELNKLKNIADE 1939
Cdd:COG4913 666 AEREiaELEAELERLDASSddlaalEEQLEELEAELEELEEELDELKGEIGRLEKELE-------QAEEELDELQDRLEA 738
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774686 1940 tqqskirAEEEAEKLRKLALEEEKRRREAEEKVKKIaaaEEEAARQRKAALEELERLRKKAEEARKQ 2006
Cdd:COG4913 739 -------AEDLARLELRALLEERFAAALGDAVEREL---RENLEERIDALRARLNRAEEELERAMRA 795
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1390-1585 |
6.19e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.83 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1390 AVDAEKQKTNIQL----ELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRiqlettEKQKYTAESELKQLRDRAA 1465
Cdd:PRK09510 74 AKRAEEQRKKKEQqqaeELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAA------LKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1466 EAEKLRKLAQDEAeklrKQVSEETQKKRQAEEELKRKSEAEKEA-AKQKQKALEDLEKlrmqAEEAERQVKQAEIEKEKQ 1544
Cdd:PRK09510 148 KAEAEAKRAAAAA----KKAAAEAKKKAEAEAAKKAAAEAKKKAeAEAAAKAAAEAKK----KAEAEAKKKAAAEAKKKA 219
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1988774686 1545 IKVAHEAAQKsAAAELQSKHMSFAEKTSKLEESLKQEHGAV 1585
Cdd:PRK09510 220 AAEAKAAAAK-AAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1490-1696 |
6.82e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.44 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1490 QKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEE---AERQVKQAE----IEKEKQiKVAHEAAQKSAAAelqs 1562
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKErlaAQEQKKQAEeaakQAALKQ-KQAEEAAAKAAAA---- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1563 khmsfaektSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTlaqe 1642
Cdd:PRK09510 145 ---------AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKA---- 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1988774686 1643 eaekqkeeaEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQE 1696
Cdd:PRK09510 212 ---------AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2081-2361 |
8.38e-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: 65.14 E-value: 8.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2081 RQQAEEAERQKTAAEEEAANQAKaqEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKL----AEQTLKQKFQ 2156
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKA--REVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELerirQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2157 VEQELTKVKL-KLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRlikkdkdST 2235
Cdd:pfam17380 365 IRQEEIAMEIsRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR-------EV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2236 QKLLAEEAENMRKLAEDAARlsvEAQEAARLRQIAEDdlNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQ-KQKDLAQE 2314
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQE---RQQQVERLRQQEEE--RKRKKLELEKEKRDRKRAEEQRRKILEKELEErKQAMIEEE 512
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1988774686 2315 QAQKLLEDKQLMQQRLEEETEEYHKSlEVERKRQLEImaeAERLRLQ 2361
Cdd:pfam17380 513 RKRKLLEKEMEERQKAIYEEERRREA-EEERRKQQEM---EERRRIQ 555
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2182-2580 |
8.42e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2182 LQRLKDEVDDAVKQRGQ-----------VEEELFKVKVQMEELLKLKNKIEEENQRL---------IKKDKDSTQKLLA- 2240
Cdd:COG4717 48 LERLEKEADELFKPQGRkpelnlkelkeLEEELKEAEEKEEEYAELQEELEELEEELeeleaeleeLREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2241 -----EEAENMRKLAEDAARL-SVEAQEAARLRQIAE-DDLNQ-----QRALAEKMLKEKMQAIQEASRLKAEAEMLQKQ 2308
Cdd:COG4717 128 lplyqELEALEAELAELPERLeELEERLEELRELEEElEELEAelaelQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2309 KDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEE-------------- 2374
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvlglla 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2375 --------EAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKS 2446
Cdd:COG4717 288 llflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2447 KEmadaqqkkiEHEKTVLQQTFMTEKEMLLKKEKL------IEDEKKRLESQFEEEVKKAKALKDEQErqKQQMEQEKKT 2520
Cdd:COG4717 368 LE---------QEIAALLAEAGVEDEEELRAALEQaeeyqeLKEELEELEEQLEELLGELEELLEALD--EEELEEELEE 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 2521 LQAtmdaalsKQKEAEEEMLRKQKEMQELERQ--RLEQERILAEENQKLREKLQQLEDAQKD 2580
Cdd:COG4717 437 LEE-------ELEELEEELEELREELAELEAEleQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1725-2051 |
8.52e-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: 65.14 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1725 VAAAQQQRKQLEDELAKVRSEmdiliqlktkaEKETMSNTEKSKQLLEAEAAKMKDLAEEAS----RLRAISEEAKHQRQ 1800
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQE-----------KEEKAREVERRRKLEEAEKARQAEMDRQAAiyaeQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1801 IAEEEAARqraEAERILKEKLAAisEATRLKtEAEIALKEKEAENERLRRQAEdEAYQRKALEDQASQHKQEIEEKIVQL 1880
Cdd:pfam17380 353 IRQEERKR---ELERIRQEEIAM--EISRMR-ELERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1881 KKSSEAEMERQkaivddtlkQRRVVEEEIRilklnfekassgkldlELELNKLKNIADETQQSKIRAEEEAEKLRKLALE 1960
Cdd:pfam17380 426 RAEQEEARQRE---------VRRLEEERAR----------------EMERVRLEEQERQQQVERLRQQEEERKRKKLELE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1961 EEKRRREAEEKV-KKIAAAEEEAARQ------------------RKAALEELERLRKKAEEARKQKD-EADKEAEKQIVV 2020
Cdd:pfam17380 481 KEKRDRKRAEEQrRKILEKELEERKQamieeerkrkllekemeeRQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRK 560
|
330 340 350
....*....|....*....|....*....|.
gi 1988774686 2021 AQQAAQKCSAAEQQVQsvLAQQIEDSITQKK 2051
Cdd:pfam17380 561 ATEERSRLEAMERERE--MMRQIVESEKARA 589
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1104-1599 |
1.01e-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: 65.14 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1104 VKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVrvhSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRE 1183
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL---TEARTERDQFSQESGNLDDQLQKLLADLHKREKE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1184 --LEQLGRQLGYYRE-----SYDWLIRWIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKA 1256
Cdd:pfam15921 393 lsLEKEQNKRLWDRDtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLES 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1257 YIDTIKDYELQLVAYKAQVEP---LVSPLKKT--KLDSASDNIIQEYVTLRTRYsELMTLTSQYIKFITDTQRRLDDEEK 1331
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTLESserTVSDLTASlqEKERAIEATNAEITKLRSRV-DLKLQELQHLKNEGDHLRNVQTECE 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1332 AAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAI-------AKAEKEAQELKLKMQE---EVSKREIAAVDAEKQKTNIQ 1401
Cdd:pfam15921 552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAgamqvekAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARVSDLE 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1402 LELQELKNLSEQQ---IKDKSQQVDEALH----SRTKIE---EEIRLIRI-------QLETT----EKQKYTAESELKQL 1460
Cdd:pfam15921 632 LEKVKLVNAGSERlraVKDIKQERDQLLNevktSRNELNslsEDYEVLKRnfrnkseEMETTtnklKMQLKSAQSELEQT 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1461 RDRAAEAEKLRKLAQDEAEKLRKQVS------EETQKKRQAEEELKRKSEAEKEAAKQKQKALEdlEKLRMQAEEAERQV 1534
Cdd:pfam15921 712 RNTLKSMEGSDGHAMKVAMGMQKQITakrgqiDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS--QELSTVATEKNKMA 789
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774686 1535 KQAEIEKEKQIKVAHEAAQKSAAaeLQSKHMSFAEKTSKLEeslKQEhgavlqlqQEAERLKKQQ 1599
Cdd:pfam15921 790 GELEVLRSQERRLKEKVANMEVA--LDKASLQFAECQDIIQ---RQE--------QESVRLKLQH 841
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1412-1614 |
1.05e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.06 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1412 EQQIKDKSQQVDEALHSRTKIEEEIRLIriqlettEKQKYTAESELKQlrdrAAEAEKLRKLAQDEAEKLRKQVSEETQK 1491
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQL-------EKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1492 KrqAEEELKRKSEAEKEAAKQKQKaLEDLEKLRMQAEEAerqvkQAEIEKEKQIKVAHEAAQKsAAAELQSKHMSFAEKT 1571
Cdd:PRK09510 148 K--AEAEAKRAAAAAKKAAAEAKK-KAEAEAAKKAAAEA-----KKKAEAEAAAKAAAEAKKK-AEAEAKKKAAAEAKKK 218
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1988774686 1572 SKLEESLKQEHGAVlQLQQEAERLKKQQEDAENSREEAEKELE 1614
Cdd:PRK09510 219 AAAEAKAAAAKAAA-EAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1494-1751 |
1.43e-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: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1494 QAEEELKRKSEAEKEAAKQKQKALEDLEKlrmQAEEAERQvKQAEIEKEKQIKVAHEAAQKSAAAELQSKHmsfAEKTSK 1573
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQ---QAEEAEKQ-RAAEQARQKELEQRAAAEKAAKQAEQAAKQ---AEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1574 LEESLKQEHGAVLQLQQEAERLKKQQEDAENsreeaekelekwrqkanealrlrlQAEDEAHKKTLAQEEAEKQKEEAER 1653
Cdd:TIGR02794 120 QAEEAKAKQAAEAKAKAEAEAERKAKEEAAK------------------------QAEEEAKAKAAAEAKKKAEEAKKKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1654 EAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRK 1733
Cdd:TIGR02794 176 EAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGA 255
|
250
....*....|....*...
gi 1988774686 1734 QLEDELAKVRSEMDILIQ 1751
Cdd:TIGR02794 256 AAGSEVDKYAAIIQQAIQ 273
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1343-1684 |
1.53e-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: 63.01 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1343 KMAEMQAELDKQKqlaeAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLEL--QELKNLSEQQIKDKSQ 1420
Cdd:pfam13868 16 LAAKCNKERDAQI----AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyrQELEEQIEEREQKRQE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1421 QVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELK 1500
Cdd:pfam13868 92 EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1501 RKSEAEKEAAKQKqkaledlEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSkhmsfAEKTSKLEESLKQ 1580
Cdd:pfam13868 172 EAEREEIEEEKER-------EIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREE-----AEKKARQRQELQQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1581 EHgavlQLQQEAERLKKQQEdaensREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAK 1660
Cdd:pfam13868 240 AR----EEQIELKERRLAEE-----AEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAER 310
|
330 340 350
....*....|....*....|....*....|.
gi 1988774686 1661 AEESALKQKEMAEEEL-------ERQRKIAE 1684
Cdd:pfam13868 311 EEELEEGERLREEEAErrerieeERQKKLKE 341
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1095-1622 |
1.70e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1095 REVHTVPSDVKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKasavSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVF 1174
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE----LEERIEELKKEIEELEEKVKELKELKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1175 TQIDLRQRELEQLGR---QLGYYRESYDWLIRWIADAKQRQEKIqavpitdsktlkeqlaqeKKLLEEIEQNKDKVDECQ 1251
Cdd:PRK03918 297 KLSEFYEEYLDELREiekRLSRLEEEINGIEERIKELEEKEERL------------------EELKKKLKELEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1252 KYAKAYiDTIKDYELQLVAYKAQVEPLvsplkktkldsASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEK 1331
Cdd:PRK03918 359 ERHELY-EEAKAKKEELERLKKRLTGL-----------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1332 AAEKLKAEERK-KMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQE-EVSKREIAAVDAEKQKTNIQLEL-QELK 1408
Cdd:PRK03918 427 AIEELKKAKGKcPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKlRKELRELEKVLKKESELIKLKELaEQLK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1409 NLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTE---KQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQV 1485
Cdd:PRK03918 507 ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1486 SEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAER--QVKQAEIEK-EKQIKVAHEAAQKSAAAELQS 1562
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEelAETEKRLEElRKELEELEKKYSEEEYEELRE 666
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1563 KHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKeLEKWRQKANE 1622
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEE 725
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1457-1876 |
1.78e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1457 LKQLRDRAAEAEKLR----KLAQDEAEKLRKQVSEETQKK---RQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEE 1529
Cdd:COG4717 48 LERLEKEADELFKPQgrkpELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1530 AERQVKQAEIEKEKQIK-------VAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQ----EHGAVLQLQQEAERLKKQ 1598
Cdd:COG4717 128 LPLYQELEALEAELAELperleelEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1599 QEDAENSREEAEKELEkwrQKANEALRLRLQAEDEAHKKTLAQEEAEKQ------------------------------- 1647
Cdd:COG4717 208 LAELEEELEEAQEELE---ELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1648 --KEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLED-ELYRLKNE 1724
Cdd:COG4717 285 llALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1725 VAAAQQQRKQLEDElAKVRSEMDILIQLKTKAEKEtmsntEKSKQLLEAEAAkMKDLAEEASRLRAISEEAKHQRQIAEE 1804
Cdd:COG4717 365 LEELEQEIAALLAE-AGVEDEEELRAALEQAEEYQ-----ELKEELEELEEQ-LEELLGELEELLEALDEEELEEELEEL 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774686 1805 EAARQRAEAERI-LKEKLAAISEATR-LKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQA-SQHKQEIEEK 1876
Cdd:COG4717 438 EEELEELEEELEeLREELAELEAELEqLEEDGELAELLQELEELKAELRELAEEWAALKLALELlEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2145-2364 |
2.13e-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: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2145 KLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELfkvKVQMEELLKLKNKIEEEN 2224
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2225 QRLiKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAAR----LRQIAEDDLNQQRALAEKmLKEKMQAIQEASRLKA 2300
Cdd:COG4942 97 AEL-EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRrlqyLKYLAPARREQAEELRAD-LAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774686 2301 EAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQ 2364
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1295-1751 |
2.43e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.21 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1295 IQEYVTLRTRYSELMTLTSQYIKF----ITDTQRRLDDEEKAAEKLKAEERKKMA-------EMQAELDKQK-------- 1355
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYVAAdymrHANERRVHLEEALELRRELYTSRRQLAaeqyrlvEMARELAELNeaesdleq 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1356 ------------QLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAvdaekqktNIQLELQELKNLSEQQIKD-KSQQV 1422
Cdd:PRK04863 329 dyqaasdhlnlvQTALRQQEKIERYQADLEELEERLEEQNEVVEEAD--------EQQEENEARAEAAEEEVDElKSQLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1423 D--EALhsrtkIEEEIRLIRIQletTEKQKYTAESELKQLRDRAAEAeklrklAQDEAEKLRKQVSEETQKKRQAEEELk 1500
Cdd:PRK04863 401 DyqQAL-----DVQQTRAIQYQ---QAVQALERAKQLCGLPDLTADN------AEDWLEEFQAKEQEATEELLSLEQKL- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1501 rkSEAEkEAAKQKQKALEDLEKL--RMQAEEAERQVKQAEIEKEKQikvAHEAAQKSAaaeLQSKHmsfaektSKLEESL 1578
Cdd:PRK04863 466 --SVAQ-AAHSQFEQAYQLVRKIagEVSRSEAWDVARELLRRLREQ---RHLAEQLQQ---LRMRL-------SELEQRL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1579 KQehgavlqlQQEAERLKKQQEDAENSREEAEKELekwrqkanEALRLRLQAEDEAHKktlaqeeaekqkeeaerEAKKR 1658
Cdd:PRK04863 530 RQ--------QQRAERLLAEFCKRLGKNLDDEDEL--------EQLQEELEARLESLS-----------------ESVSE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1659 AKAEESALKQKemaEEELERQRKIAESTAQQKLTAEQELIRLR----ADFDNAEQQRSLLEDELYRLKnevaAAQQQRKQ 1734
Cdd:PRK04863 577 ARERRMALRQQ---LEQLQARIQRLAARAPAWLAAQDALARLReqsgEEFEDSQDVTEYMQQLLERER----ELTVERDE 649
|
490
....*....|....*..
gi 1988774686 1735 LEDELAKVRSEMDILIQ 1751
Cdd:PRK04863 650 LAARKQALDEEIERLSQ 666
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
23-119 |
2.71e-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: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 23 KKTFTKWVN---------KHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDFL 88
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1988774686 89 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 119
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2416-2586 |
3.15e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2416 KEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEE 2495
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2496 EVKKAKALKdEQERQKQQMEQEKKTLQATMDAAL-SKQKEAEEEMLRKQKEMQELERQRLEQERILA---EENQKLREKL 2571
Cdd:COG4717 151 LEERLEELR-ELEEELEELEAELAELQEELEELLeQLSLATEEELQDLAEELEELQQRLAELEEELEeaqEELEELEEEL 229
|
170
....*....|....*
gi 1988774686 2572 QQLEDAQKDQHTRET 2586
Cdd:COG4717 230 EQLENELEAAALEER 244
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1354-1561 |
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 1988774686 1354 QKQLAEAHAKAIAKAEKEAqelKLKMQEEVSKREIAAVDAEKQKtniQLELQELKNLSEQQIKDKSqqvdealhsrTKIE 1433
Cdd:TIGR02794 44 DPGAVAQQANRIQQQKKPA---AKKEQERQKKLEQQAEEAEKQR---AAEQARQKELEQRAAAEKA----------AKQA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1434 EEIRLiriqlETTEKQKYTAESELKQLRDRAAEAEKLRKlaQDEAEKLRKQVSEETQKKRQAE-----EELKRKSEAEKE 1508
Cdd:TIGR02794 108 EQAAK-----QAEEKQKQAEEAKAKQAAEAKAKAEAEAE--RKAKEEAAKQAEEEAKAKAAAEakkkaEEAKKKAEAEAK 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774686 1509 A---AKQKQKALEDLEKLRMQAEEAERQVKqAEIEKEKQIKVAHEAAQKSAAAELQ 1561
Cdd:TIGR02794 181 AkaeAEAKAKAEEAKAKAEAAKAKAAAEAA-AKAEAEAAAAAAAEAERKADEAELG 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
976-1550 |
4.06e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 976 LRIEDCE--AGTVARIRKPV--EKEPLKEYIQKTTEQKKVQGELdglKKDLDKVSVKTQEVlaspqpSASAPVLRSELDl 1051
Cdd:PRK03918 155 LGLDDYEnaYKNLGEVIKEIkrRIERLEKFIKRTENIEELIKEK---EKELEEVLREINEI------SSELPELREELE- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1052 tvqkmdhahMLSSVYLEKLKTVEMVirntqgaEGVLKQYEDCLREVHTVPSDVKEVETYRAKLKKMRTEAEDEQPVFDSL 1131
Cdd:PRK03918 225 ---------KLEKEVKELEELKEEI-------EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1132 EEELKKASAVS---DKMVRVHSERDVELDHFRQQLSSLQDRWKavftqidlrqrELEQLGRQLGYYRESYDWLIRWIADA 1208
Cdd:PRK03918 289 KEKAEEYIKLSefyEEYLDELREIEKRLSRLEEEINGIEERIK-----------ELEEKEERLEELKKKLKELEKRLEEL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1209 KQRQEKIQavpitDSKTLKEQLAQEKKLLEEIEqnKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKKT--K 1286
Cdd:PRK03918 358 EERHELYE-----EAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1287 LDSASDNII--------QEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEER-----KKMAEMQAELdk 1353
Cdd:PRK03918 431 LKKAKGKCPvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklKELAEQLKEL-- 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1354 QKQLAEAHAKAIAKAEKEAQELK-----LKMQEEVSKREIAAVDA-EKQKTNIQLELQELKN-LSE--QQIKDKSQQVDE 1424
Cdd:PRK03918 509 EEKLKKYNLEELEKKAEEYEKLKeklikLKGEIKSLKKELEKLEElKKKLAELEKKLDELEEeLAEllKELEELGFESVE 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1425 ALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEetQKKRQAEEELKRKSE 1504
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE--LEKKYSEEEYEELRE 666
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1988774686 1505 AEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHE 1550
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1771-2581 |
4.40e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1771 LEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEaaRQRAEAERILKEKLAAIsEATRLKTEAEIALKEK---EAENER 1847
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREY-EGYELLKEKEALERQKeaiERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1848 LRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLE 1927
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1928 LELNKLKniaDETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRkaalEELERLRKKAEEARKQK 2007
Cdd:TIGR02169 329 AEIDKLL---AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR----DELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2008 DEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEyekakklakeaeaakekaereaalLRQQAEEA 2087
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE------------------------IKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2088 ERQKTAAEEEAANQAKAQEDAERLRKEaefeaakraqaeaaaLMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLK 2167
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKE---------------LSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2168 LDETDKQKSVLDEELQ---------RLKDEV--DDAVKQRGQveEELFKVKVQMEELLKLkNKIEEENQRLIKKDKDSTQ 2236
Cdd:TIGR02169 523 VHGTVAQLGSVGERYAtaievaagnRLNNVVveDDAVAKEAI--ELLKRRKAGRATFLPL-NKMRDERRDLSILSEDGVI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2237 KLLAEEAENMRKLAEDAA-----RLSVEAQEAA-------RLRQIAEDDLNQQRALAEKMLKEKmQAIQEASRLKAEAEM 2304
Cdd:TIGR02169 600 GFAVDLVEFDPKYEPAFKyvfgdTLVVEDIEAArrlmgkyRMVTLEGELFEKSGAMTGGSRAPR-GGILFSRSEPAELQR 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2305 LQKQKdlaqEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLrlqvsqlseaqaraeeeakkfKKQAD 2384
Cdd:TIGR02169 679 LRERL----EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL---------------------EQEEE 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2385 KVATRLheteiatQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQnksKEMADAQQKKIEHEKTVL 2464
Cdd:TIGR02169 734 KLKERL-------EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHSRIPEIQAELSKL 803
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2465 qqtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVkkAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQK 2544
Cdd:TIGR02169 804 ------EEEVSRIEARLREIEQKLNRLTLEKEY--LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
810 820 830
....*....|....*....|....*....|....*..
gi 1988774686 2545 EMQELERQRLEqeriLAEENQKLREKLQQLEDAQKDQ 2581
Cdd:TIGR02169 876 ALRDLESRLGD----LKKERDELEAQLRELERKIEEL 908
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1088-1615 |
4.45e-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: 63.06 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1088 KQYEDCLREVHTVPSDVKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQ 1167
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1168 -------------DRWKAVFTQIDLRQRELEQLGRQLGYYRESYDWLIRWIAD--AKQRQEKIQAVPITD---SKTLKEQ 1229
Cdd:TIGR00618 380 hihtlqqqkttltQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQqeLQQRYAELCAAAITCtaqCEKLEKI 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1230 LAQE--KKLLEEIEQNKDKVDECQKYAKayIDTIKDYELQLVA-------------YKAQVEPLVSPLKKTKLDSASDNI 1294
Cdd:TIGR00618 460 HLQEsaQSLKEREQQLQTKEQIHLQETR--KKAVVLARLLELQeepcplcgscihpNPARQDIDNPGPLTRRMQRGEQTY 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1295 IQEYVTLRTRYSELMTLTSQyIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQE 1374
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHA 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1375 LKLKMQEEVSKREIAAVDAEKQKTNIQLEL---QELKNLSEQQIKDKSqqvdealhSRTKIEEEIRLIRIQLETTEkqky 1451
Cdd:TIGR00618 617 LLRKLQPEQDLQDVRLHLQQCSQELALKLTalhALQLTLTQERVREHA--------LSIRVLPKELLASRQLALQK---- 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1452 tAESELKQLRDRAAEAEKLRKLAQDEAEKLrKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAE 1531
Cdd:TIGR00618 685 -MQSEKEQLTYWKEMLAQCQTLLRELETHI-EEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1532 RQVKQAEI-------EKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAEN 1604
Cdd:TIGR00618 763 HFNNNEEVtaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSA 842
|
570
....*....|.
gi 1988774686 1605 SREEAEKELEK 1615
Cdd:TIGR00618 843 TLGEITHQLLK 853
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4365-4403 |
5.18e-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: 5.18e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1988774686 4365 FLEVQYLTGGLIEPDVEGRVSIDESIRKGTIDARTAQKL 4403
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2353-2566 |
5.38e-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: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2353 AEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIAtqekmtvVERLEFERLNTSKEADDLRKAIADLENEK 2432
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR-------IAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2433 ARLKKEAEELQNKSKEMADAQQKKIEHEKTVL----------------QQTFMTEKEMLLKKEKLIEDEKKRLESQFEEE 2496
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2497 VKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQK 2566
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
136-238 |
7.16e-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: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 136 QSEDMTAKEKLLLWSQ-RMTDgyqgIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLG 213
Cdd:cd21315 11 DGKGPTPKQRLLGWIQsKVPD----LPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDaVKNAKEAMDLAEDWLD 86
|
90 100
....*....|....*....|....*
gi 1988774686 214 VTRLLDPEDVDVPHPDEKSIITYVS 238
Cdd:cd21315 87 VPQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1461-1686 |
8.75e-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: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1461 RDRAAEAEKLRKLAQDEAEKLrKQVSEETQKKRQAEEELKRKSE------AEKEAAKQKQKALEDLEKLRMQAEeAERQV 1534
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERE-TEIAIAQANREAEEAELEQEREietariAEAEAELAKKKAEERREAETARAE-AEAAY 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1535 KQAEIEKEKQIKVAHEAAQKSAAAELQSKhmsfaektsKLEESLKQEHgAVLQLQQEAERLKKQQEdaensrEEAEKEle 1614
Cdd:COG2268 269 EIAEANAEREVQRQLEIAEREREIELQEK---------EAEREEAELE-ADVRKPAEAEKQAAEAE------AEAEAE-- 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 1615 kwrqkaneALRLRLQAEDEAHKKtlaqeeaekqKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAEST 1686
Cdd:COG2268 331 --------AIRAKGLAEAEGKRA----------LAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
24-118 |
9.10e-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: 55.81 E-value: 9.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 24 KTFTKWVNKHLIKA--QRHVTDLYEDLRDGHNLISLLEVLSGETL------PREKGRMrfhkLQNVQIALDFLRHRQVKL 95
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1988774686 96 VNIRNDDIADGNPKLTLGLIWTI 118
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1574-1897 |
9.86e-09 |
|
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: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1574 LEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEahKKTLAQEEAEKQKEEAER 1653
Cdd:pfam19220 25 LKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGE--LEELVARLAKLEAALREA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1654 EAKKRAKAeeSALKQKEMAEEELERQRKIAestAQQKLTAEQELIRLRADFDNAEQQRSLLEDELyrlknevAAAQQQRK 1733
Cdd:pfam19220 103 EAAKEELR--IELRDKTAQAEALERQLAAE---TEQNRALEEENKALREEAQAAEKALQRAEGEL-------ATARERLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1734 QLEDELAKVRSEMDiliqlktKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLraISEEAKHQRQIAEEEAARQRAEA 1813
Cdd:pfam19220 171 LLEQENRRLQALSE-------EQAAELAELTRRLAELETQLDATRARLRALEGQL--AAEQAERERAEAQLEEAVEAHRA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1814 ERI-LKEKLAAIS---EAT-RLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKksseaEM 1888
Cdd:pfam19220 242 ERAsLRMKLEALTaraAATeQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQ-----EM 316
|
....*....
gi 1988774686 1889 ERQKAIVDD 1897
Cdd:pfam19220 317 QRARAELEE 325
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1400-1760 |
1.04e-08 |
|
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: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1400 IQLELQElknlSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETT----EKQKYTAESELKQLRDRAAEAEKLRKLAQ 1475
Cdd:pfam07888 32 LQNRLEE----CLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1476 DEAEKLRKqvsEETQKKRQAEEELKRKSEAEKEAAKQKQKALE---DLEKLRMQAEEAERQVKQAEIEKEK-QIKV-AHE 1550
Cdd:pfam07888 108 ASSEELSE---EKDALLAQRAAHEARIRELEEDIKTLTQRVLEretELERMKERAKKAGAQRKEEEAERKQlQAKLqQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1551 AAQKSAAAELQSKHMSFAEKTSKLEE------SLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAL 1624
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQlqdtitTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1625 RLRLQAEDEAHKKTLAQEEAEKQKEEAE---REAKKRAKAEESALKQKEMAE--------EELERQRKIAESTAQQKLTA 1693
Cdd:pfam07888 265 AQRDRTQAELHQARLQAAQLTLQLADASlalREGRARWAQERETLQQSAEADkdrieklsAELQRLEERLQEERMEREKL 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774686 1694 EQELIRLRadfDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVrseMDILIQLKTKAEKET 1760
Cdd:pfam07888 345 EVELGREK---DCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL---LEYIRQLEQRLETVA 405
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1402-1803 |
1.06e-08 |
|
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: 61.51 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1402 LELQELKNLSEQQIKDKSQQVDealhSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAqDEAEKL 1481
Cdd:COG5185 184 LTLGLLKGISELKKAEPSGTVN----SIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTS-DKLEKL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1482 RKQVSE-ETQKKRQAEEELKRKSEAEKEAAKQ----KQKALEDLEKLRMQA--EEAERQVKQAEIEKEKQIKVAH-EAAQ 1553
Cdd:COG5185 259 VEQNTDlRLEKLGENAESSKRLNENANNLIKQfentKEKIAEYTKSIDIKKatESLEEQLAAAEAEQELEESKREtETGI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1554 KSAAAELQSKHMSFAEKTSKLEESLKQEHGAVL--QLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAE 1631
Cdd:COG5185 339 QNLTAEIEQGQESLTENLEAIKEEIENIVGEVElsKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAA 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1632 DEAHKKtlaqeeaekqkeeAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELI--RLRADFDNAEQ 1709
Cdd:COG5185 419 DRQIEE-------------LQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEInrSVRSKKEDLNE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1710 QRSLLEDELYRLKNEVaaaQQQRKQLEDELAKVRSEMDILIQLKTKAEKETmsNTEKSKQLLEAEAAKMKDLAEEASRLR 1789
Cdd:COG5185 486 ELTQIESRVSTLKATL---EKLRAKLERQLEGVRSKLDQVAESLKDFMRAR--GYAHILALENLIPASELIQASNAKTDG 560
|
410
....*....|....
gi 1988774686 1790 AISEEAKHQRQIAE 1803
Cdd:COG5185 561 QAANLRTAVIDELT 574
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1606-2365 |
1.10e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.06 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1606 REEAEKELEKWRQKANEaLRLRLQAEDEAHKK-------TLAQEEAEKQKEEAEREA-----KKRAKAEESALKQKEMAE 1673
Cdd:pfam15921 73 KEHIERVLEEYSHQVKD-LQRRLNESNELHEKqkfylrqSVIDLQTKLQEMQMERDAmadirRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1674 EELERQRKIAESTAQQKLT--------------AEQELIRLRADFDNAEQQRSLLEDELYRL--KNEVAAAQQQRKQLED 1737
Cdd:pfam15921 152 HELEAAKCLKEDMLEDSNTqieqlrkmmlshegVLQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1738 ELAKVRSEM----DILIQLKTKAEKET----MSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQ 1809
Cdd:pfam15921 232 EISYLKGRIfpveDQLEALKSESQNKIelllQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1810 RAEAERILKEKLAAISEatrLKTEAEIALKEKEAENERLRRQ---AEDEAYQRKALEDQASQHKQEIEEKIvqlkkssea 1886
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQ---LRSELREAKRMYEDKIEELEKQlvlANSELTEARTERDQFSQESGNLDDQL--------- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1887 emerQKAIVDdtLKQRrvvEEEirilklnfekassgkLDLELELNklKNIADETQQSKIRAEEEAEKLrklaleeekrrr 1966
Cdd:pfam15921 380 ----QKLLAD--LHKR---EKE---------------LSLEKEQN--KRLWDRDTGNSITIDHLRREL------------ 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1967 eaeekvkkiaaaeeeaaRQRKAALEELERLRKkaeearKQKDEADKEAEKQIVVAQ---QAAQKCSAAEQQVQSV--LAQ 2041
Cdd:pfam15921 422 -----------------DDRNMEVQRLEALLK------AMKSECQGQMERQMAAIQgknESLEKVSSLTAQLESTkeMLR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2042 QIEDSITQKKLKEEyekakKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRK-EAEFEAA 2120
Cdd:pfam15921 479 KVVEELTAKKMTLE-----SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvQTECEAL 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2121 KRAQAEAAALMQ--KQQADTEM---AKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDavkq 2195
Cdd:pfam15921 554 KLQMAEKDKVIEilRQQIENMTqlvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD---- 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2196 rgqVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKL--LAEEAENM-RKLAEDAARLSVEAQEAARLRQIAED 2272
Cdd:pfam15921 630 ---LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLkRNFRNKSEEMETTTNKLKMQLKSAQS 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2273 DLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLE---DKQLMQQRLEEETEEYHKSLEVERKRQL 2349
Cdd:pfam15921 707 ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEamtNANKEKHFLKEEKNKLSQELSTVATEKN 786
|
810
....*....|....*.
gi 1988774686 2350 EIMAEAERLRLQVSQL 2365
Cdd:pfam15921 787 KMAGELEVLRSQERRL 802
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1587-2041 |
1.18e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1587 QLQQEAERLKKQQEDAENSREEAEKElekwRQKAnEALRlRLQAEDEAHKKTlaqeeaeKQKEEAEREAKKRAKAEESAL 1666
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDA----REQI-ELLE-PIRELAERYAAA-------RERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1667 KQkEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLE-DELYRLKNEVAAAQQQRKQLEDELAKVRSE 1745
Cdd:COG4913 289 RL-ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1746 MDILiQLKTKAEKETMSNT-EKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERI---LKEKL 1821
Cdd:COG4913 368 LAAL-GLPLPASAEEFAALrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparLLALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1822 AAISEATRLKTEA--------EIALKEKEAEN--ER-LRRQA-----EDEAYQR-----------------KALEDQASQ 1868
Cdd:COG4913 447 DALAEALGLDEAElpfvgeliEVRPEEERWRGaiERvLGGFAltllvPPEHYAAalrwvnrlhlrgrlvyeRVRTGLPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1869 HKQEIEEK----IVQLKKSS-----EAEMERQKAIV----DDTLKQ--RRVVEEeiRILKLN---FEKASSGKL------ 1924
Cdd:COG4913 527 ERPRLDPDslagKLDFKPHPfrawlEAELGRRFDYVcvdsPEELRRhpRAITRA--GQVKGNgtrHEKDDRRRIrsryvl 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1925 ---------DLELELNKLKNIADETQQSKIRAEEEAEKL--RKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALE-- 1991
Cdd:COG4913 605 gfdnraklaALEAELAELEEELAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEAELERLDAss 684
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 1992 -ELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQ 2041
Cdd:COG4913 685 dDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1341-1511 |
1.19e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 61.33 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1341 RKKMAEMQAELDKQKQLAEAHAKAIAK-----AEKEAQELKLKMQEEVSKREiaavdaekqktniqLELQELknlsEQQI 1415
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKealleAKEEIHKLRNEFEKELRERR--------------NELQKL----EKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1416 KDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRA-AEAEKLRKLAQDEA-EKLRKQVSEETQKKR 1493
Cdd:PRK12704 92 LQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQlQELERISGLTAEEAkEILLEKVEEEARHEA 171
|
170 180
....*....|....*....|.
gi 1988774686 1494 QA---EEELKRKSEAEKEAAK 1511
Cdd:PRK12704 172 AVlikEIEEEAKEEADKKAKE 192
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1433-1902 |
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 1988774686 1433 EEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAeklrKLAQDEAEKLRKQVS---EET--QKKRQAEEELKRKSEAEK 1507
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQL----KEQLQLLNKLLPQANllaDETlaDRLEELREELDAAQEAQA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1508 EAAkQKQKALEDLEK----LR---MQAEEAERQVKQAEiEKEKQIKvaheaAQKSAAAEL--QSKHMSFAEKTSKLEESl 1578
Cdd:COG3096 911 FIQ-QHGKALAQLEPlvavLQsdpEQFEQLQADYLQAK-EQQRRLK-----QQIFALSEVvqRRPHFSYEDAVGLLGEN- 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1579 kqehgavlqlQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRlRLQAEDEAHkktlaqeeaekqkeeaereakkR 1658
Cdd:COG3096 983 ----------SDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQ-VLASLKSSR----------------------D 1029
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1659 AKAEESALKQKEMAEeelerqrkiaestaqqkltaeqelIRLRADfDNAEQQRSLLEDELYrlkNEVAAAQQQRKQLEDE 1738
Cdd:COG3096 1030 AKQQTLQELEQELEE------------------------LGVQAD-AEAEERARIRRDELH---EELSQNRSRRSQLEKQ 1081
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1739 LAKVRSEMDILIQLKTKAEKETMSNTEkskqllEAEAAKmkdlaEEASRLRAISEEAKHQRQIAEEEAARQRAeaerilk 1818
Cdd:COG3096 1082 LTRCEAEMDSLQKRLRKAERDYKQERE------QVVQAK-----AGWCAVLRLARDNDVERRLHRRELAYLSA------- 1143
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1819 EKLAAISEatrlktEAEIALKEKEAENERLR---RQAEDEAY-QRK-ALEDQASQHKQE-IEEKIVQLKKSSEA--EMER 1890
Cdd:COG3096 1144 DELRSMSD------KALGALRLAVADNEHLRdalRLSEDPRRpERKvQFYIAVYQHLRErIRQDIIRTDDPVEAieQMEI 1217
|
490
....*....|..
gi 1988774686 1891 QKAIVDDTLKQR 1902
Cdd:COG3096 1218 ELARLTEELTSR 1229
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2082-2538 |
1.34e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2082 QQAEEAERQKTAAEEEAANQAKAQEDAERLRKE-AEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQE 2160
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEElEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2161 LTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRG-QVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLl 2239
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2240 aEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQ--EQAQ 2317
Cdd:COG4717 230 -EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKeaEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2318 KLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSeaqaraeeeakKFKKQADKVATRLHETEIAT 2397
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE-----------ELEEELQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2398 QEKMTVVERLEfERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEmaDAQQKKIEHEKTVLQQTfMTEKEMLLK 2477
Cdd:COG4717 378 EAGVEDEEELR-AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEEL-EEELEELRE 453
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 2478 KEKLIEDEKKRLESqfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEE 2538
Cdd:COG4717 454 ELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1490-1759 |
1.36e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.51 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1490 QKKRQAEEELKRKSEAE---KEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEK-EKQIKVAHEAAQKSAaaelqsKHM 1565
Cdd:PRK04863 844 RRRVELERALADHESQEqqqRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEiREQLDEAEEAKRFVQ------QHG 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1566 SFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAEN---------------SREEAEKELEKwRQKANEALRLRL-Q 1629
Cdd:PRK04863 918 NALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafaltevvqrrahfSYEDAAEMLAK-NSDLNEKLRQRLeQ 996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1630 AEDEAhkktlaqeeaekqkeeaeREAKKRAKAEESALKQKEMAEEELerqrKIAESTAQQKLT-AEQEL--IRLRADFdN 1706
Cdd:PRK04863 997 AEQER------------------TRAREQLRQAQAQLAQYNQVLASL----KSSYDAKRQMLQeLKQELqdLGVPADS-G 1053
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 1707 AEQQRSLLEDELYrlkNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKE 1759
Cdd:PRK04863 1054 AEERARARRDELH---ARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2226-2592 |
1.42e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2226 RLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRqiaeDDLNQQRALAEKMLKEKmqaiQEASRLKAEAEML 2305
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEIS----SELPELREELEKLEKEV----KELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2306 QKQKDLAQEQAQKLLEDKQLMQQRLEEeTEEYHKSLEVERKRQLEIMAEAERLRlqvsqlseaqaraeeEAKKFKKQADK 2385
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEE-LKKEIEELEEKVKELKELKEKAEEYI---------------KLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2386 VATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAE----------ELQNKSKEMADAQQK 2455
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHElyeeakakkeELERLKKRLTGLTPE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2456 KIEHEKTVLQqtfmTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQER----QKQQMEQEKKTLQATMDAALSK 2531
Cdd:PRK03918 388 KLEKELEELE----KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEYTAELKR 463
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2532 ----QKEAEEEMLRKQKEMQELERQRLEQERI-----LAEENQKLREKLQQLEDAQKDQHTRETDKVLHK 2592
Cdd:PRK03918 464 iekeLKEIEEKERKLRKELRELEKVLKKESELiklkeLAEQLKELEEKLKKYNLEELEKKAEEYEKLKEK 533
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2230-2569 |
1.59e-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: 59.93 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2230 KDKDSTQKLLAEEAENMRKLAEdAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQK 2309
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMME-EERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2310 DLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQvsqlseaqaraeeeakKFKKQADKVATR 2389
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE----------------YLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2390 LHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADL---ENEKARLKKEAEELQNKSKEMADAQQkkiehektVLQQ 2466
Cdd:pfam13868 172 EAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLyqeEQERKERQKEREEAEKKARQRQELQQ--------AREE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2467 TFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKAlkdEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEM 2546
Cdd:pfam13868 244 QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQE---EAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERL 320
|
330 340
....*....|....*....|...
gi 1988774686 2547 QELERQRleQERILAEENQKLRE 2569
Cdd:pfam13868 321 REEEAER--RERIEEERQKKLKE 341
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1487-1934 |
1.64e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 61.22 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1487 EETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEklrmqaeeaERQVKQAEIEKEKQI-----KVAHEAAQKSAAAELQ 1561
Cdd:PRK10929 24 DEKQITQELEQAKAAKTPAQAEIVEALQSALNWLE---------ERKGSLERAKQYQQVidnfpKLSAELRQQLNNERDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1562 SKHMSFAEKTSKLEESLKQEHGAVL----QLQQEAER----------LKKQQEDAENSREEAEKELE---KWRQKANEAL 1624
Cdd:PRK10929 95 PRSVPPNMSTDALEQEILQVSSQLLeksrQAQQEQDRareisdslsqLPQQQTEARRQLNEIERRLQtlgTPNTPLAQAQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1625 RLRLQAEDEAHKKTLaqeeaekqkeeaereakkrakaeesalkqkemaeEELErqrkiaesTAQQKLTAEQELIRLRAdf 1704
Cdd:PRK10929 175 LTALQAESAALKALV----------------------------------DELE--------LAQLSANNRQELARLRS-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1705 dnaeqqrslledELYrlknevaaaQQQRKQLEDELAKVRSemdiliQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEE 1784
Cdd:PRK10929 211 ------------ELA---------KKRSQQLDAYLQALRN------QLNSQRQREAERALESTELLAEQSGDLPKSIVAQ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1785 ASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAaiseatrLKTEAEIA--LKEKEAENERLRRQAEDEAYQRKAl 1862
Cdd:PRK10929 264 FKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQA-------LNTLREQSqwLGVSNALGEALRAQVARLPEMPKP- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1863 edqasqhkQEIEEKIVQLKKSS---EAEMERQ----KAIVDD----TLKQRRVVEEEIRILKLNFEKASSGKLDLELELN 1931
Cdd:PRK10929 336 --------QQLDTEMAQLRVQRlryEDLLNKQpqlrQIRQADgqplTAEQNRILDAQLRTQRELLNSLLSGGDTLILELT 407
|
...
gi 1988774686 1932 KLK 1934
Cdd:PRK10929 408 KLK 410
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
22-121 |
1.90e-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: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 22 QKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKG-----RMRFHKLQNVQIALDFLRHRQVKLV 96
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 1988774686 97 NIRNDDIADGNPKLTLGLIWTIILH 121
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
141-243 |
2.57e-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: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 141 TAKEKLLLWSQRMTdgyQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLGVTRLLD 219
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQpVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 1988774686 220 PEDVDVPHPDEKSIITYVSSLYDA 243
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1833-2469 |
2.93e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.44 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1833 EAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQH---KQEIEEKIVQLKKSSE--AEMERQKAIVDDTLKQRRVVEE 1907
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHeerREELETLEAEIEDLREtiAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1908 EIR------ILKLNFEKASSGKL-----DLELELNKLKNIADETQQSKIRAEEEAEKLRklaleeekrrreaeekvkkia 1976
Cdd:PRK02224 290 ELEeerddlLAEAGLDDADAEAVearreELEDRDEELRDRLEECRVAAQAHNEEAESLR--------------------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1977 aaeeeaarqrkaalEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSvLAQQIEDSITQKKLKEEY 2056
Cdd:PRK02224 349 --------------EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE-LRERFGDAPVDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2057 ekakklakeaeaakekaereAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRaqaeaaalmqkqqa 2136
Cdd:PRK02224 414 --------------------LEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQ-------------- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2137 DTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDEtdkqksvLDEELQRLKdevdDAVKQRGQVEEELFKVKVQMEELLKL 2216
Cdd:PRK02224 460 PVEGSPHVETIEEDRERVEELEAELEDLEEEVEE-------VEERLERAE----DLVEAEDRIERLEERREDLEELIAER 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2217 KNKIEEENQRLIKKDKDSTQklLAEEAENMRKLAEDAARLSVEAQEAArlrqiaeDDLNQQRAlaekMLKEKMQAIQEAS 2296
Cdd:PRK02224 529 RETIEEKRERAEELRERAAE--LEAEAEEKREAAAEAEEEAEEAREEV-------AELNSKLA----ELKERIESLERIR 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2297 RLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETeeyhkslevERKRQLEIMAEAERLrlqvsqlsEAQARAEEEA 2376
Cdd:PRK02224 596 TLLAAIADAEDEIERLREKREALAELNDERRERLAEKR---------ERKRELEAEFDEARI--------EEAREDKERA 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2377 KKFKKQADKVATRLHETEIATQEKMTVVERlEFERLntskeaDDLRKAIADLENEKARLK---KEAEELQNKSKEM-ADA 2452
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDLQAEIGAVEN-ELEEL------EELRERREALENRVEALEalyDEAEELESMYGDLrAEL 731
|
650
....*....|....*..
gi 1988774686 2453 QQKKIEHEKTVLQQTFM 2469
Cdd:PRK02224 732 RQRNVETLERMLNETFD 748
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1329-1541 |
3.13e-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: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1329 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAvdAEKQKtniqleLQELK 1408
Cdd:TIGR02794 78 EEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAE--AERKA------KEEAA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1409 NLSEQQIKDKSQQvdealhsrtkieeeirliriqlettEKQKYTAESELKQLRDRAAEAEKLRKLAQDE----AEKLRKQ 1484
Cdd:TIGR02794 150 KQAEEEAKAKAAA-------------------------EAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakakAEAAKAK 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774686 1485 VSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDL--EKLRMQAEEAERQVKQAEIEK 1541
Cdd:TIGR02794 205 AAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLasGSNAEKQGGARGAAAGSEVDK 263
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1324-1691 |
3.19e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1324 RRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQ---------ELKLKMQEEVSK-REIAAVDA 1393
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElaelperleELEERLEELRELeEELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1394 EKQKTNIQLE--LQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQ--KYTAESELKQLRDRAAEAE- 1468
Cdd:COG4717 171 ELAELQEELEelLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEleQLENELEAAALEERLKEARl 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1469 --------------------------------------------KLRKLAQDEAEKLRKQVSEETQKKRQAEEELKR--- 1501
Cdd:COG4717 251 llliaaallallglggsllsliltiagvlflvlgllallflllaREKASLGKEAEELQALPALEELEEEELEELLAAlgl 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1502 KSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQK----SAAAELQSKHMSFAEKTSKLEES 1577
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDeeelRAALEQAEEYQELKEELEELEEQ 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1578 LKQEHGAVLQL--QQEAERLKKQQEDAENSREEAEKELEKWRQKanealrlrlQAEDEAHKKTLAQEEAEKQKEEAEREA 1655
Cdd:COG4717 411 LEELLGELEELleALDEEELEEELEELEEELEELEEELEELREE---------LAELEAELEQLEEDGELAELLQELEEL 481
|
410 420 430
....*....|....*....|....*....|....*.
gi 1988774686 1656 KKRAKAEESALKQKEMAEEELERQRKIAESTAQQKL 1691
Cdd:COG4717 482 KAELRELAEEWAALKLALELLEEAREEYREERLPPV 517
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1343-1522 |
3.37e-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: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1343 KMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELklkmQEEVSKREIAAVDAEKQKTNIQLELQELknlsEQQIKDKSQQV 1422
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAAL----EARLEAAKTELEDLEKEIKRLELEIEEV----EARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1423 DEALHSRtkieeEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRK 1502
Cdd:COG1579 83 GNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170 180
....*....|....*....|
gi 1988774686 1503 seaEKEAAKQKQKALEDLEK 1522
Cdd:COG1579 158 ---LEELEAEREELAAKIPP 174
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1330-1562 |
3.45e-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: 58.70 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1330 EKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREiaavdAEKQKTNIQLELQELKN 1409
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1410 LSEQQIKDKSQQvDEALHSRTKIEEEIRliriQLETTEKQKYTAESELKqlrdrAAEAEKlrklaQDEAEKLRKqvsEET 1489
Cdd:TIGR02794 124 AKAKQAAEAKAK-AEAEAERKAKEEAAK----QAEEEAKAKAAAEAKKK-----AEEAKK-----KAEAEAKAK---AEA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774686 1490 QKKRQAeEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEI------EKEKQIKVAHEAAQKSAAAELQS 1562
Cdd:TIGR02794 186 EAKAKA-EEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELgdifglASGSNAEKQGGARGAAAGSEVDK 263
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1736-2359 |
3.57e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1736 EDELAKVRSEmdilIQLKTKAEKETMSNTEKSKQLLEAeaaKMKDLAEEASRLRAISEEakhqrqiaEEEAARQRAEAER 1815
Cdd:PRK03918 164 YKNLGEVIKE----IKRRIERLEKFIKRTENIEELIKE---KEKELEEVLREINEISSE--------LPELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1816 ILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEdqasqhkqEIEEKIVQLK--KSSEAEMERQKA 1893
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE--------ELEEKVKELKelKEKAEEYIKLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1894 IVDDTLKQRRVVE-------EEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRR 1966
Cdd:PRK03918 301 FYEEYLDELREIEkrlsrleEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1967 EAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKdeadKEAEKQIVVAQQAAQKCsaaeqqvqSVLAQQIEDS 2046
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI----KELKKAIEELKKAKGKC--------PVCGRELTEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2047 iTQKKLKEEYEKAKKLAKEAEaakekaereaallrQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAE 2126
Cdd:PRK03918 449 -HRKELLEEYTAELKRIEKEL--------------KEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2127 AAALMQKQQADTEMAKHKKLA----------EQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQR 2196
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLiklkgeikslKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2197 GQVEEELFKvkvqmeELLKLKNkieeenqrlIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQ 2276
Cdd:PRK03918 594 LKELEPFYN------EYLELKD---------AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2277 QRalAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKqlmqqrleEETEEYHKSLEVERKrqleIMAEAE 2356
Cdd:PRK03918 659 EE--YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL--------EEREKAKKELEKLEK----ALERVE 724
|
...
gi 1988774686 2357 RLR 2359
Cdd:PRK03918 725 ELR 727
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
990-1892 |
3.82e-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: 60.06 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 990 RKPVEKEPLKEYIQKTTEQKKVQGELDGLKKDLDKVSVKTQEvlaspqpsasapvLRSELDLTVQKMDHAHMlssvylEK 1069
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEK-------------DNSELELKMEKVFQGTD------EQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1070 LKTVEMVIRNTQGAEGvlKQYEDCLREVHTVPSDVKEvetyrakLKKMRTEAEDEQPVFdSLEEELKKASAVSDKMVRVH 1149
Cdd:TIGR00606 303 LNDLYHNHQRTVREKE--RELVDCQRELEKLNKERRL-------LNQEKTELLVEQGRL-QLQADRHQEHIRARDSLIQS 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1150 SERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQLGRQLGYYRESYDWLIRWIADAKQRQEKIQAVPITDSKTLKEQ 1229
Cdd:TIGR00606 373 LATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1230 LAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDyeLQLVAYKAQVEPLVSPLKKTKLDSAsdNIIQEYVTLRTRYSELM 1309
Cdd:TIGR00606 453 QEELKFVIKELQQLEGSSDRILELDQELRKAERE--LSKAEKNSLTETLKKEVKSLQNEKA--DLDRKLRKLDQEMEQLN 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1310 TLTSQYIKFITDTQRRLDDEEKaAEKLKAEERKKMAEMQAELDKQKQLAEAHAKaIAKAEKEAQELKLKMQEEVSKREIA 1389
Cdd:TIGR00606 529 HHTTTRTQMEMLTKDKMDKDEQ-IRKIKSRHSDELTSLLGYFPNKKQLEDWLHS-KSKEINQTRDRLAKLNKELASLEQN 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1390 AVDAEKQKTniQLELQELKnLSEQQIKDKSQQVDEALHSRTKieEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEK 1469
Cdd:TIGR00606 607 KNHINNELE--SKEEQLSS-YEDKLFDVCGSQDEESDLERLK--EEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCP 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1470 L-RKLAQDEAEkLRKQVSEETQKKRQAEEELKrksEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVA 1548
Cdd:TIGR00606 682 VcQRVFQTEAE-LQEFISDLQSKLRLAPDKLK---STESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVN 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1549 HEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQ--QEDAENSREEAEKELEKWRQKANEalrl 1626
Cdd:TIGR00606 758 RDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKiaQQAAKLQGSDLDRTVQQVNQEKQE---- 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1627 rlqaEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDN 1706
Cdd:TIGR00606 834 ----KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKE 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1707 AEQ-QRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMK-DLAEE 1784
Cdd:TIGR00606 910 QDSpLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNaQLEEC 989
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1785 ASRLRAISEEAKHQRQIAEEEAARqraeaERILKEKLaaiseaTRLKTEAEIalkekeAENERLRRQAEDEAYQRKALed 1864
Cdd:TIGR00606 990 EKHQEKINEDMRLMRQDIDTQKIQ-----ERWLQDNL------TLRKRENEL------KEVEEELKQHLKEMGQMQVL-- 1050
|
890 900
....*....|....*....|....*...
gi 1988774686 1865 QASQHKQEIEEKIVQLKKSSEAEMERQK 1892
Cdd:TIGR00606 1051 QMKQEHQKLEENIDLIKRNHVLALGRQK 1078
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2314-2587 |
5.65e-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: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2314 EQAQKLLEDKQLMQQRLEEETEEYHKSLEVERK----RQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATR 2389
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEkreyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2390 LHETEIATQEKMTVVERL-EFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEmADAQQKKIEHEKTVL---Q 2465
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-LEAEIDKLLAEIEELereI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2466 QTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQ----------EKKTLQATMDAALSKQKEA 2535
Cdd:TIGR02169 346 EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkreinelkrELDRLQEELQRLSEELADL 425
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 2536 EEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETD 2587
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2179-2583 |
5.93e-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: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2179 DEELQRLKDEVDDAVKqrgqveeELFKVKVQMEELlklKNKIEEENQRLIKKDkDSTQKLLAeeaenMRKLAEDAARLSV 2258
Cdd:pfam10174 115 EENFRRLQSEHERQAK-------ELFLLRKTLEEM---ELRIETQKQTLGARD-ESIKKLLE-----MLQSKGLPKKSGE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2259 EAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRlkaeaeMLQKQKDLAQEQA-QKLLEDKQLMQQRLEEETEEY 2337
Cdd:pfam10174 179 EDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHR------RNQLQPDPAKTKAlQTVIEMKDTKISSLERNIRDL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2338 HKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLH--ETEIATQEKMTVVERLEFERLNTS 2415
Cdd:pfam10174 253 EDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLalQTKLETLTNQNSDCKQHIEVLKES 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2416 KEADDLRKAIADLENEKARLKKEAEE--LQNKSKEMADAQQkkiehEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQF 2493
Cdd:pfam10174 333 LTAKEQRAAILQTEVDALRLRLEEKEsfLNKKTKQLQDLTE-----EKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2494 EEEVKKAKALKDEQERQK--QQMEQEKKTLQATMDAALSkQKEAEEEMLRKQKEmqELERQRLEQERILAEENQKLREKL 2571
Cdd:pfam10174 408 EQLRDKDKQLAGLKERVKslQTDSSNTDTALTTLEEALS-EKERIIERLKEQRE--REDRERLEELESLKKENKDLKEKV 484
|
410
....*....|..
gi 1988774686 2572 QQLEDAQKDQHT 2583
Cdd:pfam10174 485 SALQPELTEKES 496
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2218-2455 |
6.64e-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: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2218 NKIEEENQRL--IKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEA 2295
Cdd:COG4942 20 DAAAEAEAELeqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2296 SRLKAE-AEMLQKQKDLAQEQAQKLL---EDKQLMQQRLEeeteeYHKSLEVERKRQleimaeAERLRLQVSQLSEAQAR 2371
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALLlspEDFLDAVRRLQ-----YLKYLAPARREQ------AEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2372 AEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMAD 2451
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
....
gi 1988774686 2452 AQQK 2455
Cdd:COG4942 249 AALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2404-2581 |
7.21e-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: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2404 VERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQ-------QTFMTEKEMLl 2476
Cdd:COG3883 46 LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgsesfSDFLDRLSAL- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2477 kkEKLIEDEKKRLESQfeeevkkaKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQ 2556
Cdd:COG3883 125 --SKIADADADLLEEL--------KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
170 180
....*....|....*....|....*
gi 1988774686 2557 ERILAEENQKLREKLQQLEDAQKDQ 2581
Cdd:COG3883 195 EAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
136-243 |
7.21e-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: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 136 QSEDMTAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQ-QTNLENLEQAFSVAEKDLGV 214
Cdd:cd21313 3 DAKKQTPKQRLLGWIQ---NKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDpQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1988774686 215 TRLLDPEDVDVPHPDEKSIITYVSSLYDA 243
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4013-4049 |
7.56e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.94 E-value: 7.56e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1988774686 4013 IRLLEAQIATGGIIDPEESHRLPVEVAYNRGFFDEEM 4049
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1511-1693 |
7.90e-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: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1511 KQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAhEAAQKSAAAELQSKhmsfaektskleeslkQEHGAVLQLQQ 1590
Cdd:COG2268 180 EDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIA-QANREAEEAELEQE----------------REIETARIAEA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1591 EAERLKKQQE---DAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALK 1667
Cdd:COG2268 243 EAELAKKKAEerrEAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAE 322
|
170 180
....*....|....*....|....*.
gi 1988774686 1668 QKEMAEEELERQRKIAESTAQQKLTA 1693
Cdd:COG2268 323 AEAEAEAEAIRAKGLAEAEGKRALAE 348
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1402-1560 |
1.03e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.09 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1402 LELQEL---KNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQD-- 1476
Cdd:COG1579 10 LDLQELdseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1477 EAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKL--RMQAEEAERQVKQAEIEKE-KQIKVAHEAAQ 1553
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELeaELEEKKAELDEELAELEAElEELEAEREELA 169
|
....*..
gi 1988774686 1554 KSAAAEL 1560
Cdd:COG1579 170 AKIPPEL 176
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1323-1520 |
1.20e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.51 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1323 QRRLDDEEKaaEKLKAEERKKMAEMQA--ELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKreiAAVDAEKQktni 1400
Cdd:PRK09510 100 QERLKQLEK--ERLAAQEQKKQAEEAAkqAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK---AAAEAKKK---- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1401 qlELQELKNLSEQQIKDKsqqvdealhsrtkieeeirliriqLETTEKQKYTAESELKQLRDRAAEAEKLRKlAQDEAEK 1480
Cdd:PRK09510 171 --AEAEAAKKAAAEAKKK------------------------AEAEAAAKAAAEAKKKAEAEAKKKAAAEAK-KKAAAEA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1988774686 1481 LRKQVSEETQKKRQAEEELKRKSeAEKEAAKQKQKALEDL 1520
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKA-AEKAAAAKAAAEVDDL 262
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2320-2581 |
1.22e-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: 57.24 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2320 LEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLheteiatqe 2399
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ--------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2400 kmtvvERLEFERLNTSKEADDLRKAIADLENEKARLK--KEAEELQNKSKEMaDAQQKKIEHEKTVLQQTFMTEKEMLLK 2477
Cdd:pfam13868 99 -----EREQMDEIVERIQEEDQAEAEEKLEKQRQLREeiDEFNEEQAEWKEL-EKEEEREEDERILEYLKEKAEREEERE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2478 KEKL-IEDEKKRLESQFEEEVKKAKALKDEQE---------------RQKQQMEQEKK-TLQATMDAALSKQKEAEEEML 2540
Cdd:pfam13868 173 AEREeIEEEKEREIARLRAQQEKAQDEKAERDelraklyqeeqerkeRQKEREEAEKKaRQRQELQQAREEQIELKERRL 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1988774686 2541 RKQKEMQELERQRL-----EQERILAEENQKLREKLQQLEDAQKDQ 2581
Cdd:pfam13868 253 AEEAEREEEEFERMlrkqaEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2179-2364 |
1.25e-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: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2179 DEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLiKKDKDSTQKLLAEEAENMRKLAEDAARLSV 2258
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2259 EAQEAARLRQIAE--------DDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRL 2330
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190
....*....|....*....|....*....|....
gi 1988774686 2331 EEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQ 2364
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1329-1689 |
1.31e-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: 57.65 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1329 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQL--ELQE 1406
Cdd:pfam15709 172 ERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERNLEVaaELSG 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1407 LKNLSEQQIKDKSQQVDEALHSRT-------KIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAE 1479
Cdd:pfam15709 252 PDVINSKETEDASERGAFSSDSVVedpwlssKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1480 K-LRKQVSEETQKKRQAEEELKRKSEAEKEaaKQKQKALEDLEKLRMQAEEaERQVKQAEIEKEKQiKVAHEAAQKSAAA 1558
Cdd:pfam15709 332 KaSRDRLRAERAEMRRLEVERKRREQEEQR--RLQQEQLERAEKMREELEL-EQQRRFEEIRLRKQ-RLEEERQRQEEEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1559 ELQSKHMSFAEKTSKLEEslKQEHGAVLQLQQeaerlKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEahkkt 1638
Cdd:pfam15709 408 RKQRLQLQAAQERARQQQ--EEFRRKLQELQR-----KKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEE----- 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 1639 laqeEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQ 1689
Cdd:pfam15709 476 ----RLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1320-1611 |
1.42e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 57.57 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1320 TDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHA---KAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQ 1396
Cdd:pfam02029 52 PSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIAdekESVAERKENNEEEENSSWEKEEKRDSRLGRYKEE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1397 KTNIQlelqeLKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQD 1476
Cdd:pfam02029 132 ETEIR-----EKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1477 EAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQvkqaEIEKEKQikvaheaAQKSA 1556
Cdd:pfam02029 207 VKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESE----EFEKLRQ-------KQQEA 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774686 1557 AAELQSKHMSFAEKTSKLEESLKQEHgavlqlQQEAERLKKQQEDAENSREEAEK 1611
Cdd:pfam02029 276 ELELEELKKKREERRKLLEEEEQRRK------QEEAERKLREEEEKRRMKEEIER 324
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2132-2506 |
1.47e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.11 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2132 QKQQADTEMAKHKKLAEQTLKQKF-----QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKV 2206
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEQDWNKELkselkNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2207 KVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKlaedaarlsveaqeaarlrqiaedDLNQQRALAEKMLK 2286
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK------------------------DEQIKKLQQEKELL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2287 EKmqaiqEASRLKAEAEMLQKQ-KDLAQEQAQKLLEDKQLMQQR--LEEETEEYHKSLEVER------KRQLEI-MAEAE 2356
Cdd:TIGR04523 425 EK-----EIERLKETIIKNNSEiKDLTNQDSVKELIIKNLDNTResLETQLKVLSRSINKIKqnleqkQKELKSkEKELK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2357 RLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFE--RLNTSKEADDLRKAIADLENEKAR 2434
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKS 579
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774686 2435 LKKEAEELQNKSKEMADAQQ---KKIEhEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDE 2506
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKdliKEIE-EKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1401-1737 |
1.73e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.83 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1401 QLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKlrklaqdEAEK 1480
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE-------ELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1481 LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAEL 1560
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1561 QSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLA 1640
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1641 QEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYR 1720
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330
....*....|....*..
gi 1988774686 1721 LKNEVAAAQQQRKQLED 1737
Cdd:COG4372 325 AKKLELALAILLAELAD 341
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2135-2337 |
1.89e-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: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2135 QADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELL 2214
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2215 K-----------------------------LKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEdaarLSVEAQEAAR 2265
Cdd:COG3883 93 RalyrsggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 2266 LRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEY 2337
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
17-122 |
1.93e-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: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 17 ERDRVQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 87
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnkvNKPPYPKLGANMK--KLENCNYAVEL 93
|
90 100 110
....*....|....*....|....*....|....*.
gi 1988774686 88 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21331 94 GKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRY 129
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2212-2575 |
2.08e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2212 ELLKLKNKIEEENQRLIkkdkdSTQKLLAEEAENMRKLAED----AARLSVeAQEAARLR-QI--AEDDLNqqrALAEKm 2284
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLV-----EMARELAELNEAESDLEQDyqaaSDHLNL-VQTALRQQeKIerYQADLE---ELEER- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2285 LKEKMQAIQEASRlkaEAEMLQKQKDLAQEQAQKLleDKQL--MQQRLEEETE---EYHKSLE-VERKRQLeimaeaerl 2358
Cdd:PRK04863 364 LEEQNEVVEEADE---QQEENEARAEAAEEEVDEL--KSQLadYQQALDVQQTraiQYQQAVQaLERAKQL--------- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2359 rLQVSQLSeaqaraeeeakkfkkqADKVATRLHEteIATQEKMTVVERLEFE-RLNTSKEADD--------LRKAIADLE 2429
Cdd:PRK04863 430 -CGLPDLT----------------ADNAEDWLEE--FQAKEQEATEELLSLEqKLSVAQAAHSqfeqayqlVRKIAGEVS 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2430 NEKA------------RLKKEAEELQNKSKEMADAQQKKIEHEKTV-LQQTFMTEKEMLLKKEKLIEDEKKRLESQFE-- 2494
Cdd:PRK04863 491 RSEAwdvarellrrlrEQRHLAEQLQQLRMRLSELEQRLRQQQRAErLLAEFCKRLGKNLDDEDELEQLQEELEARLEsl 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2495 -EEVKKAKALKDEQERQKQQMEQEKKTLQA------TMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKL 2567
Cdd:PRK04863 571 sESVSEARERRMALRQQLEQLQARIQRLAArapawlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDEL 650
|
....*...
gi 1988774686 2568 REKLQQLE 2575
Cdd:PRK04863 651 AARKQALD 658
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2249-2591 |
2.16e-07 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 57.04 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2249 LAEDAARLSVEAQEAARLRQIAEDDLNQQRA-------LAEKMLKEKMQAIQEA-----------SRLKAEAEMLQKQKD 2310
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAkfkelylAKEEDLKRQNAVLQEAqveldalqnqlALARAEMENIKAVAT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2311 LAQEQAQKLLED------------KQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAER----LRLQVSQlSEAQARAEE 2374
Cdd:pfam03528 86 VSENTKQEAIDEvksqwqeevaslQAIMKETVREYEVQFHRRLEQERAQWNQYRESAEReiadLRRRLSE-GQEEENLED 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2375 EAKKFKKQADKVATRL--HETEIAT--------QEKMTVVERLEFERLNTSKEAD-----DLRKAIADLENEKARLKKEA 2439
Cdd:pfam03528 165 EMKKAQEDAEKLRSVVmpMEKEIAAlkaklteaEDKIKELEASKMKELNHYLEAEkscrtDLEMYVAVLNTQKSVLQEDA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2440 EELQNKSKEMADA-QQKKIEHekTVLQQTFMTEKEMLLKKEKLIEDEKKRLESqfeeevkkakALKDEQERQKQQmeqek 2518
Cdd:pfam03528 245 EKLRKELHEVCHLlEQERQQH--NQLKHTWQKANDQFLESQRLLMRDMQRMES----------VLTSEQLRQVEE----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2519 ktlqatmdaaLSKQKEAEEEMLRKQKEMQELERQRLEQERILA-------EENQKLREKLQQLEDAQKDQHTRETDKVLH 2591
Cdd:pfam03528 308 ----------IKKKDQEEHKRARTHKEKETLKSDREHTVSIHAvfspagvETSAPLSNVEEQINSAHGSVHSLDTDVVLG 377
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1414-1695 |
2.35e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 57.27 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1414 QIKDKSQQVDEAlhsrtKIEEEIRLIRIQlettekqkytaeselkqlRDRAAEAEKLRKLAQDEAEKLRKQVSE--ETQK 1491
Cdd:PRK05035 440 AIEQEKKKAEEA-----KARFEARQARLE------------------REKAAREARHKKAAEARAAKDKDAVAAalARVK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1492 KRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAElqskhmsfAEKT 1571
Cdd:PRK05035 497 AKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQ--------QAAN 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1572 SKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKwRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEA 1651
Cdd:PRK05035 569 AEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDP-KKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA 647
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1988774686 1652 EREAKKRAKAEESALKQKEMAEEELERQRKIAESTA----QQKLTAEQ 1695
Cdd:PRK05035 648 VAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAiaraKAKKAAQQ 695
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1454-1842 |
2.36e-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: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1454 ESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQkqkALEDLEKLRMQAEEAERQ 1533
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ---SREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1534 vkQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKtskleeslkqehgaVLQLQQEAERLKKQQEDAENSREEAEKEl 1613
Cdd:pfam07888 110 --SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQR--------------VLERETELERMKERAKKAGAQRKEEEAE- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1614 ekwrqkaNEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEeelerQRKIAESTAqqkltA 1693
Cdd:pfam07888 173 -------RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA-----HRKEAENEA-----L 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1694 EQELIRLRADFDNAEQQRSLLEDELyrlknEVAAAQQQRKQLEDELAKVRS-EMDILIQLKTKAEKETMSNTEKSKQLL- 1771
Cdd:pfam07888 236 LEELRSLQERLNASERKVEGLGEEL-----SSMAAQRDRTQAELHQARLQAaQLTLQLADASLALREGRARWAQERETLq 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774686 1772 ---EAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEklaAISEATRLKTEAEIALKEKE 1842
Cdd:pfam07888 311 qsaEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSE---SRRELQELKASLRVAQKEKE 381
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1412-1726 |
2.43e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1412 EQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQK 1491
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1492 KRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKT 1571
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1572 SKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEA 1651
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774686 1652 EREAKKRAKAEESALKQKEMAEEELERQRKIaesTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVA 1726
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALE---DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDV 355
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
969-1531 |
2.49e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 969 SELKDLRLRIEDCEAG-TVARIRKPVEKEPLKEYIQKTTEQKKVQGELDGLKKDL-----------DKVSVKTQEVLAsp 1036
Cdd:PRK02224 213 SELAELDEEIERYEEQrEQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaeterereelaEEVRDLRERLEE-- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1037 qpsasapvLRSELDltvqkmdhaHMLSSVYLEKL--KTVEMVIRNTQGAEgvlKQYEDCLREVHTVPSDV-KEVETYRAK 1113
Cdd:PRK02224 291 --------LEEERD---------DLLAEAGLDDAdaEAVEARREELEDRD---EELRDRLEECRVAAQAHnEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1114 LKKMRTEAEDEQPVFDSLEEELKKASAVSDkmvrvhsERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQLgrqlgy 1193
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVE-------DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL------ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1194 yRESYDwlirwiaDAKQRQEKIQAvpitDSKTLKEQLAQEKKLLEEieqnkDKVDECQKYAK--AYIDTIKDYELQ---L 1268
Cdd:PRK02224 418 -REERD-------ELREREAELEA----TLRTARERVEEAEALLEA-----GKCPECGQPVEgsPHVETIEEDRERveeL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1269 VAYKAQVEPLVSPLKKtKLDSASDniiqeYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLkaeeRKKMAEMQ 1348
Cdd:PRK02224 481 EAELEDLEEEVEEVEE-RLERAED-----LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL----RERAAELE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1349 AEldkqkqlAEAHAKAIAKAEKEAQElklkmqeevsKREIAAvDAEKQKTNIQLELQELKNLSEQQ--IKDKSQQVDEAL 1426
Cdd:PRK02224 551 AE-------AEEKREAAAEAEEEAEE----------AREEVA-ELNSKLAELKERIESLERIRTLLaaIADAEDEIERLR 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1427 HSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKlrklaqDEAEKLRKQVSEETQKKRQAEEELK------ 1500
Cdd:PRK02224 613 EKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDK------ERAEEYLEQVEEKLDELREERDDLQaeigav 686
|
570 580 590
....*....|....*....|....*....|....*
gi 1988774686 1501 RKSEAEKEAAKQKQKALED----LEKLRMQAEEAE 1531
Cdd:PRK02224 687 ENELEELEELRERREALENrveaLEALYDEAEELE 721
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1393-1575 |
2.59e-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: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1393 AEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETtEKQKYTAESELKQLRDRAAEAEKLRk 1472
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAA-EKAAKQAEQAAKQAEEKQKQAEEAK- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1473 lAQDEAEKLRKqvsEETQKKRQAEEELKRKSEAE---KEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKvah 1549
Cdd:TIGR02794 126 -AKQAAEAKAK---AEAEAERKAKEEAAKQAEEEakaKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKA--- 198
|
170 180
....*....|....*....|....*.
gi 1988774686 1550 EAAQKSAAAELQSKHMSFAEKTSKLE 1575
Cdd:TIGR02794 199 EAAKAKAAAEAAAKAEAEAAAAAAAE 224
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1454-1893 |
2.70e-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: 57.06 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1454 ESELKQLRDRAAEAEKLRKLAQDEAEK----LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEdLEKLRMQAEE 1529
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKkasaLKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAE-LNRLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1530 AERQVKQaeiEKEKQIKVAHE--AAQKSAAAEL----QSKHMSFAEKTSKLEEsLKQEHGAVLQLQQEAERLKKQQEDAE 1603
Cdd:pfam05557 87 ALNKKLN---EKESQLADAREviSCLKNELSELrrqiQRAELELQSTNSELEE-LQERLDLLKAKASEAEQLRQNLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1604 NSREEAE---KELEKWRQKAN-----------EALRL-RLQAEDEAHK------------KTLAQEEAEKQKEEAEREAK 1656
Cdd:pfam05557 163 SSLAEAEqriKELEFEIQSQEqdseivknsksELARIpELEKELERLRehnkhlnenienKLLLKEEVEDLKRKLEREEK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1657 KRAKAEESALKqKEMAEEELERQRKIAESTA-----------------QQKLTAEQELIRLRADFDNAEQQRSLLEDELY 1719
Cdd:pfam05557 243 YREEAATLELE-KEKLEQELQSWVKLAQDTGlnlrspedlsrrieqlqQREIVLKEENSSLTSSARQLEKARRELEQELA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1720 RLKNEVAAAQQQRKQ-------LEDELAKVRSEMDILIQLKTKAEKEtMSNTEKSKQLLEaeaaKMKDLAEEASRLRAIS 1792
Cdd:pfam05557 322 QYLKKIEDLNKKLKRhkalvrrLQRRVLLLTKERDGYRAILESYDKE-LTMSNYSPQLLE----RIEEAEDMTQKMQAHN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1793 EEAKHQRQIAEEEAARQRAEA---ERILK-----EKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQrkaLED 1864
Cdd:pfam05557 397 EEMEAQLSVAEEELGGYKQQAqtlERELQalrqqESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEME---LER 473
|
490 500 510
....*....|....*....|....*....|
gi 1988774686 1865 QASQHKQEIEE-KIVQLKKSSEAEMERQKA 1893
Cdd:pfam05557 474 RCLQGDYDPKKtKVLHLSMNPAAEAYQQRK 503
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2152-2573 |
2.75e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2152 KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQM----EELLKLKNKIEEENQRL 2227
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVedrrEEIEELEEEIEELRERF 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2228 --IKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAE---------------------DDLNQQRALAEKM 2284
Cdd:PRK02224 401 gdAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpvegsphvETIEEDRERVEEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2285 LKEKMQAIQEASRLKAEAEMLQKQKDLAQEqAQKLLEDKQLMQQRLEEETEEyhksleVERKRQleimaEAERLRLQVSQ 2364
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLVEAEDR-IERLEERREDLEELIAERRET------IEEKRE-----RAEELRERAAE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2365 LSEAQARAEEEAKKFKKQADKVATRLHETEiatQEKMTVVERLefERLNTSKEADDlrkAIADLENEKARLKKEAEELQN 2444
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELN---SKLAELKERI--ESLERIRTLLA---AIADAEDEIERLREKREALAE 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2445 KSKEmadaqqkkiehektvlqqtfmtekemllKKEKLIE--DEKKRLESQFEEE-VKKAKALKDEQERQKQQME------ 2515
Cdd:PRK02224 621 LNDE----------------------------RRERLAEkrERKRELEAEFDEArIEEAREDKERAEEYLEQVEekldel 672
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 2516 -QEKKTLQATMDAALSKQKEAEEemLRKQKEMQELERQRLEQERILAEENQ----KLREKLQQ 2573
Cdd:PRK02224 673 rEERDDLQAEIGAVENELEELEE--LRERREALENRVEALEALYDEAEELEsmygDLRAELRQ 733
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1666-1899 |
2.80e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.35 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1666 LKQKEMAEEELERQRKIAESTAQQKLTAEQElirlradfdnAEQQRsLLEDELYRLknevaAAQQQRKQLEDelakvrse 1745
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQA----------AEQER-LKQLEKERL-----AAQEQKKQAEE-------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1746 mdiliQLKTKAEKETMSNTEKSKQlleAEAAKMKdLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILK-EKLAAI 1824
Cdd:PRK09510 123 -----AAKQAALKQKQAEEAAAKA---AAAAKAK-AEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKaEAEAAA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774686 1825 SEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDqasqhKQEIEEKIVQLKKSSEAEMERQKAIVDDTL 1899
Cdd:PRK09510 194 KAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAE-----AKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1984-2336 |
2.88e-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: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1984 RQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKcsaAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLA 2063
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ---SREKHEELEEKYKELSASSEELSEEKDALLAQR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2064 KEAEAAKEKAEREAALLRQQAEEAERQktaaeeeAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKH 2143
Cdd:pfam07888 125 AAHEARIRELEEDIKTLTQRVLERETE-------LERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2144 KKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQR-----------------LKDEVDDAVKQRGQVEEELFKV 2206
Cdd:pfam07888 198 RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrslqerlnaserkvegLGEELSSMAAQRDRTQAELHQA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2207 KVQMEEL---LKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEK 2283
Cdd:pfam07888 278 RLQAAQLtlqLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRV 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 2284 MLKEKMQAIQEasrLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEE 2336
Cdd:pfam07888 358 QLSESRRELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADA 407
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1105-1538 |
2.95e-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: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1105 KEVETYRAKLKKMRTEAEDEQpvfDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQREL 1184
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKL---KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1185 EQLGRQLGyyresydwlirwIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTI-KD 1263
Cdd:TIGR00606 768 EEQETLLG------------TIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQeKQ 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1264 YELQLVAYKAQVeplvsplkKTKLDSASDNIIQEYvtlrtrYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKaeerkK 1343
Cdd:TIGR00606 836 HELDTVVSKIEL--------NRKLIQDQQEQIQHL------KSKTNELKSEKLQIGTNLQRRQQFEEQLVELST-----E 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1344 MAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNL----SEQQIKDKS 1419
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgKDDYLKQKE 976
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1420 Q-------QVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKK 1492
Cdd:TIGR00606 977 TelntvnaQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEH 1056
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1988774686 1493 RQAEEELKRKSEAEKEAAKQkQKALEDlEKLRMQAEEAERQVKQAE 1538
Cdd:TIGR00606 1057 QKLEENIDLIKRNHVLALGR-QKGYEK-EIKHFKKELREPQFRDAE 1100
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1572-1896 |
3.25e-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: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1572 SKLEESLkQEHGAVLQLQQEAERlkkqqeDAENSREEAEKELEKWRQKANEaLRLRLQAEDEAHKKTLAQEEAEKQKEEA 1651
Cdd:pfam07888 34 NRLEECL-QERAELLQAQEAANR------QREKEKERYKRDREQWERQRRE-LESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1652 EREAKKRAKAEESAL-KQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 1730
Cdd:pfam07888 106 LSASSEELSEEKDALlAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1731 QRKQLEDELAKVRSEMD----ILIQLKTKAEKETMSNTEKSKQLLEAEAAKmKDLAEEASRLrAISEEAKH--QRQIAEE 1804
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALL-EELRSLQERL-NASERKVEglGEELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1805 EAARQRAEAEriLKEKLAAISEATRLKTEAEIALKEkeaenERLRRQAEDEAYQRKALEDQasQHKQEIEEKIVQLKKS- 1883
Cdd:pfam07888 264 AAQRDRTQAE--LHQARLQAAQLTLQLADASLALRE-----GRARWAQERETLQQSAEADK--DRIEKLSAELQRLEERl 334
|
330
....*....|...
gi 1988774686 1884 SEAEMERQKAIVD 1896
Cdd:pfam07888 335 QEERMEREKLEVE 347
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1416-1835 |
3.32e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1416 KDKSQQVDEALHSR--------TKIEEEIRLIRIQ--LETTEKQKYTAESELKQLRDRAAeaeklrkLAQdeaEKLRKQv 1485
Cdd:PRK04863 279 NERRVHLEEALELRrelytsrrQLAAEQYRLVEMAreLAELNEAESDLEQDYQAASDHLN-------LVQ---TALRQQ- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1486 seetQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVK----------QAEIEKEKQIKVAHEAAQKS 1555
Cdd:PRK04863 348 ----EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDelksqladyqQALDVQQTRAIQYQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1556 AAAELQSKHMSFAEKtsKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAlrLRLQAEDEAh 1635
Cdd:PRK04863 424 ERAKQLCGLPDLTAD--NAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEV--SRSEAWDVA- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1636 kktlaqeeaekqkeeaeREAKKRAKaeesalKQKEMAEEELERQRKIAEstAQQKLTAEQELIRLRADF----------- 1704
Cdd:PRK04863 499 -----------------RELLRRLR------EQRHLAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFckrlgknldde 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1705 DNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELakvrSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEE 1784
Cdd:PRK04863 554 DELEQLQEELEARLESLSESVSEARERRMALRQQL----EQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDV 629
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 1785 ASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAE 1835
Cdd:PRK04863 630 TEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1663-2295 |
3.50e-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: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1663 ESALKQKEMAEEELERQRKIAESTAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKV 1742
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARERL---AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1743 RSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEE-ASRLRAISEEAKHQRQIAEE---EAARQRAEAERILK 1818
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARlEALLAALGLPLPASAEEFAAlraEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1819 EKLAAISEATRLKTEAEIALKEKEAENERLRRQAE--DEAYQ--RKALEDQASQHKQEI----EEkiVQLKkssEAEMER 1890
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLERRKSniPARLLalRDALAEALGLDEAELpfvgEL--IEVR---PEEERW 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1891 QKAI------------VDDTLKQ--RRVVEEEIRILKLNFEKASSGKLDLELE-------LNKLkniadETQQSKIRAEE 1949
Cdd:COG4913 477 RGAIervlggfaltllVPPEHYAaaLRWVNRLHLRGRLVYERVRTGLPDPERPrldpdslAGKL-----DFKPHPFRAWL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1950 EAEKLRKLALEeekrrreaeekvkkiaaaeeeaarqRKAALEELERLRK--------KAEEARKQKDEADKEAEKQiVVA 2021
Cdd:COG4913 552 EAELGRRFDYV-------------------------CVDSPEELRRHPRaitragqvKGNGTRHEKDDRRRIRSRY-VLG 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2022 QQAAQKCSAAEQQvqsvlAQQIEDSITQkklkeeyekakklakeaeaakekaereaalLRQQAEEAERQKtaaeeeaanq 2101
Cdd:COG4913 606 FDNRAKLAALEAE-----LAELEEELAE------------------------------AEERLEALEAEL---------- 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2102 AKAQEDAERLRKEAEFeaakraqaeaaalmQKQQADTEMAkHKKLAEqtlkqkfqVEQELTKvklkLDETDKQKSVLDEE 2181
Cdd:COG4913 641 DALQERREALQRLAEY--------------SWDEIDVASA-EREIAE--------LEAELER----LDASSDDLAALEEQ 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2182 LQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLknkIEEENQRLIKKDKDSTQKLLAEeaenmrkLAEDAARLSVEAQ 2261
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEE---LDELQDRLEAAEDLARLELRAL-------LEERFAAALGDAV 763
|
650 660 670
....*....|....*....|....*....|....*.
gi 1988774686 2262 EAARLRQIAE--DDLNQQRALAEKMLKEKMQAIQEA 2295
Cdd:COG4913 764 ERELRENLEEriDALRARLNRAEEELERAMRAFNRE 799
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1321-1558 |
3.83e-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: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1321 DTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELklkmqeevsKREIAAVDAEKQKTNI 1400
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL---------QAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1401 QLElqelKNLSEQQIKDKSQQVDEALHSRTKIEEEIRliriQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEK 1480
Cdd:COG3883 87 ELG----ERARALYRSGGSVSYLDVLLGSESFSDFLD----RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774686 1481 LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAA 1558
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1348-1810 |
4.32e-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: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1348 QAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQktniqleLQELKNLSEQQIKDKSQQVDEA-L 1426
Cdd:pfam09731 81 EPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKA-------LEEVLKEAISKAESATAVAKEAkD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1427 HSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAE--AEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKrKSE 1504
Cdd:pfam09731 154 DAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEklKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLD-NVE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1505 AEKEAAKQKQKALEDLEKLrmqaEEAERQVKQAEIEKekqikvaheaAQKSAAAELQSKHMSFAEKTSKLEESLKQEhga 1584
Cdd:pfam09731 233 EKVEKAQSLAKLVDQYKEL----VASERIVFQQELVS----------IFPDIIPVLKEDNLLSNDDLNSLIAHAHRE--- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1585 VLQLQQEAERLKKQ-QEDAENSREEAEKELEKwrqkANEALRLRLQAEDEAHKKTLaqeeaekqkeeaerEAKKRAKAEE 1663
Cdd:pfam09731 296 IDQLSKKLAELKKReEKHIERALEKQKEELDK----LAEELSARLEEVRAADEAQL--------------RLEFEREREE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1664 SALKQKEMAEEELERQRKIAESTAQQKL-TAEQEL-IRLRADFDNA-EQQRSLLE---DELYRLKNEVAAAQQQRKQLED 1737
Cdd:pfam09731 358 IRESYEEKLRTELERQAEAHEEHLKDVLvEQEIELqREFLQDIKEKvEEERAGRLlklNELLANLKGLEKATSSHSEVED 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774686 1738 ELAKVRSemdilIQLKTKAEKETM--SNTEKSKQLLEAEAAKMKDLAEE----ASRLRAISEEAKhQRQIAEEEAARQR 1810
Cdd:pfam09731 438 ENRKAQQ-----LWLAVEALRSTLedGSADSRPRPLVRELKALKELASDdevvKAALASLPEEAY-QRGVYTEAALRER 510
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1359-1716 |
4.69e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 56.03 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1359 EAHAKAIAKA-EKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSeqqikDKSQQVDEALHSRTKIEEEIR 1437
Cdd:pfam02029 1 IEDEEEAARErRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG-----QGGLDEEEAFLDRTAKREERR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1438 LIRIQlETTEKQKytaESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKE-----AAKQ 1512
Cdd:pfam02029 76 QKRLQ-EALERQK---EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQEnkwstEVRQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1513 KQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKhmSFAEKTSKLEESLKQEHGAVLQLQQEA 1592
Cdd:pfam02029 152 AEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKR--GHPEVKSQNGEEEVTKLKVTTKRRQGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1593 ERLKKQQEDAENSREEAEKELEKWRQKANEALRlrlqAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEEsalkQKEMA 1672
Cdd:pfam02029 230 LSQSQEREEEAEVFLEAEQKLEELRRRRQEKES----EEFEKLRQKQQEAELELEELKKKREERRKLLEEE----EQRRK 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1988774686 1673 EEELERQRKIAESTAQQKltaeQELIRLRAdfDNAEQQRSLLED 1716
Cdd:pfam02029 302 QEEAERKLREEEEKRRMK----EEIERRRA--EAAEKRQKLPED 339
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1653-2090 |
4.72e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 56.07 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1653 REAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQR 1732
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1733 KQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAE 1812
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1813 AERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQK 1892
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1893 AIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKV 1972
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1973 KKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKL 2052
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430
....*....|....*....|....*....|....*...
gi 1988774686 2053 KEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQ 2090
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAA 519
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1452-1688 |
6.82e-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: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1452 TAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKrkseaekeaakQKQKALEDLEKlrmQAEEAE 1531
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-----------ALQAEIDKLQA---EIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1532 RQVKQAEIEKEKQIKVAHEAAQKSAAAE--LQSKHMS-FAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREE 1608
Cdd:COG3883 79 AEIEERREELGERARALYRSGGSVSYLDvlLGSESFSdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1609 AEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQ 1688
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4116-4144 |
7.00e-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: 7.00e-07
10 20
....*....|....*....|....*....
gi 1988774686 4116 IVDPETGKEMTVYEAYRKGLIDHQTYLEL 4144
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1210-1632 |
7.18e-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: 55.52 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1210 QRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAY---KAQVEPLVSPLKK-T 1285
Cdd:pfam05557 121 QRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQeqdSEIVKNSKSELARiP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1286 KLDSASDNIIQEYVTLRTRYSELMTLTSQyikfITDTQRRLDDEEKAAEKLKAEERKKmAEMQAELDKQKQLAEAHAKAI 1365
Cdd:pfam05557 201 ELEKELERLREHNKHLNENIENKLLLKEE----VEDLKRKLEREEKYREEAATLELEK-EKLEQELQSWVKLAQDTGLNL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1366 AKAEKEAQELKLKMQEE-VSKREIAAVDAE-KQKTNIQLELQE-----LKNLSEQQIKDKSQqvdEALHSRTK-----IE 1433
Cdd:pfam05557 276 RSPEDLSRRIEQLQQREiVLKEENSSLTSSaRQLEKARRELEQelaqyLKKIEDLNKKLKRH---KALVRRLQrrvllLT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1434 EEIRLIRIQLETTEKQKYTAESELKQLRdRAAEAEKLRKLAQDEAEKLRKQVS----EETQKKRQA-----EEELKRKSE 1504
Cdd:pfam05557 353 KERDGYRAILESYDKELTMSNYSPQLLE-RIEEAEDMTQKMQAHNEEMEAQLSvaeeELGGYKQQAqtlerELQALRQQE 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1505 AEKEAAKQKQKALE---DLEKLRMQAEEAERQVKQAEIEKEKqikvaHEAAQKSAAAELQSKHMSfAEKTSKLEESLKQE 1581
Cdd:pfam05557 432 SLADPSYSKEEVDSlrrKLETLELERQRLREQKNELEMELER-----RCLQGDYDPKKTKVLHLS-MNPAAEAYQQRKNQ 505
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 1582 HGavlQLQQEAERLKKQQEDAENSREEAEKELEKWRQKAN-EALRLRLQAED 1632
Cdd:pfam05557 506 LE---KLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFkEVLDLRKELES 554
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1245-1506 |
8.46e-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: 8.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1245 DKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKKTKLD--------SASDNIIQEYVTLRTRYSELMTLTSQYI 1316
Cdd:pfam05262 79 DHILNLRRILAGYLMAAYGYERSDAETIAKFITIYNAVYRGDLDyfkefykeVVTKSLTKENAGLARRYDQWPGKTQIVI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1317 KF--------ITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREI 1388
Cdd:pfam05262 159 PLkknilsgnVSDVDTDSISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADF 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1389 AAVDAEKQKTNIQLELQELKNlSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTaESELKQLRDRAAEAE 1468
Cdd:pfam05262 239 AQDNADKQRDEVRQKQQEAKN-LPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAK-DHKAFDLKQESKASE 316
|
250 260 270
....*....|....*....|....*....|....*...
gi 1988774686 1469 KLRKLAQDEAEKLRKQVSEETQKKRQAEEElKRKSEAE 1506
Cdd:pfam05262 317 KEAEDKELEAQKKREPVAEDLQKTKPQVEA-QPTSLNE 353
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1327-1572 |
8.48e-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: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1327 DDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEevSKREIAAVDAEKQKTNIQLElqe 1406
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK--LQAEIAEAEAEIEERREELG--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1407 lKNLSEQQIKDKSQQVDEALHSRTKIEEEIRliRIQLettekqkytaeseLKQLRDRAAEAEKLRKLAQDEAEKLRKQVS 1486
Cdd:COG3883 90 -ERARALYRSGGSVSYLDVLLGSESFSDFLD--RLSA-------------LSKIADADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1487 EETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMS 1566
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
....*.
gi 1988774686 1567 FAEKTS 1572
Cdd:COG3883 234 AAAAAA 239
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1432-1741 |
9.37e-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: 54.15 E-value: 9.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1432 IEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDE-AEKLRKQVsEETQKKRQAEEELKRKseaEKEAA 1510
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyRQELEEQI-EEREQKRQEEYEEKLQ---EREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1511 KQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAV-LQLQ 1589
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIeEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1590 QEAERLKKQQEDAENSREEAEKELEKWRQKANEAlRLRLQAEDEAHKKtlaqeeaeKQKEEAEREAKKRAKAEESALKQK 1669
Cdd:pfam13868 184 REIARLRAQQEKAQDEKAERDELRAKLYQEEQER-KERQKEREEAEKK--------ARQRQELQQAREEQIELKERRLAE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 1670 EMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAK 1741
Cdd:pfam13868 255 EAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAE 326
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1654-1910 |
9.47e-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: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1654 EAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRadfdnaeQQRSLLEDELYRLKNEVAAAQQQRK 1733
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQK-------ELEQRAAAEKAAKQAEQAAKQAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1734 QLEDELAKVRSEMDILIQLKTKAEKETMSNTEKskqllEAEAAKMKDLAEEASRlraiseEAKHQRQIAEEEAaRQRAEA 1813
Cdd:TIGR02794 118 QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK-----QAEEEAKAKAAAEAKK------KAEEAKKKAEAEA-KAKAEA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1814 ERILK-EKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQK 1892
Cdd:TIGR02794 186 EAKAKaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYA 265
|
250
....*....|....*...
gi 1988774686 1893 AIVDDTLKQRRVVEEEIR 1910
Cdd:TIGR02794 266 AIIQQAIQQNLYDDPSFR 283
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1705-1953 |
9.72e-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: 9.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1705 DNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLE-AEAAKMKDLAE 1783
Cdd:TIGR02794 29 PEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQrAAAEKAAKQAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1784 EASRL-RAISEEAKHQRQIAEEEAARQR-AEAERILKEKLAAISEATRLKTEAEIALKEKEAEnerlRRQAEDEAyqrKA 1861
Cdd:TIGR02794 109 QAAKQaEEKQKQAEEAKAKQAAEAKAKAeAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEA----KKKAEAEA---KA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1862 ledqasqhKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRvvEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQ 1941
Cdd:TIGR02794 182 --------KAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEA--EAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGG 251
|
250
....*....|..
gi 1988774686 1942 QSKIRAEEEAEK 1953
Cdd:TIGR02794 252 ARGAAAGSEVDK 263
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2457-2655 |
9.80e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 55.22 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2457 IEHEKTVLQqtfmTEKEMLlkkEKLIED-EKKRLESqfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEA 2535
Cdd:PRK00409 504 IEEAKKLIG----EDKEKL---NELIASlEELEREL--EQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2536 EEEMLRKQKEMQEL---ERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDIIHLTtiETTKTVYNGQNv 2612
Cdd:PRK00409 575 AQQAIKEAKKEADEiikELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVG--DEVKYLSLGQK- 651
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1988774686 2613 GDVVDGIDKKPDPLAFDGIRDKVPASRLHELGVLPKKEFDKLK 2655
Cdd:PRK00409 652 GEVLSIPDDKEAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPK 694
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2301-2579 |
9.83e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 9.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2301 EAEMLQKQKDLAQE---QAQKLLED-KQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRlqvsQLSEAQARAEEEA 2376
Cdd:PTZ00121 1078 DFDFDAKEDNRADEateEAFGKAEEaKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR----KAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2377 KKFKKQADKvATRLHETEIATQEKMTVVER--LEFERLNTSKEADDLRKAIADLENEKARLKKE---------------A 2439
Cdd:PTZ00121 1154 VEIARKAED-ARKAEEARKAEDAKKAEAARkaEEVRKAEELRKAEDARKAEAARKAEEERKAEEarkaedakkaeavkkA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2440 EELQNKSKEMADAQQKKIEHEKTVLQQTFM---TEKEMLLKKE--------KLIEDEKKRLESQFEEEVKKAKALKDEQE 2508
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMahfARRQAAIKAEearkadelKKAEEKKKADEAKKAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2509 RQKQQMEQEKKTLQATMDAALSKQK---------------EAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQ 2573
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKaeeakkaaeaakaeaEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
|
....*.
gi 1988774686 2574 LEDAQK 2579
Cdd:PTZ00121 1393 ADEAKK 1398
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2150-2557 |
1.02e-06 |
|
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: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2150 TLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIK 2229
Cdd:pfam07888 8 TLEEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2230 KDKDSTQKLlaEEAENMRKLAEDA---------ARLSVEAQEAARLRQIAEDdlnqQRALAEKMLKEKMqaiqEASRLKA 2300
Cdd:pfam07888 88 ELRQSREKH--EELEEKYKELSASseelseekdALLAQRAAHEARIRELEED----IKTLTQRVLERET----ELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2301 EAEMLQKQKdlAQEQAQKllEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLseaqaraeeeakkfK 2380
Cdd:pfam07888 158 RAKKAGAQR--KEEEAER--KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTL--------------T 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2381 KQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIE-- 2458
Cdd:pfam07888 220 QKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREgr 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2459 ----HEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKE 2534
Cdd:pfam07888 300 arwaQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKE 379
|
410 420
....*....|....*....|....*
gi 1988774686 2535 AEEEMLRKQKEMQELER--QRLEQE 2557
Cdd:pfam07888 380 KEQLQAEKQELLEYIRQleQRLETV 404
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1839-2277 |
1.06e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.13 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1839 KEKEAENERLRRQAEDEAyqrkaledqasqHKQEIEEKIVQLKKSSEAEMERQKAIVDDtlkQRRVVEEEIRilklnfek 1918
Cdd:pfam17380 292 KFEKMEQERLRQEKEEKA------------REVERRRKLEEAEKARQAEMDRQAAIYAE---QERMAMERER-------- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1919 assgkldlelELNKLKNIADETQQSKIRAEE---EAEKLRKLaleeekrrreaeekvkkiaaAEEEAARQRKAaleelER 1995
Cdd:pfam17380 349 ----------ELERIRQEERKRELERIRQEEiamEISRMREL--------------------ERLQMERQQKN-----ER 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1996 LRKKAEEARKQKDEadkEAEKQIVVAQQAAQKCSAAEQQVQsvlAQQIEdsitQKKLKEEyekakklakeaeaakekaeR 2075
Cdd:pfam17380 394 VRQELEAARKVKIL---EEERQRKIQQQKVEMEQIRAEQEE---ARQRE----VRRLEEE-------------------R 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2076 EAALLRQQAEEAERQKtaaeeeaANQAKAQEDAERLRKEAEfeaakraqaeaaalMQKQQADtemakhKKLAEQtlKQKF 2155
Cdd:pfam17380 445 AREMERVRLEEQERQQ-------QVERLRQQEEERKRKKLE--------------LEKEKRD------RKRAEE--QRRK 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2156 QVEQELTKVKLKLDETDKQKSVLDEElqrlkdevddavkqrgqveeelfkvkvqMEEllkLKNKIEEENQRLIKKDKDST 2235
Cdd:pfam17380 496 ILEKELEERKQAMIEEERKRKLLEKE----------------------------MEE---RQKAIYEEERRREAEEERRK 544
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1988774686 2236 QKLLAEE---AENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQ 2277
Cdd:pfam17380 545 QQEMEERrriQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2134-2587 |
1.11e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.11 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2134 QQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEE- 2212
Cdd:pfam05483 102 KQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREEt 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2213 ---LLKLKNKIEE------------ENQRL-----IKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAarlrqiaED 2272
Cdd:pfam05483 182 rqvYMDLNNNIEKmilafeelrvqaENARLemhfkLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEK-------EN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2273 DLNQQRALAEKMlKEKMQAIQEASRLKAE--AEMLQKQKDLAQEqaqklLEDKQLMQQR-------LEEETEEYHKS--- 2340
Cdd:pfam05483 255 KMKDLTFLLEES-RDKANQLEEKTKLQDEnlKELIEKKDHLTKE-----LEDIKMSLQRsmstqkaLEEDLQIATKTicq 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2341 LEVERKRQLEIMAEAERLR-LQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEAD 2419
Cdd:pfam05483 329 LTEEKEAQMEELNKAKAAHsFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2420 DLRKAIAD---LENEKARLKKEAEELQNKSKEMADA-QQKKIEHEKTVLQQTFMTEKEMLLKKEklIEDEKKRLESQfee 2495
Cdd:pfam05483 409 ELKKILAEdekLLDEKKQFEKIAEELKGKEQELIFLlQAREKEIHDLEIQLTAIKTSEEHYLKE--VEDLKTELEKE--- 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2496 evkKAKALKDEQERQKQQMEQEKKTLQAT-MDAALSKQKE-------AEEEMLRKQKEMQELERQ-RLEQERILAEENQK 2566
Cdd:pfam05483 484 ---KLKNIELTAHCDKLLLENKELTQEASdMTLELKKHQEdiinckkQEERMLKQIENLEEKEMNlRDELESVREEFIQK 560
|
490 500
....*....|....*....|.
gi 1988774686 2567 LREKLQQLEDAQKDQHTRETD 2587
Cdd:pfam05483 561 GDEVKCKLDKSEENARSIEYE 581
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1591-2024 |
1.22e-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: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1591 EAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQK- 1669
Cdd:NF033838 56 QKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQFKKDTl 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1670 EMAEEELERQRKIAEstAQQKLTAEQElirlradfdnaEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVrsemdil 1749
Cdd:NF033838 136 EPGKKVAEATKKVEE--AEKKAKDQKE-----------EDRRNYPTNTYKTLELEIAESDVEVKKAELELVKE------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1750 iqlktkaEKETMSNTEKSKQlleaEAAKMKDLAEEASRLraisEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATR 1829
Cdd:NF033838 196 -------EAKEPRDEEKIKQ----AKAKVESKKAEATRL----EKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1830 LKTEAEIALKEKEAENERLRRQAE--DEAYQRKALEDQASQHKQ---EIEEKIVQLKKSSEAEMERQKaivddtlkqRRV 1904
Cdd:NF033838 261 PKRRAKRGVLGEPATPDKKENDAKssDSSVGEETLPSPSLKPEKkvaEAEKKVEEAKKKAKDQKEEDR---------RNY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1905 VEEEIRILKLNFEKASSGKLDLELELNK--LKNIADETQQSKIRAEEEAEKlrklaleeekrrreaeekvkkiaaaeeea 1982
Cdd:NF033838 332 PTNTYKTLELEIAESDVKVKEAELELVKeeAKEPRNEEKIKQAKAKVESKK----------------------------- 382
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1988774686 1983 arQRKAALEELERLRKKAEEARKQK-DEADKEAEKQIVVAQQA 2024
Cdd:NF033838 383 --AEATRLEKIKTDRKKAEEEAKRKaAEEDKVKEKPAEQPQPA 423
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1454-1693 |
1.27e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 54.22 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1454 ESELKQLRDRAAEAEKlrKLAQDE-AEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQK--QKALEDLEKLRMQAEEA 1530
Cdd:PRK07735 4 EKDLEDLKKEAARRAK--EEARKRlVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRaaAAAKAKAAALAKQKREG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1531 ERQVKQAEIEKEKqiKVAHEAAQKSAAAELQSKHMSFAEKTSklEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAE 1610
Cdd:PRK07735 82 TEEVTEEEKAKAK--AKAAAAAKAKAAALAKQKREGTEEVTE--EEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1611 KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKK-----RAKAEESAL-KQKEM-----AEEELERQ 1679
Cdd:PRK07735 158 EETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKakaaaAAKAKAAALaKQKASqgngdSGDEDAKA 237
|
250
....*....|....
gi 1988774686 1680 RKIAESTAQQKLTA 1693
Cdd:PRK07735 238 KAIAAAKAKAAAAA 251
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1323-1580 |
1.27e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 54.95 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1323 QRRLDDEekaaeKLKAEERKKMAEmqAELDKQKQLAEAHAKAIAKAEKEAQElklkmqeevskREIAAVDAEKQKTNIQL 1402
Cdd:PRK05035 459 QARLERE-----KAAREARHKKAA--EARAAKDKDAVAAALARVKAKKAAAT-----------QPIVIKAGARPDNSAVI 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1403 ELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRliRIQLETTEKQKYTAESELKQLRDRAAEAEklrKLAQDEAEKLR 1482
Cdd:PRK05035 521 AAREARKAQARARQAEKQAAAAADPKKAAVAAAIA--RAKAKKAAQQAANAEAEEEVDPKKAAVAA---AIARAKAKKAA 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1483 KQVSEETQKKRQAEEELKrKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVK-QAEIEKEKQIKVAHEAAQKSAAAELQ 1561
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPK-KAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAvAAAIARAKARKAAQQQANAEPEEAED 674
|
250
....*....|....*....
gi 1988774686 1562 SKHMSFAEKTSKLEESLKQ 1580
Cdd:PRK05035 675 PKKAAVAAAIARAKAKKAA 693
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1352-1637 |
1.44e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 54.22 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1352 DKQKQLAEAHAKAIAKAEKEAQELKLKMQEEvskrEIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTK 1431
Cdd:PRK07735 2 DPEKDLEDLKKEAARRAKEEARKRLVAKHGA----EISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1432 IEEEIRliriqlETTEKQKYTAESelkqlrdRAAEAEKLRklaqdeAEKLRKQVSEETQkkrQAEEELKRKSEAeKEAAK 1511
Cdd:PRK07735 78 KREGTE------EVTEEEKAKAKA-------KAAAAAKAK------AAALAKQKREGTE---EVTEEEKAAAKA-KAAAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1512 QKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQE 1591
Cdd:PRK07735 135 AKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAK 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1988774686 1592 AERLKKQQEdaenSREEAEKELEKWRQKANEALRLRLQAEDEAHKK 1637
Cdd:PRK07735 215 AAALAKQKA----SQGNGDSGDEDAKAKAIAAAKAKAAAAARAKTK 256
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1454-1554 |
1.48e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 54.83 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1454 ESELKQLRDRAAEAEKLRKlaqdEAEKLRKQVSEetQKKRQAEEELKRKSEAEKEAAKQ----KQKALEDLEKLR-MQAE 1528
Cdd:PRK00409 526 EELERELEQKAEEAEALLK----EAEKLKEELEE--KKEKLQEEEDKLLEEAEKEAQQAikeaKKEADEIIKELRqLQKG 599
|
90 100
....*....|....*....|....*.
gi 1988774686 1529 EAERQVKQAEIEKEKQIKVAHEAAQK 1554
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEKKEK 625
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1315-1896 |
1.54e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.91 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1315 YIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKqlaeaHAKAIAKAEKEAQELKLKMQEEVSKreiaavdAE 1394
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYN-----NLKSALNELSSLEDMKNRYESEIKT-------AE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1395 KQKTNIQLELQELKNLSEQQIKDKSqqvDEALHSRTKIEEEIRLIRiQLETTEKQKYTAESELKQLRDraaeaeKLRKLA 1474
Cdd:PRK01156 263 SDLSMELEKNNYYKELEERHMKIIN---DPVYKNRNYINDYFKYKN-DIENKKQILSNIDAEINKYHA------IIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1475 QDEAEKlrkqvsEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQ--AEIEKEKQIKVAHEAA 1552
Cdd:PRK01156 333 VLQKDY------NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERmsAFISEILKIQEIDPDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1553 QKSAAAELQSKHMSFAEKTSKLEESLK---------QEHGAVLQLQ------------QEAERLKKQQEDAENSREEAEK 1611
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRalrenldelSRNMEMLNGQsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1612 ELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEEL-ERQRKIAESTAQQK 1690
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIkNRYKSLKLEDLDSK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1691 ltaeqelirlRADFDNAEQQRSLLE-DELYRLKNEVaaaQQQRKQLEDELAKVRSEMDiliqlktkaekETMSNTEKSKQ 1769
Cdd:PRK01156 567 ----------RTSWLNALAVISLIDiETNRSRSNEI---KKQLNDLESRLQEIEIGFP-----------DDKSYIDKSIR 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1770 LLEAEAAKMKDLAEEASRLRAISEEAKhqrqiaeeeaarqraEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLR 1849
Cdd:PRK01156 623 EIENEANNLNNKYNEIQENKILIEKLR---------------GKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSR 687
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1850 RQAED---EAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVD 1896
Cdd:PRK01156 688 KALDDakaNRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGD 737
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1707-1877 |
1.68e-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: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1707 AEQQRSLLEdeLYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtMSNTEKSKQLLEAEAAKMKDLAEEA- 1785
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLELEIEEVEARIKKYe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1786 SRLRAIS--EEAKH-QRQIaeEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAL 1862
Cdd:COG1579 80 EQLGNVRnnKEYEAlQKEI--ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|....*
gi 1988774686 1863 EDQASQHKQEIEEKI 1877
Cdd:COG1579 158 LEELEAEREELAAKI 172
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
145-240 |
1.79e-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: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 145 KLLL-WSQRMTDGYqGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNL-----------------------EN 200
Cdd:cd21224 3 SLLLkWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 201 LEQAFSVAEK-----------DLG-VTRLLDPEDVDVPHPDEKSIITYVSSL 240
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1329-1626 |
1.90e-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: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1329 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELK 1408
Cdd:pfam06160 87 ALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1409 NLSEQQIKDKSQQVDEALHSRTkIEEEIRLIRI-----QLETT---------------EKQKYT-----AESELKQLRDR 1463
Cdd:pfam06160 167 ELTESGDYLEAREVLEKLEEET-DALEELMEDIpplyeELKTElpdqleelkegyremEEEGYAlehlnVDKEIQQLEEQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1464 AAEAEK-LRKLAQDEAEKLRKQVSEETQK-----------KRQAEEELKRKSEAEKEAAKQKQKALEDLEKL----RMQA 1527
Cdd:pfam06160 246 LEENLAlLENLELDEAEEALEEIEERIDQlydllekevdaKKYVEKNLPEIEDYLEHAEEQNKELKEELERVqqsyTLNE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1528 EEAERqvkQAEIEKE-KQIKVAHEAAQKsaaaELQSKHMSFAEKTSKLEESLKQehgaVLQLQQEAERLKKQQEDAENSR 1606
Cdd:pfam06160 326 NELER---VRGLEKQlEELEKRYDEIVE----RLEEKEVAYSELQEELEEILEQ----LEEIEEEQEEFKESLQSLRKDE 394
|
330 340
....*....|....*....|
gi 1988774686 1607 EEAEKELEKWRQKANEALRL 1626
Cdd:pfam06160 395 LEAREKLDEFKLELREIKRL 414
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1234-1901 |
2.04e-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: 54.67 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1234 KKLLEEIEQNKDKVDECQKYAKAY--IDTIKDYELQlvaYKAQVEPLVSPLKKtkLDSASDNIIQEYVTLRTRySElmtl 1311
Cdd:TIGR01612 1073 KEILEEAEINITNFNEIKEKLKHYnfDDFGKEENIK---YADEINKIKDDIKN--LDQKIDHHIKALEEIKKK-SE---- 1142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1312 tsqyiKFITDTQRRLDDEEKAAEKLKAEE-----RKKMAEMQAELDKQKQLAEAHAK---AIAKAEK------EAQELKL 1377
Cdd:TIGR01612 1143 -----NYIDEIKAQINDLEDVADKAISNDdpeeiEKKIENIVTKIDKKKNIYDEIKKllnEIAEIEKdktsleEVKGINL 1217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1378 KMQEEVSKREIAAVDAEKQKTNIQLELQE--LKNLSEqqIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAES 1455
Cdd:TIGR01612 1218 SYGKNLGKLFLEKIDEEKKKSEHMIKAMEayIEDLDE--IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKK 1295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1456 ELKQLRDRaaeAEKLRKLAQDEAEK---------LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQK-QKALEDLEKLRM 1525
Cdd:TIGR01612 1296 HDENISDI---REKSLKIIEDFSEEsdindikkeLQKNLLDAQKHNSDINLYLNEIANIYNILKLNKiKKIIDEVKEYTK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1526 QAEEAERQVKQAEIEKEKQIKVAHEaaqksaaaelqskHMSFAEKTSKLEESL--KQEHGAVLQLQQEAERLKKQQEDA- 1602
Cdd:TIGR01612 1373 EIEENNKNIKDELDKSEKLIKKIKD-------------DINLEECKSKIESTLddKDIDECIKKIKELKNHILSEESNId 1439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1603 ---ENSREEAE------KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAER-EAKKRAKAEEsalKQKEMA 1672
Cdd:TIGR01612 1440 tyfKNADENNEnvlllfKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKdEADKNAKAIE---KNKELF 1516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1673 EeelerQRKIAESTAQQKLTAeqelIRLRADFDNAEQQRSLLEDELYRLKN----EVAAAQQQRKQLEDElaKVRSEMDI 1748
Cdd:TIGR01612 1517 E-----QYKKDVTELLNKYSA----LAIKNKFAKTKKDSEIIIKEIKDAHKkfilEAEKSEQKIKEIKKE--KFRIEDDA 1585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1749 liqLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASrlRAISEEAKHQRQIAEEEAARQRAEaeriLKEKLAAISEat 1828
Cdd:TIGR01612 1586 ---AKNDKSNKAAIDIQLSLENFENKFLKISDIKKKIN--DCLKETESIEKKISSFSIDSQDTE----LKENGDNLNS-- 1654
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774686 1829 rLKTEAEiALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIE----EKIVQLKKSSEAEMERQKAIVDDTLKQ 1901
Cdd:TIGR01612 1655 -LQEFLE-SLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEigiiEKIKEIAIANKEEIESIKELIEPTIEN 1729
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1338-1793 |
2.05e-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: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1338 AEERKKMAEMQAEL-----DKQKQLAEAHAKAIAKAEkeaqELklkmqEEVSKREiAAVDAEKQKTNIQLELqeLKNLSE 1412
Cdd:COG3096 277 ANERRELSERALELrrelfGARRQLAEEQYRLVEMAR----EL-----EELSARE-SDLEQDYQAASDHLNL--VQTALR 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1413 QQIKDKSQQVD-EALHSRTKIEEEIRliriqlettekqkytaeselKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEetqk 1491
Cdd:COG3096 345 QQEKIERYQEDlEELTERLEEQEEVV--------------------EEAAEQLAEAEARLEAAEEEVDSLKSQLAD---- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1492 KRQAEEELKRKseaekeaAKQKQKALEDLEKLRMQAEEAERQVKQAEiekekqikvAHEAAQKSAAAELQSKHMSFAEKT 1571
Cdd:COG3096 401 YQQALDVQQTR-------AIQYQQAVQALEKARALCGLPDLTPENAE---------DYLAAFRAKEQQATEEVLELEQKL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1572 SkLEESLKQEHGAVLQLQQEAerlkkqqeDAENSREEAekelekWrQKANEALR----LRLQAEDEAHKKTlaqeEAEKQ 1647
Cdd:COG3096 465 S-VADAARRQFEKAYELVCKI--------AGEVERSQA------W-QTARELLRryrsQQALAQRLQQLRA----QLAEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1648 KEEAEREAKKRAKAEESALKQK------EMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRL 1721
Cdd:COG3096 525 EQRLRQQQNAERLLEEFCQRIGqqldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAW 604
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774686 1722 KNEVAAAQQQRKQLEDELAKVRSEMDILIQLktkAEKETMSNTEKS-----KQLLEAEAAKMKDLA-EEASRLRAISE 1793
Cdd:COG3096 605 LAAQDALERLREQSGEALADSQEVTAAMQQL---LEREREATVERDelaarKQALESQIERLSQPGgAEDPRLLALAE 679
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1829-2322 |
2.38e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1829 RLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKivqlkKSSEAEMERQKAIVDDTLKQRRVVEEE 1908
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL-----EELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1909 IRILKLNFEKASsgkldLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKA 1988
Cdd:COG4717 125 LQLLPLYQELEA-----LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1989 ALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSIT--QKKLKEEYEKAKKLAKEA 2066
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLalLGLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2067 EAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKL 2146
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2147 AEQTLKQKFQVEQE--LTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELfKVKVQMEELLKLKNKIEEEN 2224
Cdd:COG4717 360 EEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL-EELLEALDEEELEEELEELE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2225 QRlikkdkdstqklLAEEAENMRKLAEDAARLSveaqeaARLRQIAEDDLNQQRALAEKMLKEKMQ-AIQEASRLKAEAE 2303
Cdd:COG4717 439 EE------------LEELEEELEELREELAELE------AELEQLEEDGELAELLQELEELKAELReLAEEWAALKLALE 500
|
490 500
....*....|....*....|
gi 1988774686 2304 MLQK-QKDLAQEQAQKLLED 2322
Cdd:COG4717 501 LLEEaREEYREERLPPVLER 520
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1319-1804 |
2.38e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 54.04 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1319 ITDTQRRLDDEEKAAEKLKAEErkkMAEMQAELDKQK----QLAEAHAKAIAKAEKEAQelklkMQEEvskreIAAVDAE 1394
Cdd:PRK10246 389 LTHAEQKLNALPAITLTLTADE---VAAALAQHAEQRplrqRLVALHGQIVPQQKRLAQ-----LQVA-----IQNVTQE 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1395 KQKTNIQLELQElknlseQQIKDKSQQVDEAlhsRTKIEEEIRL-----IRIQLE---------TTEK---QKYTAeSEL 1457
Cdd:PRK10246 456 QTQRNAALNEMR------QRYKEKTQQLADV---KTICEQEARIkdleaQRAQLQagqpcplcgSTSHpavEAYQA-LEP 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1458 KQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQA 1537
Cdd:PRK10246 526 GVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQ 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1538 EiEKEKQIKvaheaaQKSAAAELQSKHMSFAEKTSKLEESLKQEHgAVLQLQQEAERLKKQQEDAENS-REEAEKELEKW 1616
Cdd:PRK10246 606 E-EHERQLR------LLSQRHELQGQIAAHNQQIIQYQQQIEQRQ-QQLLTALAGYALTLPQEDEEASwLATRQQEAQSW 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1617 RQKANEALRLRLQ-AEDEAHKKTLAQEEAEKQKEEAE-----REAKKRAKAEESALkQKEMAEEELERQRkIAESTAQ-- 1688
Cdd:PRK10246 678 QQRQNELTALQNRiQQLTPLLETLPQSDDLPHSEETValdnwRQVHEQCLSLHSQL-QTLQQQDVLEAQR-LQKAQAQfd 755
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1689 QKLTA---EQELIRLRADFDNA-----EQQRSLLEDELYRLK-------NEVAAAQQQRKQLEDELAKVRSEMDILIQLK 1753
Cdd:PRK10246 756 TALQAsvfDDQQAFLAALLDEEtltqlEQLKQNLENQRQQAQtlvtqtaQALAQHQQHRPDGLDLTVTVEQIQQELAQLA 835
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 1754 TKAEKETMSNTEKSKQLleaeaakmKDLAEEASRLRAISEEAKHQRQIAEE 1804
Cdd:PRK10246 836 QQLRENTTRQGEIRQQL--------KQDADNRQQQQALMQQIAQATQQVED 878
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3900-3936 |
2.43e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.71 E-value: 2.43e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1988774686 3900 RYLQGTGCIAGVFLESTKERLSIYQAMKKNMIRPGTA 3936
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2430-2575 |
2.46e-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: 52.67 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2430 NEKARLKKEAEELQNKSKEMADAQQKKIEhEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLEsqfeEEVKKAKALKDEQER 2509
Cdd:pfam02841 155 EERDKLEAKYNQVPRKGVKAEEVLQEFLQ-SKEAVEEAILQTDQALTAKEKAIEAERAKAE----AAEAEQELLREKQKE 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2510 QKQQMEQEKKTLQATMdAALSKQKEAEEEMLRKQKEMQeLERQRLEQERILAE----ENQKLREKLQQLE 2575
Cdd:pfam02841 230 EEQMMEAQERSYQEHV-KQLIEKMEAEREQLLAEQERM-LEHKLQEQEELLKEgfktEAESLQKEIQDLK 297
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1347-1529 |
2.52e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1347 MQAELDKQKQLAEAHAKaIAKAEKEAQELklkmQEEVSKREIAAVDAEKQKTNIQLELQELknlsEQQIKDKSQQVDEAL 1426
Cdd:COG1579 2 MPEDLRALLDLQELDSE-LDRLEHRLKEL----PAELAELEDELAALEARLEAAKTELEDL----EKEIKRLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1427 HSRTKIEEEIRLIRiqletTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAE 1506
Cdd:COG1579 73 ARIKKYEEQLGNVR-----NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
170 180
....*....|....*....|...
gi 1988774686 1507 KEAAKQKQKALEDLEKLRMQAEE 1529
Cdd:COG1579 148 DEELAELEAELEELEAEREELAA 170
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1297-1751 |
2.55e-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: 54.06 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1297 EYVTLRTRyseLMTLTSQYikfiTDTQRRLddeEKAAEKLKAEErKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL- 1375
Cdd:pfam10174 304 ELLALQTK---LETLTNQN----SDCKQHI---EVLKESLTAKE-QRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLt 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1376 --KLKMQEEVSKREiAAVDAEKQKTNIqleLQE-LKNLSEQqIKDKSQQVDEalhsrtkieeeirlIRIQLETTEKQKYT 1452
Cdd:pfam10174 373 eeKSTLAGEIRDLK-DMLDVKERKINV---LQKkIENLQEQ-LRDKDKQLAG--------------LKERVKSLQTDSSN 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1453 AESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEK----LRMQAE 1528
Cdd:pfam10174 434 TDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEhassLASSGL 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1529 EAERQVKQAEIEKEK----------QIKVAHEAAQKSAAAElqskhmSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQ 1598
Cdd:pfam10174 514 KKDSKLKSLEIAVEQkkeecsklenQLKKAHNAEEAVRTNP------EINDRIRLLEQEVARYKEESGKAQAEVERLLGI 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1599 QEDAENSREEAEKELEKWRQKAneALRLRLQAEDEAHKKTLAQEEAEKQKEEAErEAKKRAKAEESALKQKEMAE--EEL 1676
Cdd:pfam10174 588 LREVENEKNDKDKKIAELESLT--LRQMKEQNKKVANIKHGQQEMKKKGAQLLE-EARRREDNLADNSQQLQLEElmGAL 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1677 ERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAA---------------QQQRKQLEDELAK 1741
Cdd:pfam10174 665 EKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAaisekdaniallelsSSKKKKTQEEVMA 744
|
490
....*....|
gi 1988774686 1742 VRSEMDILIQ 1751
Cdd:pfam10174 745 LKREKDRLVH 754
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1451-1897 |
2.68e-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: 53.49 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1451 YTAESELKQLRDRAAEaeklrKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEA----EKEAAKQKQKALEDLEKLRMQ 1526
Cdd:pfam05667 91 YPNEPDIRKILMFLVE-----KLPRESSEAADQPVGKSAVLQRAIAAAIRSQLAApwlpPECKPHQRRQGSRALRPFHTQ 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1527 A-EEAERQVKQAEIEKEkqikvaheaaqksaAAELQSKHMSFAE----KTSKLEESLKQEHGAVLQLQQEAERLKKQQED 1601
Cdd:pfam05667 166 TlVLPGRKGKTLKNSKE--------------LKEFYSEYLPPVTaqpsSRASVVPSLLERNAAELAAAQEWEEEWNSQGL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1602 AENSREEAEK--ELEKWRQKANEALRLRLQAEDEAHkktlaqeeaekqkeeaeREAKKRAKAEESALKQKEMAEEELERQ 1679
Cdd:pfam05667 232 ASRLTPEEYRkrKRTKLLKRIAEQLRSAALAGTEAT-----------------SGASRSAQDLAELLSSFSGSSTTDTGL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1680 RKIAESTAQQKLTAEQELIRLRADFDNAEQQrslLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILI----QLKTK 1755
Cdd:pfam05667 295 TKGSRFTHTEKLQFTNEAPAATSSPPTKVET---EEELQQQREEELEELQEQLEDLESSIQELEKEIKKLEssikQVEEE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1756 AEKETMSNTEKSKQ----------LLEAEA--AKMKDLAEEAS-RLRAISEE-AKHQRQIAEE------EAARQRAEAER 1815
Cdd:pfam05667 372 LEELKEQNEELEKQykvkkktldlLPDAEEniAKLQALVDASAqRLVELAGQwEKHRVPLIEEyralkeAKSNKEDESQR 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1816 I------LKEKLAAISEATRLKTEaeiALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIE-EKIVQLKKSSEAEM 1888
Cdd:pfam05667 452 KleeikeLREKIKEVAEEAKQKEE---LYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEiTKILSDTKSLQKEI 528
|
490
....*....|....*.
gi 1988774686 1889 -------ERQKAIVDD 1897
Cdd:pfam05667 529 nsltgklDRTFTVTDE 544
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2447-2579 |
2.78e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.63 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2447 KEMADAQQKKIEHE-KTVLQQTfmtEKEM-LLKKEKLIE--DEKKRLESQFEEEVKKAKalkDEQERQKQQMEQEKKTLQ 2522
Cdd:PRK12704 26 KKIAEAKIKEAEEEaKRILEEA---KKEAeAIKKEALLEakEEIHKLRNEFEKELRERR---NELQKLEKRLLQKEENLD 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774686 2523 ATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLrEKLQQL--EDAQK 2579
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLtaEEAKE 157
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1466-1823 |
2.78e-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: 53.42 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1466 EAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQI 1545
Cdd:pfam15709 164 TPASISHAERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERNL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1546 KVAHEAAQK----SAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQ---------EDAENSREEAEKE 1612
Cdd:pfam15709 244 EVAAELSGPdvinSKETEDASERGAFSSDSVVEDPWLSSKYDAEESQVSIDGRSSPTQtfvvtgnmeSEEERSEEDPSKA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1613 LEKWRQKANEAlRLRLQAEdEAHKKTLAQeeaekqkeeaerEAKKRAKAEESALKQkemaeEELERQRKIAE--STAQQK 1690
Cdd:pfam15709 324 LLEKREQEKAS-RDRLRAE-RAEMRRLEV------------ERKRREQEEQRRLQQ-----EQLERAEKMREelELEQQR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1691 LTAEqelIRLRADFDNAEQQRSllEDELYRLKNEVAAAQQQRKQLEDELAKVrsemdiLIQLKTKAEKETMSNTEKSKQL 1770
Cdd:pfam15709 385 RFEE---IRLRKQRLEEERQRQ--EEEERKQRLQLQAAQERARQQQEEFRRK------LQELQRKKQQEEAERAEAEKQR 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774686 1771 LEAEAAKmkdLAEEASRLRAISEEAK--HQRQIAEEEAARQRAEAERILKEKLAA 1823
Cdd:pfam15709 454 QKELEMQ---LAEEQKRLMEMAEEERleYQRQKQEAEEKARLEAEERRQKEEEAA 505
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1096-1704 |
3.23e-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: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1096 EVHTVPSDVKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAvsdkmvrvHSERDVELDHFRQQLSSLqDRWKAvFT 1175
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAER--------YAAARERLAELEYLRAAL-RLWFA-QR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1176 QIDLRQRELEQLgrqlgyyRESYDWLIRWIADAKQRQEKIQAvpitDSKTLKEQLAQ-----EKKLLEEIEQNKDKVDEC 1250
Cdd:COG4913 289 RLELLEAELEEL-------RAELARLEAELERLEARLDALRE----ELDELEAQIRGnggdrLEQLEREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1251 QKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLK--KTKLDSASDNIIQEYVTLRTRYSELmtltsqyikfiTDTQRRLDD 1328
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAalLEALEEELEALEEALAEAEAALRDL-----------RRELRELEA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1329 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIA-----KAEKEA-----------QELKLKMQEEVSKREIAAVD 1392
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGelievRPEEERwrgaiervlggFALTLLVPPEHYAAALRWVN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1393 AEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTK-----IEEEI--RLIRIQLETTEkqkytaesELKQLRdRAA 1465
Cdd:COG4913 507 RLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHpfrawLEAELgrRFDYVCVDSPE--------ELRRHP-RAI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1466 EAEKLRKLAQDEAEK-LRKQVSEE-------TQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQA 1537
Cdd:COG4913 578 TRAGQVKGNGTRHEKdDRRRIRSRyvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYS 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1538 eiekEKQIKVAheaaqkSAAAELqskhmsfAEKTSKLEEsLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWR 1617
Cdd:COG4913 658 ----WDEIDVA------SAEREI-------AELEAELER-LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1618 QKANEALRLRLQAEDEAHkktlaqEEAEKQKEEAEREAKKRAKAEESALKQKEMAeEELERQRKIAESTAQQkltAEQEL 1697
Cdd:COG4913 720 KELEQAEEELDELQDRLE------AAEDLARLELRALLEERFAAALGDAVERELR-ENLEERIDALRARLNR---AEEEL 789
|
....*..
gi 1988774686 1698 IRLRADF 1704
Cdd:COG4913 790 ERAMRAF 796
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1664-1868 |
3.30e-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: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1664 SALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAK-- 1741
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1742 --------VRSEMDILIQLK---------------TKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKH- 1797
Cdd:COG3883 93 ralyrsggSVSYLDVLLGSEsfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAe 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 1798 -QRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQ 1868
Cdd:COG3883 173 lEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
2404-2574 |
3.40e-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: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2404 VERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKsKEMADAQQKKIEHEKTVLQQTFMTEKEmllKKEKLIE 2483
Cdd:pfam15066 372 VEELIEDKYNVILEKNDINKTLQNLQEILANTQKHLQESRKE-KETLQLELKKIKVNYVHLQERYITEMQ---QKNKSVS 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2484 D--EKKRLESQFEEEVKKAKALKDEQERqkqqmeqekktlqATMDA--ALSKQKEA-EEEMLRKQKEMQELERQRLeqer 2558
Cdd:pfam15066 448 QclEMDKTLSKKEEEVERLQQLKGELEK-------------ATTSAldLLKREKETrEQEFLSLQEEFQKHEKENL---- 510
|
170
....*....|....*.
gi 1988774686 2559 ilaEENQKLREKLQQL 2574
Cdd:pfam15066 511 ---EERQKLKSRLEKL 523
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3701-3735 |
3.49e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.49e-06
10 20 30
....*....|....*....|....*....|....*
gi 1988774686 3701 LLEAQAATGFIVDPLKNETLTVDEAVRKGVVGPEI 3735
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1675-1819 |
3.99e-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: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1675 ELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRS---------E 1745
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyealqkE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774686 1746 MDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKE 1819
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2398-2571 |
4.02e-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: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2398 QEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQ---NKSKEMADAQQKKIEHEKTvLQQTFMTEKEM 2474
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEkeiKRLELEIEEVEARIKKYEE-QLGNVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2475 L-LKKEklIEDEKKRLeSQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAalsKQKEAEEEMLRKQKEMQELERQR 2553
Cdd:COG1579 92 EaLQKE--IESLKRRI-SDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAER 165
|
170
....*....|....*...
gi 1988774686 2554 LEQERILAEENQKLREKL 2571
Cdd:COG1579 166 EELAAKIPPELLALYERI 183
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1724-1879 |
4.38e-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: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1724 EVAAAQQQRKQledELAKVRSEMDILIQLKTKAEKETmsntEKSKQLLEAEAAKMKDLAEEASRLRAIS---------EE 1794
Cdd:COG2268 213 EIAIAQANREA---EEAELEQEREIETARIAEAEAEL----AKKKAEERREAETARAEAEAAYEIAEANaerevqrqlEI 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1795 AKHQRQI--AEEEAARQRAEAERILKEKLAAISEATRLKTEAE----IALKEKEAENERLRRQAEdEAYQRKALEDQASQ 1868
Cdd:COG2268 286 AEREREIelQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEaeaiRAKGLAEAEGKRALAEAW-NKLGDAAILLMLIE 364
|
170
....*....|.
gi 1988774686 1869 HKQEIEEKIVQ 1879
Cdd:COG2268 365 KLPEIAEAAAK 375
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1702-2051 |
4.39e-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: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1702 ADF-DNAEQQRSLLEDELyRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMK- 1779
Cdd:COG3096 271 ADYmRHANERRELSERAL-ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKi 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1780 -----DLAEEASRLRA---ISEEAKHQRQIAEEEAARQRAEAERiLKEKLA---------------------AISEATRL 1830
Cdd:COG3096 350 eryqeDLEELTERLEEqeeVVEEAAEQLAEAEARLEAAEEEVDS-LKSQLAdyqqaldvqqtraiqyqqavqALEKARAL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1831 KTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQ---ASQHKQEIEeKIVQLKKSSEAEMERQKAivDDTLKQrrvVEE 1907
Cdd:COG3096 429 CGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKlsvADAARRQFE-KAYELVCKIAGEVERSQA--WQTARE---LLR 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1908 EIRILKLNFEKASSGKLDL-ELE-----LNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEE 1981
Cdd:COG3096 503 RYRSQQALAQRLQQLRAQLaELEqrlrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSE 582
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 1982 AARQRKAALEELERLRKKAEEARKQKDEADKEAEkQIVVAQQAAQKCSAAEQQV--QSVLAQQIEDSITQKK 2051
Cdd:COG3096 583 LRQQLEQLRARIKELAARAPAWLAAQDALERLRE-QSGEALADSQEVTAAMQQLleREREATVERDELAARK 653
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1366-1637 |
4.52e-06 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 52.77 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1366 AKAEKEAQELKlKMQEEVSKREIAAVDAEKQKTNIQLELQElknlSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLET 1445
Cdd:PRK11637 40 AHASDNRDQLK-SIQQDIAAKEKSVRQQQQQRASLLAQLKK----QEEAISQASRKLRETQNTLNQLNKQIDELNASIAK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1446 TEKQKYTAESELKQLRDRAaeaeklrkLAQDEAEKLRKQVS-EETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLR 1524
Cdd:PRK11637 115 LEQQQAAQERLLAAQLDAA--------FRQGEHTGLQLILSgEESQRGERILAYFGYLNQARQETIAELKQTREELAAQK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1525 MQAEEAERQVKQAEIEKEKQ---IKVAHEAAQKSAAAelqskhmsfaektskLEESLKQEHGAVLQLQQEAERLKKQQED 1601
Cdd:PRK11637 187 AELEEKQSQQKTLLYEQQAQqqkLEQARNERKKTLTG---------------LESSLQKDQQQLSELRANESRLRDSIAR 251
|
250 260 270
....*....|....*....|....*....|....*..
gi 1988774686 1602 AE-NSREEAEKElekwrqkANEALRLRlQAEDEAHKK 1637
Cdd:PRK11637 252 AErEAKARAERE-------AREAARVR-DKQKQAKRK 280
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1817-2589 |
4.58e-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: 53.13 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1817 LKEKLAAISEATRLKTEAEIALKEKEAENERLRrqaedEAYQRKALEDQASQHKQEIEEKIV--QLKKSSEAEMERQKAI 1894
Cdd:TIGR00606 171 LKQKFDEIFSATRYIKALETLRQVRQTQGQKVQ-----EHQMELKYLKQYKEKACEIRDQITskEAQLESSREIVKSYEN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1895 VDDTLKQRRVVEEEIRilklnfekasSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLrklaleeekrRREAEEKVKK 1974
Cdd:TIGR00606 246 ELDPLKNRLKEIEHNL----------SKIMKLDNEIKALKSRKKQMEKDNSELELKMEKV----------FQGTDEQLND 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1975 IAAAEEEAARQRKAAL----EELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQK 2050
Cdd:TIGR00606 306 LYHNHQRTVREKERELvdcqRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2051 KLKEeyekakklakeaeaaKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfEAAKRAQAEAAAL 2130
Cdd:TIGR00606 386 PFSE---------------RQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKK-GLGRTIELKKEIL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2131 MQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSV---LDEE--LQRLKDEVDDAVKQRGQVEEELFK 2205
Cdd:TIGR00606 450 EKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTetlKKEVksLQNEKADLDRKLRKLDQEMEQLNH 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2206 VKVQMEELLKLKNKIEEENQRLIKKDKDSTQKL--LAEEAENMRKLAEDAARLSVEAQ-----------EAARLRQIAED 2272
Cdd:TIGR00606 530 HTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELtsLLGYFPNKKQLEDWLHSKSKEINqtrdrlaklnkELASLEQNKNH 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2273 DLNQQRALAEKMLK--EKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYH-------KSLEV 2343
Cdd:TIGR00606 610 INNELESKEEQLSSyeDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqRVFQT 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2344 ERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRK 2423
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2424 AIADLENEKARLKKeAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEML------LKKEKLIEDEKKRLESQFEEEV 2497
Cdd:TIGR00606 770 QETLLGTIMPEEES-AKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLdrtvqqVNQEKQEKQHELDTVVSKIELN 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2498 KKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELER---QRLEQERILAEENQKLREKLQQL 2574
Cdd:TIGR00606 849 RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIReikDAKEQDSPLETFLEKDQQEKEEL 928
|
810
....*....|....*
gi 1988774686 2575 EDAQKDQHTRETDKV 2589
Cdd:TIGR00606 929 ISSKETSNKKAQDKV 943
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1323-1551 |
4.91e-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: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1323 QRRLDDEEKAAEKLKA--EERKKMAEMQAELDKQ-KQLAEAHAKAIAKAEKEAQELKLKMQEEVSK---REIAAVDAEKQ 1396
Cdd:pfam13868 65 EERKEERKRYRQELEEqiEEREQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKLEKQRQLREeidEFNEEQAEWKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1397 KTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESElkQLRDRAAEAEKLRKLAQD 1476
Cdd:pfam13868 145 LEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERD--ELRAKLYQEEQERKERQK 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774686 1477 EAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEA 1551
Cdd:pfam13868 223 EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK 297
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1658-1833 |
4.98e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1658 RAKAEESALKQKEMAEEELERQRKIAESTAQQKLT-AEQELIRLRADFDNAEQQRsllEDELYRLKNEVaaaQQQRKQLE 1736
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELRER---RNELQKLEKRL---LQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1737 DELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDL-------AEEASR--LRAISEEAKHQRQI----AE 1803
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELerisgltAEEAKEilLEKVEEEARHEAAVlikeIE 179
|
170 180 190
....*....|....*....|....*....|.
gi 1988774686 1804 EEAarqRAEAERILKEKLA-AIseaTRLKTE 1833
Cdd:PRK12704 180 EEA---KEEADKKAKEILAqAI---QRCAAD 204
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1584-1823 |
5.29e-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: 52.07 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1584 AVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEE 1663
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1664 SALKQKEMAEEELERQRKIAESTAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVR 1743
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQ---PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1744 SEMDILIQLKT--KAEKETMSNTEKSKQLLEAEAAkmKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKL 1821
Cdd:COG4942 171 AERAELEALLAelEEERAALEALKAERQKLLARLE--KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
..
gi 1988774686 1822 AA 1823
Cdd:COG4942 249 AA 250
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1504-1871 |
5.35e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.56 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1504 EAEKEAAKQK-QKALEDLEKLRmQAEEAERQVKQAEIEKEKQIkVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQeh 1582
Cdd:pfam02029 2 EDEEEAARERrRRAREERRRQK-EEEEPSGQVTESVEPNEHNS-YEEDSELKPSGQGGLDEEEAFLDRTAKREERRQK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1583 gavlQLQQEAERLKKQQED--------AENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTlaqeeaekqkeeaeRE 1654
Cdd:pfam02029 78 ----RLQEALERQKEFDPTiadekesvAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIRE--------------KE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1655 AKKRAKAEEsalkQKEMAEEELERQRKIAESTAQQKltaeqelirlraDFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQ 1734
Cdd:pfam02029 140 YQENKWSTE----VRQAEEEGEEEEDKSEEAEEVPT------------ENFAKEEVKDEKIKKEKKVKYESKVFLDQKRG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1735 LEDELAKVRSEMDILIQLKTKAEKETMSNT----EKSKQLLEAEAAKmkdlaEEASRLRAISE----EAKHQRQiaeEEA 1806
Cdd:pfam02029 204 HPEVKSQNGEEEVTKLKVTTKRRQGGLSQSqereEEAEVFLEAEQKL-----EELRRRRQEKEseefEKLRQKQ---QEA 275
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 1807 ARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERL------RRQAEDEAYQRKALEDQASQHKQ 1871
Cdd:pfam02029 276 ELELEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRmkeeieRRRAEAAEKRQKLPEDSSSEGKK 346
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
19-118 |
5.50e-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: 48.42 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 19 DRVQKKTFTKWVNKHLIKA--QRHVTDLYEDLRDGHNLISLLEVLSGETLPREKG--RMRFHKLQNVQIALDFLRHRQVK 94
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 1988774686 95 LVNIRNDDIADGNPKLTLGLIWTI 118
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2231-2445 |
5.59e-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: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2231 DKDSTQKLLAEEAENMRKLaEDAARLSVEAQE-AARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQK 2309
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL-ERAHEALEDAREqIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2310 DLAQEQAQKLLEDKQLMQQRLEEETEEYhksLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATR 2389
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREEL---DELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2390 LHETEIATQEK----MTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNK 2445
Cdd:COG4913 375 LPASAEEFAALraeaAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2479-2584 |
5.71e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2479 EKLIEDEKKRLESQFEEEVKKAKalkDEQERQKQQMEQEKKTLQATMdAALSKQKEAEEEMLRKQKEMQELERQRLE-QE 2557
Cdd:PRK12704 41 KRILEEAKKEAEAIKKEALLEAK---EEIHKLRNEFEKELRERRNEL-QKLEKRLLQKEENLDRKLELLEKREEELEkKE 116
|
90 100
....*....|....*....|....*..
gi 1988774686 2558 RILAEENQKLREKLQQLEDAQKDQHTR 2584
Cdd:PRK12704 117 KELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1481-1660 |
6.01e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1481 LRKQVSEetQKKRQAEEELKR-KSEAEKEAAKQKQKAL----EDLEKLRmqaEEAERQVKQAEIE---KEKQIKVAHEA- 1551
Cdd:PRK12704 24 VRKKIAE--AKIKEAEEEAKRiLEEAKKEAEAIKKEALleakEEIHKLR---NEFEKELRERRNElqkLEKRLLQKEENl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1552 AQKSAAAELQSKHMsfaektSKLEESLKQEHGAVLQLQQEAERLKKQQED-----AENSREEAEKE-LEKWRQKA-NEAL 1624
Cdd:PRK12704 99 DRKLELLEKREEEL------EKKEKELEQKQQELEKKEEELEELIEEQLQeleriSGLTAEEAKEIlLEKVEEEArHEAA 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 1988774686 1625 RLRLQAEDEAHKktlaqeeaekqkeeaerEAKKRAK 1660
Cdd:PRK12704 173 VLIKEIEEEAKE-----------------EADKKAK 191
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
601-693 |
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 1988774686 601 HAFVSAATKELMWLNDKEEEEVNFDWSDRNTNMTAKKDNYSGLMRELELREKKVNDIQALGDRLVRDGHPGKKTVESFTA 680
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1988774686 681 ALQTQWSWILQLC 693
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1354-1546 |
6.68e-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: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1354 QKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREiAAVDAEKQKTNIqLELQELKNLSEQQIKDKSQQVDEALHSRTKIE 1433
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAE-AALEEFRQKNGL-VDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1434 EEIRLIRIQLETTEKQKYT--AESELKQLRDRAAEAE-KLRKLAQD------EAEKLRKQVSEETQKKRQAEEELKRKSE 1504
Cdd:COG3206 240 ARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEaELAELSARytpnhpDVIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1988774686 1505 AEKEAAKQKQKALED-LEKLRMQAEE-AERQVKQAEIEKEKQIK 1546
Cdd:COG3206 320 AELEALQAREASLQAqLAQLEARLAElPELEAELRRLEREVEVA 363
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1404-1814 |
6.78e-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: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1404 LQELKNLSEQQIK---DKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEK 1480
Cdd:pfam05622 26 LQEEKNSLQQENKklqERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1481 LRKQVSEETQKK------RQAEEELKrKSEAEKEAAKQKqkaLEDLEKLRMQA---EEAERQVKQAEIEKEKQIKVA--- 1548
Cdd:pfam05622 106 LTSLAEEAQALKdemdilRESSDKVK-KLEATVETYKKK---LEDLGDLRRQVkllEERNAEYMQRTLQLEEELKKAnal 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1549 --HEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQedaENSREeaekelekwrqkANEALRL 1626
Cdd:pfam05622 182 rgQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIER---DTLRE------------TNEELRC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1627 RLQAEDEAHKKTLAQEEAEKQKEEAEREakkrakaeesaLKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDN 1706
Cdd:pfam05622 247 AQLQQAELSQADALLSPSSDPGDNLAAE-----------IMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLED 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1707 AEQQRSLLEDELyRLKNE-VAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEketmsntEKSKQLLEAEAAKMKdlAEEA 1785
Cdd:pfam05622 316 ANRRKNELETQN-RLANQrILELQQQVEELQKALQEQGSKAEDSSLLKQKLE-------EHLEKLHEAQSELQK--KKEQ 385
|
410 420
....*....|....*....|....*....
gi 1988774686 1786 SRLRAISEEAKHQRQIAEEEAARQRAEAE 1814
Cdd:pfam05622 386 IEELEPKQDSNLAQKIDELQEALRKKDED 414
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2177-2448 |
6.85e-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: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2177 VLDEelQRLKDEVDDAVKQRGQ---VEEELFKVKVQMEELLKlknkIEEENQRLikkdkdstqkllAEEAENMRKLAEDA 2253
Cdd:COG4913 217 MLEE--PDTFEAADALVEHFDDlerAHEALEDAREQIELLEP----IRELAERY------------AAARERLAELEYLR 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2254 ARLSV-EAQEAARLRQIAEDDLNQQRALAEKmlkEKMQAIQEASRLKAEAEMLQKQKDLAQ----EQAQKLLEDKQLMQQ 2328
Cdd:COG4913 279 AALRLwFAQRRLELLEAELEELRAELARLEA---ELERLEARLDALREELDELEAQIRGNGgdrlEQLEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2329 RLEEETEEYHKSLeveRKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLE 2408
Cdd:COG4913 356 ERERRRARLEALL---AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1988774686 2409 FERLNTSKEADDLRKAIAD-LENEKARLKKEAEELQNKSKE 2448
Cdd:COG4913 433 RRKSNIPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3901-3939 |
7.01e-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: 7.01e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1988774686 3901 YLQGTGCIAGVFLESTKERLSIYQAMKKNMIRPGTAFEL 3939
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1663-1896 |
8.05e-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: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1663 ESALKQKEMAEEELERQRKIAEsTAQQKLTA---EQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDEL 1739
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1740 AKVRSEMDILIQLKTKAEKETmsntekskQLLEAEAakmkDLAEEASRLRaiseeAKHQRQIAeeeAARQRAEAERILKE 1819
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRA--------QLAELEA----ELAELSARYT-----PNHPDVIA---LRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1820 KLAAISEAtrLKTEAEiALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIE--EKIVQ--LKKSSEAEMERQKAIV 1895
Cdd:COG3206 310 EAQRILAS--LEAELE-ALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEvaRELYEslLQRLEEARLAEALTVG 386
|
.
gi 1988774686 1896 D 1896
Cdd:COG3206 387 N 387
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1413-1682 |
8.18e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1413 QQIKDKSQQVDEALHSRTKIEEEIRLIRIQLET--TEKQKYTAE-----SELKQLRDRAAEAEKLRKLAQDEAEKLRKQV 1485
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDElnEELKELAEKrdelnAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1486 SEETQKKRQAEEELKRKSEAEKEAA------KQKQKALEDLEKlRMQAE----EAERQV--KQAEIEKE-KQIKVAHEAA 1552
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNkaggsiDKLRKEIERLEW-RQQTEvlspEEEKELveKIKELEKElEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1553 QK-----SAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRlR 1627
Cdd:COG1340 160 EKlkelrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK-E 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774686 1628 LQAEDEAHKKTLAQEeaekqkeeaerEAKKRAKAEESALKQKEMAEEELERQRKI 1682
Cdd:COG1340 239 LRELRKELKKLRKKQ-----------RALKREKEKEELEEKAEEIFEKLKKGEKL 282
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1429-1957 |
8.53e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.21 E-value: 8.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1429 RTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKlAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKE 1508
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKS-SNLELENIKKQIADDEKSHSITLKEIERLSIEYNN 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1509 AAKQKQKALEDLEKLRMQAEEAERqvkqaeiekekqikvaHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQL 1588
Cdd:PRK01156 230 AMDDYNNLKSALNELSSLEDMKNR----------------YESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1589 QQEAERLKKQQEDAENSREEAEKelekwrqkaneaLRLRLQAEDEAHKKtLAQEEAEKQKEEAEREAKKRAKAEESALKQ 1668
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSN------------IDAEINKYHAIIKK-LSVLQKDYNDYIKKKSRYDDLNNQILELEG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1669 KEMAEEELER-----QRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLED---ELYRLKNEVAAAQQQRKQLEDELA 1740
Cdd:PRK01156 361 YEMDYNSYLKsieslKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEinvKLQDISSKVSSLNQRIRALRENLD 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1741 KVRSEMDILIQLKTKAEKETMSNTEKSKQLLEaeaakmkDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEK 1820
Cdd:PRK01156 441 ELSRNMEMLNGQSVCPVCGTTLGEEKSNHIIN-------HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1821 LAAISEATRLKTEAE-----IALKEKEAENERLRRQAEDEAYQRKALEDQASQHkqeiEEKIVQLKKSSEAEMERQKAIV 1895
Cdd:PRK01156 514 INKSINEYNKIESARadledIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKR----TSWLNALAVISLIDIETNRSRS 589
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774686 1896 DDTLKQRRVVEEEIRILKLNFEKASS----GKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKL 1957
Cdd:PRK01156 590 NEIKKQLNDLESRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNY 655
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2416-2575 |
8.77e-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: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2416 KEADDLRKAIADLENEKARLKKEAEELQNKSKEmADAQQKKIEHEktvlqqtfmtekemLLKKEKLIEDEKKRLESqfee 2495
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELED-LEKEIKRLELE--------------IEEVEARIKKYEEQLGN---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2496 eVKKAKALK------DEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLRE 2569
Cdd:COG1579 85 -VRNNKEYEalqkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*.
gi 1988774686 2570 KLQQLE 2575
Cdd:COG1579 164 EREELA 169
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1100-1274 |
9.14e-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: 49.75 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1100 VPSDVKEVETYRAKLKKMRTEAEDEQPVFDSLEEElkkasavSDKMVRVHSERDVELdhfRQQLSSLQDRWKAVFTQIDL 1179
Cdd:cd00176 28 YGDDLESVEALLKKHEALEAELAAHEERVEALNEL-------GEQLIEEGHPDAEEI---QERLEELNQRWEELRELAEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1180 RQRELEQLGRQLGYYRESYDwLIRWIADAKQRQEKIQavPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYID 1259
Cdd:cd00176 98 RRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLE 174
|
170
....*....|....*
gi 1988774686 1260 TIKDYELQLVAYKAQ 1274
Cdd:cd00176 175 EGHPDADEEIEEKLE 189
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1442-1868 |
9.64e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.83 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1442 QLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLE 1521
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1522 KLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQED 1601
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1602 AENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRK 1681
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1682 IAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDElyrlknevAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETM 1761
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAE--------AVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEAL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1762 SNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEK 1841
Cdd:COG5278 423 ELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLA 502
|
410 420
....*....|....*....|....*..
gi 1988774686 1842 EAENERLRRQAEDEAYQRKALEDQASQ 1868
Cdd:COG5278 503 LALAALLLAAAEAALAAALAAALASAE 529
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1384-1556 |
1.15e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1384 SKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDksqqvdEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQlrdr 1463
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKE------EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1464 aaeaeKLRKLaqdeaEKLRKQVSEETQKKRQAEEELKRKseaEKEAAKQKQKALEDLEKL-RMQAEEAERQV-----KQA 1537
Cdd:PRK12704 101 -----KLELL-----EKREEELEKKEKELEQKQQELEKK---EEELEELIEEQLQELERIsGLTAEEAKEILlekveEEA 167
|
170
....*....|....*....
gi 1988774686 1538 EIEKEKQIKVAHEAAQKSA 1556
Cdd:PRK12704 168 RHEAAVLIKEIEEEAKEEA 186
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2479-2587 |
1.17e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2479 EKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTlqatmdaalskqkEAEEEMLRKQKEMQELERQRLEQER 2558
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRN-------------EFEKELRERRNELQKLEKRLLQKEE 96
|
90 100
....*....|....*....|....*....
gi 1988774686 2559 ILAEENQKLREKLQQLEDAQKDQHTRETD 2587
Cdd:PRK12704 97 NLDRKLELLEKREEELEKKEKELEQKQQE 125
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1986-2441 |
1.24e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1986 RKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSvLAQQIEDSITQKKLKEEYEKAKKLAKE 2065
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2066 AEAAKEKAEReaalLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfeaakraqaeaaalmqkqqadtemAKHKK 2145
Cdd:COG4717 127 LLPLYQELEA----LEAELAELPERLEELEERLEELRELEEELEELEAELA------------------------ELQEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2146 LAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELfkvkvqmeELLKLKNKIEEENQ 2225
Cdd:COG4717 179 LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL--------EAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2226 RLI------------KKDKDSTQK----------LLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRA---- 2279
Cdd:COG4717 251 LLLiaaallallglgGSLLSLILTiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAalgl 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2280 ---LAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKlledKQLMQQRLEEETEEYHKSLEVERKRQlEIMAEAE 2356
Cdd:COG4717 331 ppdLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI----AALLAEAGVEDEEELRAALEQAEEYQ-ELKEELE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2357 RLRLQVSQLSEAQARAEEEAKKF--KKQADKVATRLHETEIATQEKMTVVERLEfERLNTSKEADDLRKAIADLENEKAR 2434
Cdd:COG4717 406 ELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELE-AELEQLEEDGELAELLQELEELKAE 484
|
....*..
gi 1988774686 2435 LKKEAEE 2441
Cdd:COG4717 485 LRELAEE 491
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2216-2578 |
1.25e-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: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2216 LKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEdaARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEA 2295
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLH--GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2296 SRLKAEAEMLQKQKDLAQEQAQKlleDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSeaqaraeee 2375
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKK---QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVT--------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2376 akKFKKQADKVATRLheteiatQEKMTVVERLEFERLNTSKEADDL---RKAIADLENEKARLKKEAEElQNKSKEMADA 2452
Cdd:TIGR00618 304 --QIEQQAQRIHTEL-------QSKMRSRAKLLMKRAAHVKQQSSIeeqRRLLQTLHSQEIHIRDAHEV-ATSIREISCQ 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2453 QQKKIEHEKTVLQQtfmteKEMLLKKEKLIedekKRLESQFEEEVKKAKALKDEQERQKQQMeqekktlqatmdAALSKQ 2532
Cdd:TIGR00618 374 QHTLTQHIHTLQQQ-----KTTLTQKLQSL----CKELDILQREQATIDTRTSAFRDLQGQL------------AHAKKQ 432
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1988774686 2533 KEAEEEMLRKQKEMQELERQRLEQERILAEE-NQKLREKLQQLEDAQ 2578
Cdd:TIGR00618 433 QELQQRYAELCAAAITCTAQCEKLEKIHLQEsAQSLKEREQQLQTKE 479
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2234-2577 |
1.28e-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: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2234 STQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQ-QRALAekmLKEKMQAIQE-----ASRLkAEAEMLQK 2307
Cdd:COG3096 296 GARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLvQTALR---QQEKIERYQEdleelTERL-EEQEEVVE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2308 QKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQ------LEIMAEAERLrLQVSQLSEAQARAEEEAkkFKK 2381
Cdd:COG3096 372 EAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiqyqqaVQALEKARAL-CGLPDLTPENAEDYLAA--FRA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2382 QADKV-------ATRLHETEIATQE---KMTVVERL--EFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEM 2449
Cdd:COG3096 449 KEQQAteevlelEQKLSVADAARRQfekAYELVCKIagEVERSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2450 AdaQQKKIEHEKTVLQQTFMTEkemlLKKEKLIEDEKKRLESQFEE---EVKKAKALKDEQERQKQQMEQEKKTLQA--- 2523
Cdd:COG3096 529 R--QQQNAERLLEEFCQRIGQQ----LDAAEELEELLAELEAQLEEleeQAAEAVEQRSELRQQLEQLRARIKELAArap 602
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774686 2524 ---TMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDA 2577
Cdd:COG3096 603 awlAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQ 659
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2265-2592 |
1.35e-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: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2265 RLRQIAEDDLNQQRALAEKMLKEKMQAIQE---ASRLKAEAEMLQKQKDLAqEQAQKLLEDKQLMQQRLEEETEEY---- 2337
Cdd:NF033838 92 KLSDIKTEYLYELNVLKEKSEAELTSKTKKeldAAFEQFKKDTLEPGKKVA-EATKKVEEAEKKAKDQKEEDRRNYptnt 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2338 HKSLEVERKRQLEIMAEAERlrlqvsQLSEAQARAEEEAKKFKKQADKVATRlheteiatQEKMTVVERLEFERlntsKE 2417
Cdd:NF033838 171 YKTLELEIAESDVEVKKAEL------ELVKEEAKEPRDEEKIKQAKAKVESK--------KAEATRLEKIKTDR----EK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2418 ADDLRKAIADLENEKARLKKEAEELQNKSKEMA--------DAQQKKIEHEKT----VLQQTFMTEKemlLKKEKLI-ED 2484
Cdd:NF033838 233 AEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAkrgvlgepATPDKKENDAKSsdssVGEETLPSPS---LKPEKKVaEA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2485 EKKRLESQfeeevKKAKALKDEQERQKQQMEQekKTLQATMDAALSKQKEAEEEMLRKQ-KEMQELERQRLEQERILAEE 2563
Cdd:NF033838 310 EKKVEEAK-----KKAKDQKEEDRRNYPTNTY--KTLELEIAESDVKVKEAELELVKEEaKEPRNEEKIKQAKAKVESKK 382
|
330 340 350
....*....|....*....|....*....|...
gi 1988774686 2564 NQKLR-EKLQQLEDAQKDQHTR---ETDKVLHK 2592
Cdd:NF033838 383 AEATRlEKIKTDRKKAEEEAKRkaaEEDKVKEK 415
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2415-2548 |
1.37e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.37 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2415 SKEADDLRKAIADLENEKARLKKEAEELQNKSKEmadAQQKKiehektvlqqtfmteKEMLLKKEKLIEDEKK---RLES 2491
Cdd:PRK00409 512 GEDKEKLNELIASLEELERELEQKAEEAEALLKE---AEKLK---------------EELEEKKEKLQEEEDKlleEAEK 573
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 2492 QFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDA-----ALSKQKEAEEEMLRKQKEMQE 2548
Cdd:PRK00409 574 EAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELiearkRLNKANEKKEKKKKKQKEKQE 635
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
21-122 |
1.39e-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: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 21 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRF----HKLQNVQIALDFLRHRQVKLV 96
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 1988774686 97 NIRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1667-1954 |
1.41e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1667 KQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEM 1746
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1747 DILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQ----IAEEEAARQRAEAERILKEKLA 1822
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEelaaLEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1823 AISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQR 1902
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 1903 RVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKL 1954
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1323-1537 |
1.42e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.37 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1323 QRRLDDEEKAAEKLKAEERKKMAEMQaelDKQKQLAEAHAKAIAKAEKEAQElKLKMqeevSKREIAAVDAEKQktniQL 1402
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELE---EKKEKLQEEEDKLLEEAEKEAQQ-AIKE----AKKEADEIIKELR----QL 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1403 ELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYtaeSELKQlrdraaEAEKLRKLAQDEAeklr 1482
Cdd:PRK00409 597 QKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEVKY---LSLGQ------KGEVLSIPDDKEA---- 663
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 1483 kQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEK------LR-MQAEEAERQVKQA 1537
Cdd:PRK00409 664 -IVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTvsleldLRgMRYEEALERLDKY 724
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1227-1875 |
1.48e-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: 51.56 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1227 KEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKK-----TKLDSASDNIIQEyvtl 1301
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKnkdkiNKLNSDLSKINSE---- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1302 rtryselmtltsqyIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL---KLK 1378
Cdd:TIGR04523 112 --------------IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELeneLNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1379 MQEEVSKREIAAVDAEKQKTNIQLELQELKNLsEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELK 1458
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK-IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1459 QLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAE---EELKRKSEAE-----KEAAKQKQKALEDLEKLRMQAEEA 1530
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKseiSDLNNQKEQDwnkelKSELKNQEKKLEEIQNQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1531 ERQVKQaEIEKEKQikvaheaaqksaaaELQSKHMSFAEKTSKLEESlkqehgavlqlQQEAERLKKQQEDAENSREEAE 1610
Cdd:TIGR04523 337 ISQLNE-QISQLKK--------------ELTNSESENSEKQRELEEK-----------QNEIEKLKKENQSYKQEIKNLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1611 KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK 1690
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1691 LTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMS-------- 1762
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDledelnkd 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1763 NTEKSKQLLEAEaakMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEklaaISEATRLKTEAEIALKEKE 1842
Cdd:TIGR04523 551 DFELKKENLEKE---IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE----IEEKEKKISSLEKELEKAK 623
|
650 660 670
....*....|....*....|....*....|...
gi 1988774686 1843 AENERLRRQAEDEAYQRKALEDQASQHKQEIEE 1875
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1555-1814 |
1.51e-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: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1555 SAAAELQSKHMSFAEKTSKLEESLKQehgaVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAlrlrlQAEDEA 1634
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-----EAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1635 HKKTLaqeeaekqkeeaereaKKRAKAE-------------------ESALKQKEMAEEELERQRKIAESTAQQKLTAEQ 1695
Cdd:COG3883 84 RREEL----------------GERARALyrsggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1696 ELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEA 1775
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 1988774686 1776 AKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAE 1814
Cdd:COG3883 228 AAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1306-1563 |
1.66e-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: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1306 SELMTLTSQYIKFITD---TQRRLDDEEKAaeklkAEERKKMaemqaELDKQKQLAeahakAIAKAEKEAQELKLKMQEE 1382
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERA-----EADRQRL-----EQEKQQQLA-----AISGSQSQLESTDQNALET 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1383 VSKREIAAVDAEKQKTNIQLE--LQELKNLSEQQ-----------------IKDKSQ-QVDEA-LHSRTKIEEeirliri 1441
Cdd:NF012221 1603 NGQAQRDAILEESRAVTKELTtlAQGLDALDSQAtyagesgdqwrnpfaggLLDRVQeQLDDAkKISGKQLAD------- 1675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1442 qlettEKQKYTAesELKQLRDRAAEAEKlrklAQDEAEKLRKQVSEETQKKR-QAEeelKRKSEA---EKEAAKQKQKAL 1517
Cdd:NF012221 1676 -----AKQRHVD--NQQKVKDAVAKSEA----GVAQGEQNQANAEQDIDDAKaDAE---KRKDDAlakQNEAQQAESDAN 1741
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1988774686 1518 EDLEKLRMQaeeAERQVKQAEIEKEKqikvaheaAQKSAAAELQSK 1563
Cdd:NF012221 1742 AAANDAQSR---GEQDASAAENKANQ--------AQADAKGAKQDE 1776
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
17-125 |
1.66e-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: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 17 ERDRVQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEV---------LSGETLPREKGRMRfhKLQNVQIALDF 87
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1988774686 88 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQVS 125
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1411-1957 |
1.66e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1411 SEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQdEAEKLRKQVSEETQ 1490
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIK-TAESDLSMELEKNN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1491 KKRQAEEELKRkseAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAeiekEKQIKVAHEAAQKsaAAELQSKHMSFAEK 1570
Cdd:PRK01156 274 YYKELEERHMK---IINDPVYKNRNYINDYFKYKNDIENKKQILSNI----DAEINKYHAIIKK--LSVLQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1571 TSKLEE------SLKQEHGAVLQLQQEAERLKKQqedaensREEAEKELEKWRQKANEALRLRLQAEDE--AHKKTLAQE 1642
Cdd:PRK01156 345 KSRYDDlnnqilELEGYEMDYNSYLKSIESLKKK-------IEEYSKNIERMSAFISEILKIQEIDPDAikKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1643 EAEKQKEEAEREAKKRakaeesALKQKEMaeeELERQRKIAESTAQQKLT----AEQELIRLRADFDNaeqQRSLLEDEL 1718
Cdd:PRK01156 418 LQDISSKVSSLNQRIR------ALRENLD---ELSRNMEMLNGQSVCPVCgttlGEEKSNHIINHYNE---KKSRLEEKI 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1719 YRLKNEVAAAQQQRKQLE--------DELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRA 1790
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKkrkeylesEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1791 ISEE---AKHQRQIAEEEAARQRAEaerilkEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAY----QRKALE 1863
Cdd:PRK01156 566 KRTSwlnALAVISLIDIETNRSRSN------EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANnlnnKYNEIQ 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1864 DQASQhKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRvVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQS 1943
Cdd:PRK01156 640 ENKIL-IEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIND-IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDR 717
|
570
....*....|....
gi 1988774686 1944 KIRAEEEAEKLRKL 1957
Cdd:PRK01156 718 INDINETLESMKKI 731
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2290-2578 |
1.77e-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: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2290 QAIQEASRLKAEAEMLqKQKDLAQEQAQKLLEDKQLMQQRLEEET--EEYHKSLEVERKRQLEIM---------AEAERL 2358
Cdd:COG3206 75 SLSASDSPLETQIEIL-KSRPVLERVVDKLNLDEDPLGEEASREAaiERLRKNLTVEPVKGSNVIeisytspdpELAAAV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2359 ------RLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEkmtvverleFER----LNTSKEADDLRKAIADL 2428
Cdd:COG3206 154 analaeAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE---------FRQknglVDLSEEAKLLLQQLSEL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2429 ENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEkemLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQE 2508
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ---LRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774686 2509 RQKQQMEQEKKTLQATMDAALSKQKeAEEEMLRKQ--------KEMQELERQRLEQERILAEENQKLREKLQQLEDAQ 2578
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAELEALQ-AREASLQAQlaqlearlAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1105-1633 |
1.89e-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: 51.33 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1105 KEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKA--------------SAVSDKM----VRVHSERD---VELDHFRQQL 1163
Cdd:pfam01576 517 RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLqrelealtqqleekAAAYDKLektkNRLQQELDdllVDLDHQRQLV 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1164 SSLQDRWKavftQIDLRQRELEQLGRQLGYYRESydwlirwiADAKQRQEKIQAVPITdsktlkeqlaqekKLLEEIEQN 1243
Cdd:pfam01576 597 SNLEKKQK----KFDQMLAEEKAISARYAEERDR--------AEAEAREKETRALSLA-------------RALEEALEA 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1244 KDKVDECQKYAKAYIDtikdyelQLVAYKAQVEPLVSPLKKTKldSASDNIIQEyvtLRTRYSElmtltsqyikfitdtq 1323
Cdd:pfam01576 652 KEELERTNKQLRAEME-------DLVSSKDDVGKNVHELERSK--RALEQQVEE---MKTQLEE---------------- 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1324 rrLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKA-EKEAQELKLKMQEEVSKREIAAvdAEKQKtnIQL 1402
Cdd:pfam01576 704 --LEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQlVKQVRELEAELEDERKQRAQAV--AAKKK--LEL 777
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1403 ELQELknlsEQQIKDKSQQVDEALHSRTKIE----------EEIRLIR----IQLETTEKQKYTAESELKQLRDRAAEAE 1468
Cdd:pfam01576 778 DLKEL----EAQIDAANKGREEAVKQLKKLQaqmkdlqrelEEARASRdeilAQSKESEKKLKNLEAELLQLQEDLAASE 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1469 KLRKLAQDEAEKLRKQVSEETQKKRQAEEElKRKSEAEkeaAKQKQKALEDLE-KLRMQAEEAERQVKQAE-IEKEKQIK 1546
Cdd:pfam01576 854 RARRQAQQERDELADEIASGASGKSALQDE-KRRLEAR---IAQLEEELEEEQsNTELLNDRLRKSTLQVEqLTTELAAE 929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1547 VAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEH-GAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALr 1625
Cdd:pfam01576 930 RSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFkSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVL- 1008
|
....*...
gi 1988774686 1626 lrLQAEDE 1633
Cdd:pfam01576 1009 --LQVEDE 1014
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
2258-2565 |
1.91e-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: 51.10 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2258 VEAQEAARLRQIAEDDLNQQRAlaekmlkekmQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLE--DKQLMQQR--LEEE 2333
Cdd:pfam15818 10 LEALEELRMRREAETQYEEQIG----------KIIVETQELKWQKETLQNQKETLAKQHKEAMAvfKKQLQMKMcaLEEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2334 TEEYHKSLEVERKrqlEIMAEAERLR-LQVSQLSEAQARAEEEAKKfkkQADKVATRLHETEIATQEK--MTVVERLEFE 2410
Cdd:pfam15818 80 KGKYQLATEIKEK---EIEGLKETLKaLQVSKYSLQKKVSEMEQKL---QLHLLAKEDHHKQLNEIEKyyATITGQFGLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2411 RLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEhEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLE 2490
Cdd:pfam15818 154 KENHGKLEQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIK-SKVTCQYKMGEENINLTIKEQKFQELQERLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2491 SQFEEEVKKAKALKDEQERQK---------QQMEQEKKTLQATMDAALSKQKEaEEEMLRKQKEMQElERQRLEQERILA 2561
Cdd:pfam15818 233 MELELNKKINEEITHIQEEKQdiiisfqhmQQLLQQQTQANTEMEAELKALKE-NNQTLERDNELQR-EKVKENEEKFLN 310
|
....
gi 1988774686 2562 EENQ 2565
Cdd:pfam15818 311 LQNE 314
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1323-1548 |
1.93e-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: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1323 QRRLDDEEKAAEKLK----AEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEevskreiaavdAEKQKT 1398
Cdd:pfam09787 17 ARILQSKEKLIASLKegsgVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE-----------LEAQQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1399 NIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRiqlETTEKQKYTAESELKQLrdraaeaeklrklaQDEA 1478
Cdd:pfam09787 86 EEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLE---EELRRSKATLQSRIKDR--------------EAEI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774686 1479 EKLRKQVSEETQKKRQaEEELKRKSEAEKEAAKQKQKALEDL--EK--LRMQAEEAERQVKQAEIEKEKQIKVA 1548
Cdd:pfam09787 149 EKLRNQLTSKSQSSSS-QSELENRLHQLTETLIQKQTMLEALstEKnsLVLQLERMEQQIKELQGEGSNGTSIN 221
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2250-2461 |
1.94e-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: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2250 AEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQR 2329
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2330 LEEETEEYhksleVERKRQLEIMAEAERLRLQVSQ------------LSEAQARAEEEAKKFKKQADKVATRLHETEIAT 2397
Cdd:COG4942 99 LEAQKEEL-----AELLRALYRLGRQPPLALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774686 2398 QEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEK 2461
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1433-1623 |
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: 50.21 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1433 EEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQ 1512
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1513 KQKALEDLEKL--------------RMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSkhmsFAEKTSKLEESL 1578
Cdd:COG3883 95 LYRSGGSVSYLdvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1988774686 1579 KQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEA 1623
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1328-1580 |
2.02e-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: 50.72 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1328 DEEKAAEKLKAEERKKMAEMQAELDKQKQLAEahakaiAKAEKEAQELKLKMQEEvskreiaavdaekqktniqLELqel 1407
Cdd:pfam15709 329 EQEKASRDRLRAERAEMRRLEVERKRREQEEQ------RRLQQEQLERAEKMREE-------------------LEL--- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1408 knlsEQQikdksqqvdealhsrtKIEEEIRLIRIQLEttEKQKYTAESELKQLRDRAAEAEKLRKlaqdEAEKLRKQVSE 1487
Cdd:pfam15709 381 ----EQQ----------------RRFEEIRLRKQRLE--EERQRQEEEERKQRLQLQAAQERARQ----QQEEFRRKLQE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1488 ETQKKRQAEEElkrKSEAEKEAAKQKQKALEDLEKLRMQAEEAER----QVKQAEIEKEKQikvahEAAQKSAAAELQSK 1563
Cdd:pfam15709 435 LQRKKQQEEAE---RAEAEKQRQKELEMQLAEEQKRLMEMAEEERleyqRQKQEAEEKARL-----EAEERRQKEEEAAR 506
|
250
....*....|....*..
gi 1988774686 1564 hMSFAEKTSKLEESLKQ 1580
Cdd:pfam15709 507 -LALEEAMKQAQEQARQ 522
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1206-1522 |
2.08e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.07 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1206 ADAKQRQEKI--QAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQ-VEPLVSPL 1282
Cdd:PRK11281 39 ADVQAQLDALnkQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDnDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1283 KKT-------KLDSASDNIIQEYVTLRTRYSELMTLTSQYI---KFITDTQRR-------LDDEEKAAEKLKAEERKKMA 1345
Cdd:PRK11281 119 STLslrqlesRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraqAALYANSQRlqqirnlLKGGKVGGKALRPSQRVLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1346 EMQAELDKQ-------------------KQLAEAHAKaIAKAEKEAQEL-------KLKMQEEVSKREIAAVDAEKQKTN 1399
Cdd:PRK11281 199 AEQALLNAQndlqrkslegntqlqdllqKQRDYLTAR-IQRLEHQLQLLqeainskRLTLSEKTVQEAQSQDEAARIQAN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1400 --IQLEL--------------QELKNLSEQQIKDKsQQVDEALHSRTKIEEEIR-------LIRIQLEttEKQKYTAESE 1456
Cdd:PRK11281 278 plVAQELeinlqlsqrllkatEKLNTLTQQNLRVK-NWLDRLTQSERNIKEQISvlkgsllLSRILYQ--QQQALPSADL 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 1457 LKQLRDRAAeaeKLRkLAQDEAEKLRKQVSE-----ETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEK 1522
Cdd:PRK11281 355 IEGLADRIA---DLR-LEQFEINQQRDALFQpdayiDKLEAGHKSEVTDEVRDALLQLLDERRELLDQLNK 421
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2404-2593 |
2.08e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2404 VERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMAD-------AQQKKIEHEKTVLQQTFMTEKEMLL 2476
Cdd:PHA02562 236 IEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2477 KKEKLIEDEKKRLESQFEEEVKKAKALKDeqerqkqQMEQEKKTLQATMDAALskqkeaeeemlRKQKEMQELERQRLEQ 2556
Cdd:PHA02562 316 EKLDTAIDELEEIMDEFNEQSKKLLELKN-------KISTNKQSLITLVDKAK-----------KVKAAIEELQAEFVDN 377
|
170 180 190
....*....|....*....|....*....|....*..
gi 1988774686 2557 ERILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKD 2593
Cdd:PHA02562 378 AEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1488-1805 |
2.14e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 50.36 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1488 ETQKKRQAE--EELKRKSEAEKEAAKQKQKALEDLEKlrmqaeeAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHM 1565
Cdd:PRK07735 8 EDLKKEAARraKEEARKRLVAKHGAEISKLEEENREK-------EKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1566 SFAEKTSklEESLKQEHGAVLQLQQEAERLKKQQEdaENSREEAEKELEKWRQKANEALRLRLQAedeahkktlaqeeae 1645
Cdd:PRK07735 81 GTEEVTE--EEKAKAKAKAAAAAKAKAAALAKQKR--EGTEEVTEEEKAAAKAKAAAAAKAKAAA--------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1646 kqkeeaerEAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQqrslleDELYRLKNEV 1725
Cdd:PRK07735 142 --------LAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTE------EEKAKAKAKA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1726 AAAQQQRKQledELAKvrsemdiliQLKTKAEKETMSNTEKSKQlleAEAAKMKdlAEEASRLRAISEEAKHQRQIAEEE 1805
Cdd:PRK07735 208 AAAAKAKAA---ALAK---------QKASQGNGDSGDEDAKAKA---IAAAKAK--AAAAARAKTKGAEGKKEEEPKQEE 270
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
22-119 |
2.19e-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: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 22 QKKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 88
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1988774686 89 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 119
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQII 135
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1593-1837 |
2.46e-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: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1593 ERLKKQQEDAENSREEAEKELEKWRQKANealrlRLQAEDEAHKKtlaqeeaekqkeeaeREAKKRAKAEESALKQKEMA 1672
Cdd:COG2268 192 RKIAEIIRDARIAEAEAERETEIAIAQAN-----REAEEAELEQE---------------REIETARIAEAEAELAKKKA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1673 EEELERQRKIAESTAQQKLtaeqelirlradfdnaeqqrslledelyrlknevaAAQQQRKQLEDELAKVRSEMDILIQL 1752
Cdd:COG2268 252 EERREAETARAEAEAAYEI-----------------------------------AEANAEREVQRQLEIAEREREIELQE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1753 KTKAEKEtmsNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKhqrqiAEEEAARQRAEAERILKEklAAISEAtRLKT 1832
Cdd:COG2268 297 KEAEREE---AELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGL-----AEAEGKRALAEAWNKLGD--AAILLM-LIEK 365
|
....*
gi 1988774686 1833 EAEIA 1837
Cdd:COG2268 366 LPEIA 370
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1106-2016 |
2.60e-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: 50.82 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1106 EVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRW-KAVFTQIDLRQREL 1184
Cdd:TIGR01612 780 ELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFlNKVDKFINFENNCK 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1185 EQLGRQlgyyRESYDWLIRWI-ADAKQRQEKIQAVPITDSKTLkeqLAQEKKLLEEIEQNKD---KVDECQKYAKAYIDT 1260
Cdd:TIGR01612 860 EKIDSE----HEQFAELTNKIkAEISDDKLNDYEKKFNDSKSL---INEINKSIEEEYQNINtlkKVDEYIKICENTKES 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1261 IKDYELQLVAYKAQVEPLVSPLKKTkldsasdNIIQEyvtlrtryselmTLTSQYIKFITDTQRRLDDEEKAAEkLKAEE 1340
Cdd:TIGR01612 933 IEKFHNKQNILKEILNKNIDTIKES-------NLIEK------------SYKDKFDNTLIDKINELDKAFKDAS-LNDYE 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1341 RKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAqelklkmQEEVSKREIAAVDAEKQKTNIQLELQ-ELKNLSEQQIKDKS 1419
Cdd:TIGR01612 993 AKNNELIKYFNDLKANLGKNKENMLYHQFDEK-------EKATNDIEQKIEDANKNIPNIEIAIHtSIYNIIDEIEKEIG 1065
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1420 QQVdEALHSRTKIEEEIRLIRIQlETTEKQKYTAESELKQlRDRAAEAEKLRKLAQDeaeklRKQVSEETQKKRQAEEEL 1499
Cdd:TIGR01612 1066 KNI-ELLNKEILEEAEINITNFN-EIKEKLKHYNFDDFGK-EENIKYADEINKIKDD-----IKNLDQKIDHHIKALEEI 1137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1500 KRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAE-----IEKEKQI-----KVAHEAAQ----KSAAAELQSKHM 1565
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIEnivtkIDKKKNIydeikKLLNEIAEiekdKTSLEEVKGINL 1217
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1566 SFAEKTSKL------EESLKQEH--GAVLQLQQEAERLKKQQEDAENsreeaEKELEKWRQKANEALRLRlQAEDEAHKK 1637
Cdd:TIGR01612 1218 SYGKNLGKLflekidEEKKKSEHmiKAMEAYIEDLDEIKEKSPEIEN-----EMGIEMDIKAEMETFNIS-HDDDKDHHI 1291
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1638 TLAQEEAEKQKEEAEREAKKRAKAEESALK--QKEMAEEELERQRKIAE-STAQQKLTAEQELIRL---RADFDNAEQQR 1711
Cdd:TIGR01612 1292 ISKKHDENISDIREKSLKIIEDFSEESDINdiKKELQKNLLDAQKHNSDiNLYLNEIANIYNILKLnkiKKIIDEVKEYT 1371
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1712 SLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKM-------KDLAEE 1784
Cdd:TIGR01612 1372 KEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIdtyfknaDENNEN 1451
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1785 ASRLRAISEEAKHQRQ-IAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEaENERLRRQAEDEA------Y 1857
Cdd:TIGR01612 1452 VLLLFKNIEMADNKSQhILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIE-KNKELFEQYKKDVtellnkY 1530
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1858 QRKALEDQASQHKQEIEEKIVQLKKSS-----EAEMERQKaiVDDTLKQRRVVEEEIRilklNFEKASSGKLDLELEL-- 1930
Cdd:TIGR01612 1531 SALAIKNKFAKTKKDSEIIIKEIKDAHkkfilEAEKSEQK--IKEIKKEKFRIEDDAA----KNDKSNKAAIDIQLSLen 1604
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1931 --NKLKNIAD-ETQQSKIRAEEEA--EKLRKLALEEEKRRreaeekvkkiAAAEEEAARQRKAALEELERLRKKAEEARK 2005
Cdd:TIGR01612 1605 feNKFLKISDiKKKINDCLKETESieKKISSFSIDSQDTE----------LKENGDNLNSLQEFLESLKDQKKNIEDKKK 1674
|
970
....*....|.
gi 1988774686 2006 QKDEADKEAEK 2016
Cdd:TIGR01612 1675 ELDELDSEIEK 1685
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1702-2153 |
2.62e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.29 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1702 ADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKE---TMSNTEKSKQLLEAeaakM 1778
Cdd:COG5278 79 EPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEaalALVRSGEGKALMDE----I 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1779 KDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQ 1858
Cdd:COG5278 155 RARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALEL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1859 RKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAD 1938
Cdd:COG5278 235 LAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1939 ETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQI 2018
Cdd:COG5278 315 AAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2019 VVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEA 2098
Cdd:COG5278 395 IAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAAL 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774686 2099 ANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQ 2153
Cdd:COG5278 475 AALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAE 529
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2432-2604 |
2.63e-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: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2432 KARLKKEAEELQNKSKEMADAQQKKIEhektvLQQTFMTEkEMLLKKEKLiEDEKKRLEsqfEEEVKKAKALKDEQERQK 2511
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELE-----LEQQRRFE-EIRLRKQRL-EEERQRQE---EEERKQRLQLQAAQERAR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2512 QQMEQEKKTLQatmDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAE--ENQKLREKLQQLEDAQKDQHTRETDKV 2589
Cdd:pfam15709 423 QQQEEFRRKLQ---ELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEmaEEERLEYQRQKQEAEEKARLEAEERRQ 499
|
170
....*....|....*
gi 1988774686 2590 LHKDIIHLTTIETTK 2604
Cdd:pfam15709 500 KEEEAARLALEEAMK 514
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2147-2318 |
2.82e-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: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2147 AEQTLkQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELL------KLKNKI 2220
Cdd:COG3206 194 AEAAL-EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLqspviqQLRAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2221 EEENQRLIKKDKDST------QKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQE 2294
Cdd:COG3206 273 AELEAELAELSARYTpnhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
170 180 190
....*....|....*....|....*....|..
gi 1988774686 2295 ASRLKAEAE--------MLQKQKDLAQEQAQK 2318
Cdd:COG3206 353 LRRLEREVEvarelyesLLQRLEEARLAEALT 384
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2212-2586 |
2.93e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 50.57 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2212 ELLKLKNKIEEENQRLIKKDKDSTQ-KLLAEEAENMRKLAEDAARL----------SVEaQEAARLRQIAEDDLNQQRAL 2280
Cdd:PRK10246 455 EQTQRNAALNEMRQRYKEKTQQLADvKTICEQEARIKDLEAQRAQLqagqpcplcgSTS-HPAVEAYQALEPGVNQSRLD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2281 AekMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDkqlmQQRLEEETEEYHKSLEVERKRQLEI---MAEAER 2357
Cdd:PRK10246 534 A--LEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQE----EQALTQQWQAVCASLNITLQPQDDIqpwLDAQEE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2358 LRLQVSQLSeaqaraeeeaKKFKKQADKVATRLHETEIATQekmtvverLEFERLNTSKEADDLRKAIADLENEKARL-- 2435
Cdd:PRK10246 608 HERQLRLLS----------QRHELQGQIAAHNQQIIQYQQQ--------IEQRQQQLLTALAGYALTLPQEDEEASWLat 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2436 -KKEAEELQNKSKEMADAQQKKieHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQfeeevkkAKALKDEQERQKQQM 2514
Cdd:PRK10246 670 rQQEAQSWQQRQNELTALQNRI--QQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQ-------CLSLHSQLQTLQQQD 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2515 EQEKKTL---QATMDAALSKQ----KEA-------EEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKD 2580
Cdd:PRK10246 741 VLEAQRLqkaQAQFDTALQASvfddQQAflaalldEETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDL 820
|
....*.
gi 1988774686 2581 QHTRET 2586
Cdd:PRK10246 821 TVTVEQ 826
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4109-4137 |
3.17e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 3.17e-05
10 20
....*....|....*....|....*....
gi 1988774686 4109 VRKRRVVIVDPETGKEMTVYEAYRKGLID 4137
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2476-2580 |
3.22e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.30 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2476 LKKEKLIEDEKKRLESQFEEevkkAKALKDEQERQKQQMEQEKKTLQAtmdaALSKQKEAEEEMLRKQKEMQELERQRLE 2555
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQ----TLALLDKIDRQKEETEQLKQQLAQ----APAKLRQAQAELEALKDDNDEETRETLS 119
|
90 100
....*....|....*....|....*
gi 1988774686 2556 QERiLAEENQKLREKLQQLEDAQKD 2580
Cdd:PRK11281 120 TLS-LRQLESRLAQTLDQLQNAQND 143
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1431-1581 |
3.25e-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: 48.38 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1431 KIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKS------- 1503
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyea 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1504 -EAEKEAAKQKQKALEDLEK-LRMQAEEAERQVK--QAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLK 1579
Cdd:COG1579 94 lQKEIESLKRRISDLEDEILeLMERIEELEEELAelEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
..
gi 1988774686 1580 QE 1581
Cdd:COG1579 174 PE 175
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2130-2583 |
3.42e-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: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2130 LMQKQQADTEMAKHKKLAEQTLKQKFqveqeLTKVKLKLDETDKQKSVLDEELQRLKDEVDD----AVKQRGQVEEELFK 2205
Cdd:pfam05557 59 LLEKREAEAEEALREQAELNRLKKKY-----LEALNKKLNEKESQLADAREVISCLKNELSElrrqIQRAELELQSTNSE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2206 VKVQMEELLKLKNKIEEENQRliKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEA----ARLRQIAEDDLNQQRALA 2281
Cdd:pfam05557 134 LEELQERLDLLKAKASEAEQL--RQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVknskSELARIPELEKELERLRE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2282 E-KMLKEkmqAIQEASRLKAEAEMLQKQKDlAQEQAQKLLEDKQLMQQRLEEETEEYHK----------SLEVERKRQLE 2350
Cdd:pfam05557 212 HnKHLNE---NIENKLLLKEEVEDLKRKLE-REEKYREEAATLELEKEKLEQELQSWVKlaqdtglnlrSPEDLSRRIEQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2351 IMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLEN 2430
Cdd:pfam05557 288 LQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDK 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2431 E---------KARLKKEAEEL----QNKSKEMaDAQQKKIEHEKTVL-QQTFMTEKEMLLKKEKLIEDEKKRLESQFEEE 2496
Cdd:pfam05557 368 EltmsnyspqLLERIEEAEDMtqkmQAHNEEM-EAQLSVAEEELGGYkQQAQTLERELQALRQQESLADPSYSKEEVDSL 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2497 VKKAKALKDEQERQKQQ-----MEQEKKTLQATMDAALSKQkeaeeeMLRKQKEMQELERQRLEQERILAEENQKLREKL 2571
Cdd:pfam05557 447 RRKLETLELERQRLREQkneleMELERRCLQGDYDPKKTKV------LHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLL 520
|
490
....*....|..
gi 1988774686 2572 QQLEDAQKDQHT 2583
Cdd:pfam05557 521 KKLEDDLEQVLR 532
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2259-2581 |
3.58e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.87 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2259 EAQEAAR-LRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDkqlMQQRLEEETEEY 2337
Cdd:pfam02029 3 DEEEAAReRRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDR---TAKREERRQKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2338 HKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKV---ATRLHETEIATQEKMTVVERLEfERLNT 2414
Cdd:pfam02029 80 QEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYkeeETEIREKEYQENKWSTEVRQAE-EEGEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2415 SKEADDLRKAI--ADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQ 2492
Cdd:pfam02029 159 EEDKSEEAEEVptENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2493 FEEEVKKAKALKDEQERQKQQME-QEKKTLQatmdaalSKQKEAE---EEMLRKQKE---MQELERQRLEQERILA---- 2561
Cdd:pfam02029 239 EAEVFLEAEQKLEELRRRRQEKEsEEFEKLR-------QKQQEAElelEELKKKREErrkLLEEEEQRRKQEEAERklre 311
|
330 340
....*....|....*....|...
gi 1988774686 2562 -EENQKLREKLQ--QLEDAQKDQ 2581
Cdd:pfam02029 312 eEEKRRMKEEIErrRAEAAEKRQ 334
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1429-1522 |
3.81e-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: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1429 RTKIEEEIRLIRIQLETTEKQKYTAESELKQLRdraAEAEKLRKLAQDEAEKLRKQVseetqkKRQAEEELKR-KSEAEK 1507
Cdd:cd06503 32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEAR---AEAQEIIEEARKEAEKIKEEI------LAEAKEEAERiLEQAKA 102
|
90
....*....|....*
gi 1988774686 1508 EAAKQKQKALEDLEK 1522
Cdd:cd06503 103 EIEQEKEKALAELRK 117
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1321-1614 |
4.13e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 49.59 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1321 DTQRRLDD-EEKAAEKLKAEERKKMAEMQAElDKQKQLAEAHAKAIAKAEKEAQELklkmqEEVSKREIAAVDAEKQKTN 1399
Cdd:PRK07735 2 DPEKDLEDlKKEAARRAKEEARKRLVAKHGA-EISKLEEENREKEKALPKNDDMTI-----EEAKRRAAAAAKAKAAALA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1400 IQLELQELKNLSEQQIKDKSQQVDEAlhsrtkieeeirliRIQLETTEKQKYTAESELKQlRDRAAEAEKLRKLAQDEAE 1479
Cdd:PRK07735 76 KQKREGTEEVTEEEKAKAKAKAAAAA--------------KAKAAALAKQKREGTEEVTE-EEKAAAKAKAAAAAKAKAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1480 KLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVaheAAQKSAAAE 1559
Cdd:PRK07735 141 ALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAA---AAAKAKAAA 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774686 1560 LQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKkqQEDAENSREEAEKELE 1614
Cdd:PRK07735 218 LAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAK--TKGAEGKKEEEPKQEE 270
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
2482-2616 |
4.43e-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: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2482 IEDEKKRLeSQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATmdaaLSKQKEAEEEMLRKQKEMQELER--QRLEQERI 2559
Cdd:COG2433 408 LTEEEEEI-RRLEEQVERLEAEVEELEAELEEKDERIERLERE----LSEARSEERREIRKDREISRLDReiERLERELE 482
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774686 2560 -LAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDIIHLTTIETTKTVYnGQNVGDVV 2616
Cdd:COG2433 483 eERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEY-GLKEGDVV 539
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1427-1598 |
4.57e-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: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1427 HSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAE-AEKLRKlAQDEAEKLRKQVSEETQKKRQAEEELkrkSEA 1505
Cdd:pfam10168 554 LAREEIQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKlAEKYEE-IKDKQEKLMRRCKKVLQRLNSQLPVL---SDA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1506 EKEAAKQkqkaledLEKLRMQAEEAERQVKQAEIEKEKQIKvaHEAAQKSAAaelQSKHMSFAEKTSK-LEESLKQEHGA 1584
Cdd:pfam10168 630 EREMKKE-------LETINEQLKHLANAIKQAKKKMNYQRY--QIAKSQSIR---KKSSLSLSEKQRKtIKEILKQLGSE 697
|
170
....*....|....
gi 1988774686 1585 VLQLQQEAERLKKQ 1598
Cdd:pfam10168 698 IDELIKQVKDINKH 711
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2267-2575 |
4.72e-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: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2267 RQIAEDDLNQQRALAEKMLKEKMQAIQEasRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERK 2346
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEE--EEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2347 RQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKvatrlheteiatQEKMTVVERLEFERLNTSKEADdlrkaia 2426
Cdd:pfam13868 110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE------------EEREEDERILEYLKEKAEREEE------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2427 dLENEKARLKKEAEELQNKskemADAQQKKIEHEKTvlqqtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDE 2506
Cdd:pfam13868 171 -REAEREEIEEEKEREIAR----LRAQQEKAQDEKA--------ERDELRAKLYQEEQERKERQKEREEAEKKARQRQEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2507 QERQKQQMEQEKKTLQATMDaalsKQKEAEEEMLRKQKEMQELERQRLEQERI-----------LAEENQKLREKLQQLE 2575
Cdd:pfam13868 238 QQAREEQIELKERRLAEEAE----REEEEFERMLRKQAEDEEIEQEEAEKRRMkrlehrrelekQIEEREEQRAAEREEE 313
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3976-4007 |
4.93e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.93e-05
10 20 30
....*....|....*....|....*....|..
gi 1988774686 3976 KLLSAERAVTGYRDPYTGKTISLFQAMKKGLI 4007
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1319-1516 |
5.12e-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: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1319 ITDTQRRLDDEEKAAEKLKAEER---KKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEvsKREIAAVDAEK 1395
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAaleRRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ--KEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1396 QKTNIQLELQELKNLSE-QQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDR---------AA 1465
Cdd:COG4942 114 YRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEleeeraaleAL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 1466 EAEKLRKLAQDEAEKlrKQVSEETQKKRQAEEELKRK-SEAEKEAAKQKQKA 1516
Cdd:COG4942 194 KAERQKLLARLEKEL--AELAAELAELQQEAEELEALiARLEAEAAAAAERT 243
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3074-3110 |
5.23e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 5.23e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1988774686 3074 KLLSAERAVTGYRDPYTGKTVSLFQAMKKDLIPKEQG 3110
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1323-1638 |
5.35e-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: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1323 QRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKqLAEAHAKaiAKAEKEAQELKLKMQEEvskreiaavdaekqktniql 1402
Cdd:pfam15558 78 ERRRADRREKQVIEKESRWREQAEDQENQRQEK-LERARQE--AEQRKQCQEQRLKEKEE-------------------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1403 ELQELKNLSEQQIKDKSQQvdeALHSRTKIEEEIRLIRIQLETTEKQKYTAeseLKQLRDRAAEAEKLRKLAQDEAEKLR 1482
Cdd:pfam15558 135 ELQALREQNSLQLQERLEE---ACHKRQLKEREEQKKVQENNLSELLNHQA---RKVLVDCQAKAEELLRRLSLEQSLQR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1483 KQVSEETQKKRQAeEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQikVAHEAAQKSAAAELQS 1562
Cdd:pfam15558 209 SQENYEQLVEERH-RELREKAQKEEEQFQRAKWRAEEKEEERQEHKEALAELADRKIQQARQ--VAHKTVQDKAQRAREL 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774686 1563 KHMSfaEKTSKLEEsLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKT 1638
Cdd:pfam15558 286 NLER--EKNHHILK-LKVEKEEKCHREGIKEAIKKKEQRSEQISREKEATLEEARKTARASFHMREKVREETNNRT 358
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1340-2554 |
5.49e-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: 50.05 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1340 ERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELK---LKMQEEVSK---REIAAVDAEKQKTNIQLELQE-LKNLSe 1412
Cdd:TIGR01612 535 KAKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENedsIHLEKEIKDlfdKYLEIDDEIIYINKLKLELKEkIKNIS- 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1413 qqikDKSQQVDEALHSRTKIEEEIRLIRiqlETTEKQKYTAESELKQlRDRAAEAEK--LRKLAQDEAEKLRKQVSEETQ 1490
Cdd:TIGR01612 614 ----DKNEYIKKAIDLKKIIENNNAYID---ELAKISPYQVPEHLKN-KDKIYSTIKseLSKIYEDDIDALYNELSSIVK 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1491 KKRQAEEELKRKSEAEKEAAKQKQKALEDleklrMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSaaaelqskHMSFAEK 1570
Cdd:TIGR01612 686 ENAIDNTEDKAKLDDLKSKIDKEYDKIQN-----METATVELHLSNIENKKNELLDIIVEIKKHI--------HGEINKD 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1571 TSKLEESLKQEhgavlqlqqeaerlKKQQEDAENSREEAEKELEKWRQKANEalrLRLQAEDEAHKKTLAQEEAEKQKEE 1650
Cdd:TIGR01612 753 LNKILEDFKNK--------------EKELSNKINDYAKEKDELNKYKSKISE---IKNHYNDQINIDNIKDEDAKQNYDK 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1651 AEREAKKRAKAEESALK----QKEMAEEELERQRKIA--ESTAQQKLTAEQELI-----RLRADFdnAEQQRSLLEDEL- 1718
Cdd:TIGR01612 816 SKEYIKTISIKEDEIFKiineMKFMKDDFLNKVDKFInfENNCKEKIDSEHEQFaeltnKIKAEI--SDDKLNDYEKKFn 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1719 --YRLKNEVAAAQQQRKQLEDELAKVRSEMDIliqlkTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLraiseEAK 1796
Cdd:TIGR01612 894 dsKSLINEINKSIEEEYQNINTLKKVDEYIKI-----CENTKESIEKFHNKQNILKEILNKNIDTIKESNLI-----EKS 963
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1797 HQRQIaEEEAARQRAEAERILKEklAAISEATRLKTEAeiaLKEKEAENERLRRQAEDEAYQRKaleDQASQHKQEIEEK 1876
Cdd:TIGR01612 964 YKDKF-DNTLIDKINELDKAFKD--ASLNDYEAKNNEL---IKYFNDLKANLGKNKENMLYHQF---DEKEKATNDIEQK 1034
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1877 IVQLKKS-SEAEMERQKAIVDDTLKQRRVVEEEIRILKLN-FEKASSGKLDLELELNKLK--NIADETQQSKIRAEEEae 1952
Cdd:TIGR01612 1035 IEDANKNiPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEiLEEAEINITNFNEIKEKLKhyNFDDFGKEENIKYADE-- 1112
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1953 klrklaleeekrrreaeekVKKIAAAEEEAARQRKAALEELERLRKKAE----EARKQKDEADKEAEKQIvvaqqAAQKC 2028
Cdd:TIGR01612 1113 -------------------INKIKDDIKNLDQKIDHHIKALEEIKKKSEnyidEIKAQINDLEDVADKAI-----SNDDP 1168
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2029 SAAEQQVQSVLAQ-----QIEDSItQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAK 2103
Cdd:TIGR01612 1169 EEIEKKIENIVTKidkkkNIYDEI-KKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEA 1247
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2104 AQEDAERLRKEAEfeaaKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQ--ELTKVKLKLDETDKQKSVLDEE 2181
Cdd:TIGR01612 1248 YIEDLDEIKEKSP----EIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENisDIREKSLKIIEDFSEESDINDI 1323
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2182 LQRLKDEVDDAVKQRGQVEE------------ELFKVKVQMEELLKLKNKIEEENQRlIKKDKDSTQKLLAEEAEN---- 2245
Cdd:TIGR01612 1324 KKELQKNLLDAQKHNSDINLylneianiynilKLNKIKKIIDEVKEYTKEIEENNKN-IKDELDKSEKLIKKIKDDinle 1402
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2246 ------------------MRKLAEDAAR-LSVEAQEAARLRQIAEDDLNQQRALAE-KMLKEKMQAIQEASR-------- 2297
Cdd:TIGR01612 1403 eckskiestlddkdidecIKKIKELKNHiLSEESNIDTYFKNADENNENVLLLFKNiEMADNKSQHILKIKKdnatndhd 1482
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2298 -----LKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLE--------IMAEAERLRLQVSQ 2364
Cdd:TIGR01612 1483 fnineLKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAktkkdseiIIKEIKDAHKKFIL 1562
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2365 LSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSkeadDLRKAIADLENEKARLKKEAEELQn 2444
Cdd:TIGR01612 1563 EAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKIS----DIKKKINDCLKETESIEKKISSFS- 1637
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2445 kskemADAQQKKIEHEKTVLQ--QTFMtekEMLLKKEKLIEDEKKRLESqfeeevkkakaLKDEQERQKQQMEQEKKTLQ 2522
Cdd:TIGR01612 1638 -----IDSQDTELKENGDNLNslQEFL---ESLKDQKKNIEDKKKELDE-----------LDSEIEKIEIDVDQHKKNYE 1698
|
1290 1300 1310
....*....|....*....|....*....|..
gi 1988774686 2523 ATMDAALSKQKEAEEEMLRKQKEMQELERQRL 2554
Cdd:TIGR01612 1699 IGIIEKIKEIAIANKEEIESIKELIEPTIENL 1730
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1181-1913 |
5.55e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1181 QRELEQLGRQLGYYRESYDWLIRWIADAKQRQEKIQavpitdskTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDT 1260
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQ--------TRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEE 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1261 IKDYELQLVAYKAQVEplvsplkkTKLDSASDniiqeyvtLRTRYSELMTLtsqyIKFITDTQRRLDDEEKAAEKLKAEE 1340
Cdd:PRK04863 447 FQAKEQEATEELLSLE--------QKLSVAQA--------AHSQFEQAYQL----VRKIAGEVSRSEAWDVARELLRRLR 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1341 RKKMaemqaeLDKQKQLAEAHAKAIAKAEKEAQELKlKMQEEVSKREIAAVDAEKqktniqlELQELKNLSEQQIKDKSQ 1420
Cdd:PRK04863 507 EQRH------LAEQLQQLRMRLSELEQRLRQQQRAE-RLLAEFCKRLGKNLDDED-------ELEQLQEELEARLESLSE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1421 QVDEALHSRTKIEEEIRLIRIQ---LETTEKQKYTAESELKQLRDRAAEA----EKLRKLAQDEAEKLRK---QVSEETQ 1490
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARiqrLAARAPAWLAAQDALARLREQSGEEfedsQDVTEYMQQLLEREREltvERDELAA 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1491 KKRQAEEELKRKSEAEK-------------------------------------------------EAAKQKQKALEDL- 1520
Cdd:PRK04863 653 RKQALDEEIERLSQPGGsedprlnalaerfggvllseiyddvsledapyfsalygparhaivvpdlSDAAEQLAGLEDCp 732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1521 EKLRM-------------QAEEAERQV------KQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESlkqe 1581
Cdd:PRK04863 733 EDLYLiegdpdsfddsvfSVEELEKAVvvkiadRQWRYSRFPEVPLFGRAAREKRIEQLRAEREELAERYATLSFD---- 808
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1582 hgavlqlQQEAERLKKQQEDAENS------REEAEKELEKWRQKANEALRlRLQAEDEAHKKTLAQEEAEKQKEEAEREA 1655
Cdd:PRK04863 809 -------VQKLQRLHQAFSRFIGShlavafEADPEAELRQLNRRRVELER-ALADHESQEQQQRSQLEQAKEGLSALNRL 880
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1656 KKRAK--AEESALKQKEMAEEELERQRKIAESTAQQKLTA---EQELIRLRADFDNAEQqrslledelyrLKNEVAAAQQ 1730
Cdd:PRK04863 881 LPRLNllADETLADRVEEIREQLDEAEEAKRFVQQHGNALaqlEPIVSVLQSDPEQFEQ-----------LKQDYQQAQQ 949
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1731 QRKQLedelakvrsemdiliQLKTKAEKETMSNTEkskQLLEAEAAKMkdLAEEA---SRLRAISEEAKHQRQIAEEEAA 1807
Cdd:PRK04863 950 TQRDA---------------KQQAFALTEVVQRRA---HFSYEDAAEM--LAKNSdlnEKLRQRLEQAEQERTRAREQLR 1009
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1808 RQRAEAERILKEKLAAISEATRLKTEaeiaLKEKEAENERLRRQAEDEAyqrkalEDQASQHKQEIEEKIV--QLKKSS- 1884
Cdd:PRK04863 1010 QAQAQLAQYNQVLASLKSSYDAKRQM----LQELKQELQDLGVPADSGA------EERARARRDELHARLSanRSRRNQl 1079
|
810 820
....*....|....*....|....*....
gi 1988774686 1885 EAEMERQKAIVDDTLKQRRVVEEEIRILK 1913
Cdd:PRK04863 1080 EKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2149-2573 |
5.59e-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: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2149 QTLKQKFQVEQELTKVKlkldetdkqksvldEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEEL-LKLKNKIEEENQrl 2227
Cdd:pfam05701 32 QTVERRKLVELELEKVQ--------------EEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELkLNLERAQTEEAQ-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2228 IKKDKDstqklLAE-EAENMRKLAEDAARLSVEAQ-EAARLRQIAeddlnqqrALAE-KMLKEKMQAIQEasrlkaEAEM 2304
Cdd:pfam05701 96 AKQDSE-----LAKlRVEEMEQGIADEASVAAKAQlEVAKARHAA--------AVAElKSVKEELESLRK------EYAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2305 LQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEY---HKSLEVERKRQLEimAEAERLRLQVSqlseaqaraeeeakkfkK 2381
Cdd:pfam05701 157 LVSERDIAIKRAEEAVSASKEIEKTVEELTIELiatKESLESAHAAHLE--AEEHRIGAALA-----------------R 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2382 QADKVAtrlHETEIATQEKmtvverlEFERLNtskeaDDLRKAiadlENEKARLKKEAEELQNKSKEMADAQQKKIEHEK 2461
Cdd:pfam05701 218 EQDKLN---WEKELKQAEE-------ELQRLN-----QQLLSA----KDLKSKLETASALLLDLKAELAAYMESKLKEEA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2462 TVLQQTFMTE---KEMLLKKEKLIEDEKKRLESQfEEEVK----KAKALKDEQERQK------QQ-----------MEQE 2517
Cdd:pfam05701 279 DGEGNEKKTStsiQAALASAKKELEEVKANIEKA-KDEVNclrvAAASLRSELEKEKaelaslRQregmasiavssLEAE 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2518 KKTLQATMDAALSKQKEAEEEMLRKQKEMQElERQRLEQERILA----EENQKLREKLQQ 2573
Cdd:pfam05701 358 LNRTKSEIALVQAKEKEAREKMVELPKQLQQ-AAQEAEEAKSLAqaarEELRKAKEEAEQ 416
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1815-2581 |
5.69e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1815 RILKEKLAAISEATRLKTEAEIALKEKEAENERL---RRQAEDEAYQRKALEDQ-------------ASQHKQEIEEKIV 1878
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDyqaasdhlnlvqtALRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1879 QLKKSSEAeMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKiRAEEEAEKLRKLA 1958
Cdd:PRK04863 356 DLEELEER-LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAV-QALERAKQLCGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1959 LEEEkrrreaeekvkkiaaaeeeaarqrKAALEELERLRKKAEEArkqkDEADKEAEKQIVVAQQAAQKCSAAEQQVQSv 2038
Cdd:PRK04863 434 DLTA------------------------DNAEDWLEEFQAKEQEA----TEELLSLEQKLSVAQAAHSQFEQAYQLVRK- 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2039 LAQQIEDSITQKKLKEeyekakklAKEAEAAKEKAEREAALLRQQAEEAERQktaaeeeaanqAKAQEDAERLRKEAEFE 2118
Cdd:PRK04863 485 IAGEVSRSEAWDVARE--------LLRRLREQRHLAEQLQQLRMRLSELEQR-----------LRQQQRAERLLAEFCKR 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2119 AAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSV---LDEELQRLKDEVDDAVKQ 2195
Cdd:PRK04863 546 LGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFED 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2196 RGQVEEelfkvkvQMEELLKLKNKIEEENQRLikkdkdstqkllaeeAENMRKLAEDAARLS-VEAQEAARLRQIAE--- 2271
Cdd:PRK04863 626 SQDVTE-------YMQQLLERERELTVERDEL---------------AARKQALDEEIERLSqPGGSEDPRLNALAErfg 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2272 --------DDLNQQRA-LAEKMLKEKMQAIQeASRLKAEAEMLQKQKDlaqeqaqkLLEDKQLMQ---QRLEE---ETEE 2336
Cdd:PRK04863 684 gvllseiyDDVSLEDApYFSALYGPARHAIV-VPDLSDAAEQLAGLED--------CPEDLYLIEgdpDSFDDsvfSVEE 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2337 YHKSLEVErkrqleimaEAERlRLQVSQLSEA----QARAEEEAKKFKKQADKVATRLHETEIATQEkmtvVERL--EFE 2410
Cdd:PRK04863 755 LEKAVVVK---------IADR-QWRYSRFPEVplfgRAAREKRIEQLRAEREELAERYATLSFDVQK----LQRLhqAFS 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2411 R-----LNTSKEAD------DLRKAIADLENEKARLKKEAEELQN---KSKEMADAQQKKIEHEKTVLQQTFMTEKEMLl 2476
Cdd:PRK04863 821 RfigshLAVAFEADpeaelrQLNRRRVELERALADHESQEQQQRSqleQAKEGLSALNRLLPRLNLLADETLADRVEEI- 899
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2477 kKEKLIEDEK-----KRLESQFEEEVKKAKALKDEQE------RQKQQMEQEKKTLQATMDA---------ALSKQKEAe 2536
Cdd:PRK04863 900 -REQLDEAEEakrfvQQHGNALAQLEPIVSVLQSDPEqfeqlkQDYQQAQQTQRDAKQQAFAltevvqrraHFSYEDAA- 977
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1988774686 2537 eEMLRKQKEMQELERQRLEQ-ERILAEENQKLREKLQQLedAQKDQ 2581
Cdd:PRK04863 978 -EMLAKNSDLNEKLRQRLEQaEQERTRAREQLRQAQAQL--AQYNQ 1020
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3444-3479 |
5.83e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 5.83e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1988774686 3444 LLEAQIVSGGIIDPVKSHRVPTDVAYQKNILSRDIA 3479
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1114-1620 |
5.89e-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: 49.25 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1114 LKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQlgrqlgy 1193
Cdd:TIGR04523 234 IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1194 yresyDWlirwiadakqrqekiqavpitdSKTLKEQLAQEKKLLEEIEqnkDKVDECQKYAKAYIDTIKDyelqlvayka 1273
Cdd:TIGR04523 307 -----DW----------------------NKELKSELKNQEKKLEEIQ---NQISQNNKIISQLNEQISQ---------- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1274 qveplvspLKKTKLDSASDNiiqeyvtlRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKkmaemqaeLDK 1353
Cdd:TIGR04523 347 --------LKKELTNSESEN--------SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK--------IQN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1354 QKQLAEAHAKAIAKAEKEAQEL-----KLKMQEEVSKREIAavDAEKQKTNIQLELQELKNLSEQQikdkSQQVDEalhs 1428
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLekeieRLKETIIKNNSEIK--DLTNQDSVKELIIKNLDNTRESL----ETQLKV---- 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1429 rtkIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKlrklaqdEAEKLRKQVSEETQKKRQAEEElkrKSEAEKE 1508
Cdd:TIGR04523 473 ---LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEE-------KVKDLTKKISSLKEKIEKLESE---KKEKESK 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1509 AAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQehgaVLQL 1588
Cdd:TIGR04523 540 ISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK----ISSL 615
|
490 500 510
....*....|....*....|....*....|..
gi 1988774686 1589 QQEAERLKKQQEDAENSREEAEKELEKWRQKA 1620
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1328-1626 |
5.95e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.06 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1328 DEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQEL 1407
Cdd:PRK04778 105 HEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1408 KNLSEQ----QIKDKSQQVDEALHSRTKIEEEIRLIRIQLETT---------------EKQKY-----TAESELKQLRDR 1463
Cdd:PRK04778 185 VELTESgdyvEAREILDQLEEELAALEQIMEEIPELLKELQTElpdqlqelkagyrelVEEGYhldhlDIEKEIQDLKEQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1464 AAEAEK-LRKLAQDEAEKLRKQVSEETQkkrQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQ----AEEAERqVKQA- 1537
Cdd:PRK04778 265 IDENLAlLEELDLDEAEEKNEEIQERID---QLYDILEREVKARKYVEKNSDTLPDFLEHAKEQnkelKEEIDR-VKQSy 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1538 -----EIEK----EKQIKvAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEhgAVLQLQQE--AERLkKQQEDAENsr 1606
Cdd:PRK04778 341 tlnesELESvrqlEKQLE-SLEKQYDEITERIAEQEIAYSELQEELEEILKQL--EEIEKEQEklSEML-QGLRKDEL-- 414
|
330 340
....*....|....*....|
gi 1988774686 1607 eEAEKELEKWRQKANEALRL 1626
Cdd:PRK04778 415 -EAREKLERYRNKLHEIKRY 433
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1588-2041 |
6.46e-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: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1588 LQQEAERLKKQQEDAENSREEAEKELEKWRqKANEALRLRL---QAEDEAHKK--TLAQEEAEKQKEEAEREAKKRAKAE 1662
Cdd:pfam05701 47 VQEEIPEYKKQSEAAEAAKAQVLEELESTK-RLIEELKLNLeraQTEEAQAKQdsELAKLRVEEMEQGIADEASVAAKAQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1663 --------ESALKQKEMAEEELERQRKIAESTAQQK-----------------------LTAE-----QELIRLRADFDN 1706
Cdd:pfam05701 126 levakarhAAAVAELKSVKEELESLRKEYASLVSERdiaikraeeavsaskeiektveeLTIEliatkESLESAHAAHLE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1707 AEQQR------------------SLLEDELYRLKNEVAAAQQQRKQLE---DELAKVRSEMDILIQLKTKAEKETMSNTE 1765
Cdd:pfam05701 206 AEEHRigaalareqdklnwekelKQAEEELQRLNQQLLSAKDLKSKLEtasALLLDLKAELAAYMESKLKEEADGEGNEK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1766 KSKQLLEAEAAKMKDLAEEasrLRAISEEAKHQRQIAEEEAARQRAEAErilKEKlAAISEATRLKTEAEIALKEKEAEN 1845
Cdd:pfam05701 286 KTSTSIQAALASAKKELEE---VKANIEKAKDEVNCLRVAAASLRSELE---KEK-AELASLRQREGMASIAVSSLEAEL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1846 ERLRrqAEDEAYQRKALEDQasqhkqeieEKIVQL-KKSSEAEMErqkaiVDDTLKQRRVVEEEIRILKLNFEKASSGKL 1924
Cdd:pfam05701 359 NRTK--SEIALVQAKEKEAR---------EKMVELpKQLQQAAQE-----AEEAKSLAQAAREELRKAKEEAEQAKAAAS 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1925 DLELELnklkniadETQQSKIRAEEEAEKLRKLALEEEKRRREAEEkvkkiAAAEEEAARQRKAALEELERLRKKAEEAR 2004
Cdd:pfam05701 423 TVESRL--------EAVLKEIEAAKASEKLALAAIKALQESESSAE-----STNQEDSPRGVTLSLEEYYELSKRAHEAE 489
|
490 500 510
....*....|....*....|....*....|....*..
gi 1988774686 2005 KQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQ 2041
Cdd:pfam05701 490 ELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEE 526
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3368-3401 |
6.56e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 6.56e-05
10 20 30
....*....|....*....|....*....|....
gi 1988774686 3368 LLEAQAASGFIVDPVRNQCLSVDEAVKSGVVGPE 3401
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1653-1876 |
6.84e-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: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1653 REAKKRAKAEESALKQKEMAEE-----ELERQRKIAE-STAQQKLTAEQELirlrADFDNAEQQRSLLEDELYRLKNEVA 1726
Cdd:NF012221 1548 SKHAKQDDAAQNALADKERAEAdrqrlEQEKQQQLAAiSGSQSQLESTDQN----ALETNGQAQRDAILEESRAVTKELT 1623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1727 AAQQQRKQLEDE-------------------LAKVRSEMDiliqlktKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASR 1787
Cdd:NF012221 1624 TLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLD-------DAKKISGKQLADAKQRHVDNQQKVKDAVAKSEA 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1788 LRAISEeakHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAledQAS 1867
Cdd:NF012221 1697 GVAQGE---QNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQA---DAK 1770
|
....*....
gi 1988774686 1868 QHKQEIEEK 1876
Cdd:NF012221 1771 GAKQDESDK 1779
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1330-1577 |
6.86e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.10 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1330 EKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIqlelqelkn 1409
Cdd:pfam02029 137 EKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEV--------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1410 lseqqikdKSQQVDEALHSRTKIEEEIRLIRIQLETTE---KQKYTAESELKQLRDRAAEAEklrklaQDEAEKLRkqvs 1486
Cdd:pfam02029 208 --------KSQNGEEEVTKLKVTTKRRQGGLSQSQEREeeaEVFLEAEQKLEELRRRRQEKE------SEEFEKLR---- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1487 eetQKKRQAE---EELKRKSEaekeaakQKQKALEDlEKLRMQAEEAERQVKqaEIEKEKQIKvaheaaqksaaAELQSK 1563
Cdd:pfam02029 270 ---QKQQEAElelEELKKKRE-------ERRKLLEE-EEQRRKQEEAERKLR--EEEEKRRMK-----------EEIERR 325
|
250
....*....|....
gi 1988774686 1564 HMSFAEKTSKLEES 1577
Cdd:pfam02029 326 RAEAAEKRQKLPED 339
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1434-1581 |
7.16e-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: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1434 EEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEE--ELKRKSEAEKEAAK 1511
Cdd:pfam05262 199 DMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKpaDTSSPKEDKQVAEN 278
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1512 QKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSaAAELQSKHMSFAEKTSKLEESLKQE 1581
Cdd:pfam05262 279 QKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDK-ELEAQKKREPVAEDLQKTKPQVEAQ 347
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
1345-1743 |
7.29e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 49.20 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1345 AEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDE 1424
Cdd:COG4995 76 LLLALALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1425 ALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSE 1504
Cdd:COG4995 156 AAAAAAAAALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1505 AEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSkhmsfAEKTSKLEESLKQEHGA 1584
Cdd:COG4995 236 LLLALLALAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALAL-----AAAALALALLLAAAAAA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1585 VLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEES 1664
Cdd:COG4995 311 ALAALALLLLAALLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALL 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1665 ALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQ-QRSLLEDELYRLkneVAAAQQQRKQLEDELAKVR 1743
Cdd:COG4995 391 AALLLLAAALLALAAAQLLRLLLAALALLLALAAYAAARLALLALiEYIILPDRLYAF---VQLYQLLIAPIEAELPGIK 467
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1584-1910 |
7.37e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.38 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1584 AVLQLQQEAERLKKQQEDAENSREEAEKELEkwRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEE 1663
Cdd:pfam13868 22 KERDAQIAEKKRIKAEEKEEERRLDEMMEEE--RERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1664 SALKQKEMAEEELERQRKIAESTAQQKLTAE--QELIRLRADFDNAEQQRSLLEDElyRLKNEVAAAQQQRKQLEDELAK 1741
Cdd:pfam13868 100 REQMDEIVERIQEEDQAEAEEKLEKQRQLREeiDEFNEEQAEWKELEKEEEREEDE--RILEYLKEKAEREEEREAEREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1742 VRSEMDILIQLKTKAEKETMsnteksKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKL 1821
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQ------DEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1822 AAIsEATRLKTEAEIALKEKEAENERLRRQAEDeayQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQ 1901
Cdd:pfam13868 252 LAE-EAEREEEEFERMLRKQAEDEEIEQEEAEK---RRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAER 327
|
....*....
gi 1988774686 1902 RRVVEEEIR 1910
Cdd:pfam13868 328 RERIEEERQ 336
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
22-119 |
7.53e-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: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 22 QKKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 88
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1988774686 89 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 119
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 135
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1722-1900 |
7.95e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 49.25 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1722 KNEVAAAQQQRKQLEDElAKVRSEmdiLIQLKTKAEKEtmsntEKSKQLLEAEAakmKDLAEEAS-RLRAISEeakhqrq 1800
Cdd:PTZ00491 662 KSQEAAARHQAELLEQE-ARGRLE---RQKMHDKAKAE-----EQRTKLLELQA---ESAAVESSgQSRAEAL------- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1801 iAEEEAARQRAEAErilkeklaaiSEATRLKTEAEIALKEKEAENERLRRQAEdeayqrkaLEDQASQHKQEIEEKivql 1880
Cdd:PTZ00491 723 -AEAEARLIEAEAE----------VEQAELRAKALRIEAEAELEKLRKRQELE--------LEYEQAQNELEIAKA---- 779
|
170 180
....*....|....*....|....
gi 1988774686 1881 KKSSEAEMERQKAIVD----DTLK 1900
Cdd:PTZ00491 780 KELADIEATKFERIVEalgrETLI 803
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1388-1609 |
8.15e-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: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1388 IAAVDAEKQKTNIQLELQELKNLSEQ---QIKDKSQQVDEAlhsrtkiEEEIRLIRIQLETTEKQKYTAESELKQLRDRA 1464
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAaqaELDALQAELEEL-------NEEYNELQAELEALQAEIDKLQAEIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1465 AEA-EKLRKLAQDEAEK------------------------LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQkalED 1519
Cdd:COG3883 82 EERrEELGERARALYRSggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKL---AE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1520 LEKLRMQAEEAERQVKQAEIEKEKQIkvaheaaqksaaAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQ 1599
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALL------------AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
250
....*....|
gi 1988774686 1600 EDAENSREEA 1609
Cdd:COG3883 227 AAAAAAAAAA 236
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
23-88 |
8.15e-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: 8.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 23 KKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREK----GRMRFHKLQNVQIALDFL 88
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1453-1612 |
8.20e-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: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1453 AESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQA----EEELKRKSEAEKEAAKQKQKALE-DLEKLRMQA 1527
Cdd:pfam04012 34 MQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAAltkgNEELAREALAEKKSLEKQAEALEtQLAQQRSAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1528 EEAERQV-----KQAEIEKEKQIKVAHEAAQKSAAAELQSKH-MSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQED 1601
Cdd:pfam04012 114 EQLRKQLaaletKIQQLKAKKNLLKARLKAAKAQEAVQTSLGsLSTSSATDSFERIEEKIEEREARADAAAELASAVDLD 193
|
170
....*....|.
gi 1988774686 1602 AENSREEAEKE 1612
Cdd:pfam04012 194 AKLEQAGIQME 204
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1771-1901 |
8.25e-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: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1771 LEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAarqRAEAERILKEklaAISEATRLKTEaeiALKEKEAENERLRR 1850
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEA---RAEAAEIIAE---ARKEAEAIAEE---AKAEAEAEAERIIA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774686 1851 QAEDEAYQ-----RKALEDQASQHKQEIEEKIVQlkksSEAEMERQKAIVDDTLKQ 1901
Cdd:COG0711 100 QAEAEIEQerakaLAELRAEVADLAVAIAEKILG----KELDAAAQAALVDRFIAE 151
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
130-243 |
8.28e-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: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 130 DIQVNGQSEDMTAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVA 208
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQ---NKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKpVTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|....*
gi 1988774686 209 EKDLGVTRLLDPEDVDVPHPDEKSIITYVSSLYDA 243
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1447-1615 |
8.71e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1447 EKQKYTAESELKQLRDRA-AEAEKLRKL----AQDEAEKLRKQVSEETQKKR-----------QAEEELKRKSeaekEAA 1510
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAkKEAEAIKKEalleAKEEIHKLRNEFEKELRERRnelqklekrllQKEENLDRKL----ELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1511 KQKQKALEDLEKlRMQAEEAERQVKQAEIEK--EKQIKVAHEAAQksaaaelqskhMSFAEKTSKLEESLKQEhgavlqL 1588
Cdd:PRK12704 106 EKREEELEKKEK-ELEQKQQELEKKEEELEEliEEQLQELERISG-----------LTAEEAKEILLEKVEEE------A 167
|
170 180
....*....|....*....|....*..
gi 1988774686 1589 QQEAERLKKQQEdaENSREEAEKELEK 1615
Cdd:PRK12704 168 RHEAAVLIKEIE--EEAKEEADKKAKE 192
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1527-2001 |
8.96e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1527 AEEAERQVKQA-EIEKEKQIKVAHEAAQKSAAAELQSKhmsfAEKTSKLEESLKQEHGAV---LQLQQEAERLKKQQEDA 1602
Cdd:PRK04863 278 ANERRVHLEEAlELRRELYTSRRQLAAEQYRLVEMARE----LAELNEAESDLEQDYQAAsdhLNLVQTALRQQEKIERY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1603 ENSREEAEKELEkwrqkanEALRLRLQAEDEAhkktlaqeeaekqkeeAEREAKKRAkAEESALK-QKEMA--EEELERQ 1679
Cdd:PRK04863 354 QADLEELEERLE-------EQNEVVEEADEQQ----------------EENEARAEA-AEEEVDElKSQLAdyQQALDVQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1680 --RKIAESTAQQKLTAEQELIRLRA-DFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKA 1756
Cdd:PRK04863 410 qtRAIQYQQAVQALERAKQLCGLPDlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEV 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1757 EKETMSNTEKSkqlLEAEAAKMKDLAEEASRLRAISEEAKhQRQIAEEEAARQRAEAERILKEKLAAISEATRLkteaei 1836
Cdd:PRK04863 490 SRSEAWDVARE---LLRRLREQRHLAEQLQQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQL------ 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1837 aLKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEE--KIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKL 1914
Cdd:PRK04863 560 -QEELEARLESLSESVSEARERRMALRQQLEQLQARIQRlaARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLE 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1915 NfEKassgkldlELELNKlkniaDETQQSKIRAEEEAEKLRklaleeekrrreaeekvkkiaaaeeeaarQRKAAleELE 1994
Cdd:PRK04863 639 R-ER--------ELTVER-----DELAARKQALDEEIERLS-----------------------------QPGGS--EDP 673
|
....*..
gi 1988774686 1995 RLRKKAE 2001
Cdd:PRK04863 674 RLNALAE 680
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1459-1715 |
1.02e-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: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1459 QLRDRAAEAEKLRKLAQDEAEKLRKQVSEetqkKRQAEEELKRKS-----EAEKEAAKQKQKALED-LEKLRMQAEEAER 1532
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEE----AEAALEEFRQKNglvdlSEEAKLLLQQLSELESqLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1533 QVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKkqqedaensreeaeke 1612
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALR---------------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1613 lekwRQKANEALRLRLQAEDEAhkktlaqeeaekqkeeaereakKRAKAEESALKQkemaeeELERQRKIAESTAQQklt 1692
Cdd:COG3206 305 ----AQLQQEAQRILASLEAEL----------------------EALQAREASLQA------QLAQLEARLAELPEL--- 349
|
250 260
....*....|....*....|....
gi 1988774686 1693 aEQELIRLRADFDNAEQQ-RSLLE 1715
Cdd:COG3206 350 -EAELRRLEREVEVARELyESLLQ 372
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1719-2034 |
1.12e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.41 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1719 YRL-KNEVAAAQQQRKQleDELAKVRSEMDILIQLKTKAEKEtmsntEKSKQLLEAEAAKMKD-LAEEASRLRAISEEAK 1796
Cdd:PRK05035 431 YRQaKAEIRAIEQEKKK--AEEAKARFEARQARLEREKAARE-----ARHKKAAEARAAKDKDaVAAALARVKAKKAAAT 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1797 HQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAedeayqRKALEDQASQhkqEIEEK 1876
Cdd:PRK05035 504 QPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKA------KKAAQQAANA---EAEEE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1877 IVQLKKSSEAEMERQKAivddtlkqrrvveeeiRILKLNFEKASSGKLDLELELNKlkniadetqqSKIRAEEEAEKLRK 1956
Cdd:PRK05035 575 VDPKKAAVAAAIARAKA----------------KKAAQQAASAEPEEQVAEVDPKK----------AAVAAAIARAKAKK 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1957 LALEEEKRRREAEEKvkkiaaaeeeaarqRKAALE-ELERLR-KKAEEARKQKDEADKEAE-KQIVVAQQAAQKCSAAEQ 2033
Cdd:PRK05035 629 AEQQANAEPEEPVDP--------------RKAAVAaAIARAKaRKAAQQQANAEPEEAEDPkKAAVAAAIARAKAKKAAQ 694
|
.
gi 1988774686 2034 Q 2034
Cdd:PRK05035 695 Q 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1770-2016 |
1.16e-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: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1770 LLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEeAARQRAEAERILKEKLAAISEATRL--KTEAEIALKEKEAE--N 1845
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAelE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1846 ERLRRQAEDEAYQRKALEDQ--ASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRvveEEIRILKLNFEKASSGK 1923
Cdd:COG4942 90 KEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR---EQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1924 LDLELELNKLKNIADETQQSKIRAEEEAEKLRKLAleeekrrREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEA 2003
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLL-------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
250
....*....|...
gi 1988774686 2004 RKQKDEADKEAEK 2016
Cdd:COG4942 240 AERTPAAGFAALK 252
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1392-1805 |
1.16e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.54 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1392 DAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESEL--KQLRDRAAEAEK 1469
Cdd:COG5022 814 SYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELaeRQLQELKIDVKS 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1470 LRKLA----QDEAE--KLRKQVSEETQKKRQA-------EEELKRKSEAEKEAAKQKQKaLEDLEKLRMQ-------AEE 1529
Cdd:COG5022 894 ISSLKlvnlELESEiiELKKSLSSDLIENLEFkteliarLKKLLNNIDLEEGPSIEYVK-LPELNKLHEVesklketSEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1530 AERQVKQAEIEKEKQIKVAHEAAQ-KSAAAELQSKHMSFAEKTSkleeSLKQEHGAVLQLQQEAERLKkqQEDAENSREE 1608
Cdd:COG5022 973 YEDLLKKSTILVREGNKANSELKNfKKELAELSKQYGALQESTK----QLKELPVEVAELQSASKIIS--SESTELSILK 1046
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1609 AEKELEKWRQKANEALRLRLQAEDEAhKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQ 1688
Cdd:COG5022 1047 PLQKLKGLLLLENNQLQARYKALKLR-RENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKL 1125
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1689 QKLTAEQELIRLRADF-DNAEQQRSLLEDELYRLKNEvaaaqqqrKQLEDELAKVRsemdiLIQLKTKAEKETMSNTEKS 1767
Cdd:COG5022 1126 NLLQEISKFLSQLVNTlEPVFQKLSVLQLELDGLFWE--------ANLEALPSPPP-----FAALSEKRLYQSALYDEKS 1192
|
410 420 430
....*....|....*....|....*....|....*...
gi 1988774686 1768 KQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEE 1805
Cdd:COG5022 1193 KLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEG 1230
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
22-119 |
1.18e-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: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 22 QKKTFTKWVN---------KHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 88
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1988774686 89 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 119
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1329-1596 |
1.22e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 48.05 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1329 EEKAAEKLKAEErkKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNiqlELQELK 1408
Cdd:PRK07735 38 EEENREKEKALP--KNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAA---ALAKQK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1409 NLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEklrklAQDEAEKLRKqvsee 1488
Cdd:PRK07735 113 REGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAA-----AKAKAAALAK----- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1489 tQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSfa 1568
Cdd:PRK07735 183 -QKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAKTKGAE-- 259
|
250 260 270
....*....|....*....|....*....|
gi 1988774686 1569 ektSKLEESLKQEHGAVLQ--LQQEAERLK 1596
Cdd:PRK07735 260 ---GKKEEEPKQEEPSVNQpyLNKYVEVIK 286
|
|
| SH3_and_anchor |
TIGR04211 |
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ... |
2156-2245 |
1.28e-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: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2156 QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLknkiEEENQRLIKKDKDST 2235
Cdd:TIGR04211 70 ELQQELAELQEELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIKQISANAIEL----DEENRELREELAELK 145
|
90
....*....|
gi 1988774686 2236 QKLLAEEAEN 2245
Cdd:TIGR04211 146 QENEALEAEN 155
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2135-2336 |
1.28e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2135 QADTEMAKHKKLAEQTL---KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQR------GQVEEELFK 2205
Cdd:PRK11281 53 LLEAEDKLVQQDLEQTLallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2206 VKVQMEEllkLKNKIEEENQRLIkkdkdsTQKLLAEEA-----ENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRAL 2280
Cdd:PRK11281 133 TLDQLQN---AQNDLAEYNSQLV------SLQTQPERAqaalyANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQAL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 2281 AEKMLKEKMQAIQEASRLKaeaEMLQKQKDLAQEQAQKLLEDKQLMQ-----QRLeEETEE 2336
Cdd:PRK11281 204 LNAQNDLQRKSLEGNTQLQ---DLLQKQRDYLTARIQRLEHQLQLLQeainsKRL-TLSEK 260
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1590-1811 |
1.30e-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: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1590 QEAERLKKQQEDAENSREEAEKELEkwrQKAnEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQK 1669
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLE---QQA-EEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1670 EMAEEELERQRK-IAESTAQQKLTAEQELIRLRADFDNAEQQRsllEDELYRLKNEVAAAQQQRKQLEDELAKVRSEmdi 1748
Cdd:TIGR02794 126 AKQAAEAKAKAEaEAERKAKEEAAKQAEEEAKAKAAAEAKKKA---EEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE--- 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 1749 liQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRA 1811
Cdd:TIGR02794 200 --AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1254-1486 |
1.32e-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: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1254 AKAYIDTIKDYELQLVAYKAQVEPLVSPLKKTKldSASDNIIQEYVTLRTRYSELMTL---TSQYIKFITDTQRRLDDEE 1330
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALK--KEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1331 KAAEKLKAEERKKMAEMQAELdkQKQLAEAHAKAIAKAEKEAQELK-LKMQEEVSKREIAAVDAEKQKTNiqlELQELKN 1409
Cdd:COG4942 93 AELRAELEAQKEELAELLRAL--YRLGRQPPLALLLSPEDFLDAVRrLQYLKYLAPARREQAEELRADLA---ELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774686 1410 LSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKL-RKLAQDEAEKLRKQVS 1486
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiARLEAEAAAAAERTPA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1674-2196 |
1.34e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1674 EELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQ--QQRKQLEDELAKVRSEmdiliq 1751
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPER------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1752 lktkaeketmsntekskqlLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLK 1831
Cdd:COG4717 148 -------------------LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1832 TEAEIALKEKEAENERLRRQAEDEayqrkaledQASQHKQEIEEKIVQLKKSSEAEmerqKAIVDDTLKQRRVVEEEIRI 1911
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQL---------ENELEAAALEERLKEARLLLLIA----AALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1912 LKLNFekASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALeeekrrreaeekvKKIAAAEEEAARQRKAALE 1991
Cdd:COG4717 276 AGVLF--LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEL-------------EELLAALGLPPDLSPEELL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1992 ELERLRKKAEEARKQKDEADKEAEKQivvaqqaaqkcsAAEQQVQSVLAQQIEDSItqkklkEEYEKAKKLAKEAEAAKE 2071
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLE------------ELEQEIAALLAEAGVEDE------EELRAALEQAEEYQELKE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2072 KAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAakraqaeaaalMQKQQADTEMAKHKKLAEQTL 2151
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEE-----------LREELAELEAELEQLEEDGEL 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 2152 KQKfqvEQELTKVKLKLDETDKQ-------KSVLDEELQRLKDEVDDAVKQR 2196
Cdd:COG4717 472 AEL---LQELEELKAELRELAEEwaalklaLELLEEAREEYREERLPPVLER 520
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2271-2545 |
1.38e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2271 EDDLNQQRALAEKMLKE----KMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEEteeyhksleveRK 2346
Cdd:COG1340 10 LEELEEKIEELREEIEElkekRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL-----------KE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2347 RQLEIMAEAERLRLQVSQLSEAQARAEEEA---KKFKKQADKVATRLHETEIATQEKMTVVERLE--FERLNTSKEADDL 2421
Cdd:COG1340 79 ERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKelEKELEKAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2422 RKAIADLENEKARLKKEAEELQNKSKEMADAQQKKieHEKtvlqqtfMTEkemLLKKEKLIEDEKKRLESQFEEEVKKAK 2501
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQEL--HEE-------MIE---LYKEADELRKEADELHKEIVEAQEKAD 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1988774686 2502 ALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKE 2545
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 ... |
1490-1622 |
1.40e-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: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1490 QKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEaerqvkqaeiekekqikvaheaAQKSAAAELQsKHMSFAE 1569
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIARE----------------------AQQNYERELV-LHAEDIK 57
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 1570 KTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANE 1622
Cdd:pfam07926 58 ALQALREELNELKAEIAELKAEAESAKAELEESEESWEEQKKELEKELSELEK 110
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
28-118 |
1.41e-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: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 28 KWVNKHLIKAQR---HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM---RFHKLQNVQIALDFLRhrQVKLVN-IRN 100
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
|
90
....*....|....*...
gi 1988774686 101 DDIADGNPKLTLGLIWTI 118
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
905-1500 |
1.41e-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: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 905 RLIMRNLELHYQDFMRDSQDSQLFGPDDRMQVEDDYTKSTQHFDNLLRSmeKGQQNETLCKNYISELKDLRLRIEDCEAG 984
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ--KLEERSQKESKARSGLKVLLALIKDGVGG 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 985 TVARIRKPVEKEPLKEYIQKTTEQKKVQGELDGLKKDLDKVSVKTQEVLASPQPSASAPVLRSELDLTVQKMDHAHMLSS 1064
Cdd:pfam02463 523 RIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPI 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1065 VYLEKLKTVEMVIRNTQGAEGVLKQYEDCLREVHTVPSDVKEVETYRAK-------LKKMRTEAEDEQPVFDSLEEELKK 1137
Cdd:pfam02463 603 LNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGvsleeglAEKSEVKASLSELTKELLEIQELQ 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1138 ASAVSDKMVRVHSERDVELDhFRQQLSSLQDRWKAVFTQIDLRQRELEQLGRQLGYYREsydwLIRWIADAKQRQEKIQA 1217
Cdd:pfam02463 683 EKAESELAKEEILRRQLEIK-KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKL----LKQKIDEEEEEEEKSRL 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1218 VPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKayidtIKDYELQLVAYKAQVEPLVSPLKKTKLDSASDNIIQE 1297
Cdd:pfam02463 758 KKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEK-----LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKE 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1298 YVTLRTRYSELMTLTSQYiKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQlaeahakaiaKAEKEAQELKL 1377
Cdd:pfam02463 833 EELEELALELKEEQKLEK-LAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES----------KEEKEKEEKKE 901
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1378 KMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESEL 1457
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1988774686 1458 KQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELK 1500
Cdd:pfam02463 982 EFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
2156-2579 |
1.42e-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: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2156 QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDST 2235
Cdd:pfam09730 38 ELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRDEIKEYKVREARLLQDYSELEEENISLQKQVSVLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2236 QKLLAEEA--ENMRKLAEDAARLSVEAQEAARLRQIaeddlnqqralAEKMLKEKMQAIQEASRLKAeaemlqkqkDLAQ 2313
Cdd:pfam09730 118 QNQVEFEGlkHEITRKEEETELLNSQLEEAIRLREI-----------AERQLDEALETLKTEREQKN---------SLRK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2314 EQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLhet 2393
Cdd:pfam09730 178 ELSHYMTLNDFDYVSHLSISLDGLKFSEDEGAGTEPNNDGEAMDGGENGGGGLKNSGLDNRTSTPRKSEVFPPAPSL--- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2394 eiatqekmtvVERLeFERLNTSkEADDLRKAIADLENEKARLKKEAEELQnksKEMADAQQKKIEHEKTVLQqtfMTEKE 2473
Cdd:pfam09730 255 ----------VSDL-LSELNIS-EIQKLKQQLIQVEREKVSLLSTLQESQ---KQLEQAKGALSEQQEKVNR---LTENL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2474 MLLKKEKLIEDEKKRLESqfeEEVKKAKALKDEQERQKQQMEqekkTLQATMDAALSKQKEAEEEMLRKQKEMQELERQR 2553
Cdd:pfam09730 317 EAMRGLQASKERQDALDS---EKDRDSHEDGDYYEVDINGPE----ILECKYRVAVEEAGELREELKALKARYNTLEERY 389
|
410 420
....*....|....*....|....*.
gi 1988774686 2554 LEQERILAEENQKLREKLQQLEDAQK 2579
Cdd:pfam09730 390 KEEKTRWEAEAQDLAEKIRQLEKASH 415
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1500-1911 |
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 1988774686 1500 KRKSEAEKEAAKQKQKALEDLEKLRMQAEE----AERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLE 1575
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEaeqkAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1576 ESLKQEHGAVLQLQQEAERLKKQQEDAENSREEA----EKELEKWRQKANEALRLRLQAE-DEAHKKTLAQEEAEKQKEE 1650
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAaaaeKEKAEEAKRKAEEEAKRKAEEErKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1651 AEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 1730
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1731 QRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQR 1810
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1811 AEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMER 1890
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGL 400
|
410 420
....*....|....*....|.
gi 1988774686 1891 QKAIVDDTLKQRRVVEEEIRI 1911
Cdd:COG3064 401 LGLRLDLGAALLEAASAVELR 421
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1481-1769 |
1.49e-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: 47.98 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1481 LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAE-EAERQVKQAEIEKEKqIKVAHEAAQKSAAAE 1559
Cdd:pfam15964 319 VRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELErQKERLEKELASQQEK-RAQEKEALRKEMKKE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1560 ---LQSKHMSFAEKTSKLEESL----KQEHGAVLQLQQEAERLKKQQED--------------AENSREEAEKELEKWRQ 1618
Cdd:pfam15964 398 reeLGATMLALSQNVAQLEAQVekvtREKNSLVSQLEEAQKQLASQEMDvtkvcgemryqlnqTKMKKDEAEKEHREYRT 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1619 KANEALRLrlqAEDEAHKKTLAQEEAEKQKEEAEREAkkrAKAEESALKQKEMAEE--------ELER---QRKIAESTA 1687
Cdd:pfam15964 478 KTGRQLEI---KDQEIEKLGLELSESKQRLEQAQQDA---ARAREECLKLTELLGEsehqlhltRLEKesiQQSFSNEAK 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1688 QQKLTAEQELIRLRADFDNAEQQRSLLEDELYRL---KNEVAAAQQQR-----KQLEDELAKVRSEMDILIQ----LKTK 1755
Cdd:pfam15964 552 AQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLltsQNTFIAKLKEEcctlaKKLEEITQKSRSEVEQLSQekeyLQDR 631
|
330
....*....|....
gi 1988774686 1756 AEKETMSNTEKSKQ 1769
Cdd:pfam15964 632 LEKLQKRNEELEEQ 645
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1491-1824 |
1.56e-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: 47.22 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1491 KKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQaeiEKEKQIKVAHEAAQKSAAAELQSKHMsfaek 1570
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQ---ELEEQIEEREQKRQEEYEEKLQEREQ----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1571 tskLEESLKQEHgavLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKtlaqeeaekqkeE 1650
Cdd:pfam13868 103 ---MDEIVERIQ---EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKE------------K 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1651 AEREAKKRAKAEEsalkQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 1730
Cdd:pfam13868 165 AEREEEREAEREE----IEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1731 QRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQR 1810
Cdd:pfam13868 241 REEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERL 320
|
330
....*....|....
gi 1988774686 1811 AEAERILKEKLAAI 1824
Cdd:pfam13868 321 REEEAERRERIEEE 334
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1585-1909 |
1.64e-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: 47.34 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1585 VLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRL-------QAEDEAHKKTLAQEEAEKQKEEAEREAKK 1657
Cdd:pfam15558 13 MLARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLqqsqeqwQAEKEQRKARLGREERRRADRREKQVIEK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1658 RAKAEESALKQKEMAEEELERQRKIAESTAQ---QKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVaaAQQQRKQ 1734
Cdd:pfam15558 93 ESRWREQAEDQENQRQEKLERARQEAEQRKQcqeQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKER--EEQKKVQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1735 LEDELAKVRSE-MDILIQLKTKAEKETMSNT---------EKSKQLLEAEAAKMKDLA----EEASRLRAISEEAKHQRQ 1800
Cdd:pfam15558 171 ENNLSELLNHQaRKVLVDCQAKAEELLRRLSleqslqrsqENYEQLVEERHRELREKAqkeeEQFQRAKWRAEEKEEERQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1801 ------IAEEEAARQRAE--AERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKaledqasqhkqe 1872
Cdd:pfam15558 251 ehkealAELADRKIQQARqvAHKTVQDKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKK------------ 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 1988774686 1873 iEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEI 1909
Cdd:pfam15558 319 -EQRSEQISREKEATLEEARKTARASFHMREKVREET 354
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1482-1621 |
1.78e-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: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1482 RKQvsEETQKKRQAEEELKRKSEAEKEAAKQ--KQKALEDLEKlrmqaeeaerqvKQAEIEKEKQIKVAHEAAQKSAAAE 1559
Cdd:pfam13904 63 AKQ--RQRQKELQAQKEEREKEEQEAELRKRlaKEKYQEWLQR------------KARQQTKKREESHKQKAAESASKSL 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774686 1560 LQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSR--EEAEKELEKWRQKAN 1621
Cdd:pfam13904 129 AKPERKVSQEEAKEVLQEWERKKLEQQQRKREEEQREQLKKEEEEQErkQLAEKAWQKWMKNVK 192
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1356-1555 |
1.87e-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: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1356 QLAEAHAKAIAKAEKEAQELKLKMQEEVSkreiaavdaekqktniqlELQELKNLSEQQIKDKSQQVDEALHSRTKIEEE 1435
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQQREEELE------------------ELQEQLEDLESSIQELEKEIKKLESSIKQVEEE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1436 IRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLrKQVSEETQKKRQAE-EELKRKSEAEKEAAKQKQ 1514
Cdd:pfam05667 372 LEELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRL-VELAGQWEKHRVPLiEEYRALKEAKSNKEDESQ 450
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1988774686 1515 KALEDLEKLRMQAEEAERQVKQAEiEKEKQIKVAHEAAQKS 1555
Cdd:pfam05667 451 RKLEEIKELREKIKEVAEEAKQKE-ELYKQLVAEYERLPKD 490
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2152-2333 |
1.87e-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: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2152 KQKFQ--VEQELTKVKLKLDETDKQKSV--LDEELQRLKDEVDDAVKQ---------------RGQVEEELFKVK---VQ 2209
Cdd:cd16269 88 DQKFQkkLMEQLEEKKEEFCKQNEEASSkrCQALLQELSAPLEEKISQgsysvpggyqlyledREKLVEKYRQVPrkgVK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2210 MEELLK--LKNKIEEENQRLiKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAaRLRQIAEDdlnQQRALAE--KML 2285
Cdd:cd16269 168 AEEVLQefLQSKEAEAEAIL-QADQALTEKEKEIEAERAKAEAAEQERKLLEEQQR-ELEQKLED---QERSYEEhlRQL 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1988774686 2286 KEKMQaiQEASRLKAEAEMLQKQKDlaQEQAQKLLEDKQLMQQRLEEE 2333
Cdd:cd16269 243 KEKME--EERENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEE 286
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1479-1672 |
1.95e-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: 47.30 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1479 EKLRKQVSEETQKKRQAEEELKRKSEaekEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAA 1558
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDLKERESQ---EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1559 ELQSKHMSFAEKtSKLEESLKQEhgavlqlqqeaerLKKQQEDAENSREEAEKELEkwrQKANEALRLRLQAEDEAHKKT 1638
Cdd:pfam05262 261 PKPADTSSPKED-KQVAENQKRE-------------IEKAQIEIKKNDEEALKAKD---HKAFDLKQESKASEKEAEDKE 323
|
170 180 190
....*....|....*....|....*....|....
gi 1988774686 1639 LAQEEAEKQKEEAEREAKKRAKAEESALKQKEMA 1672
Cdd:pfam05262 324 LEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAID 357
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2784-2820 |
1.95e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 1.95e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1988774686 2784 IRVLEAQLATGGIIDPINSHRVPTETAYKQGHYDAEM 2820
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1781-1954 |
2.01e-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: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1781 LAEEASRLRAiSEEAKHQRQIAEEEAARQRAEAERI---LKEKLAAISEATRLKTEAEIALKEKEAENERLRrqaEDEAY 1857
Cdd:pfam07888 40 LQERAELLQA-QEAANRQREKEKERYKRDREQWERQrreLESRVAELKEELRQSREKHEELEEKYKELSASS---EELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1858 QRKALEDQASQHKQEIEE------KIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELN 1931
Cdd:pfam07888 116 EKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170 180
....*....|....*....|...
gi 1988774686 1932 KLKNIADETQQSKIRAEEEAEKL 1954
Cdd:pfam07888 196 ELRNSLAQRDTQVLQLQDTITTL 218
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2389-2553 |
2.11e-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: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2389 RLHETEIATQEKMTVVERLE--FERLNTSKEADDLRKAIADLENEKARLKKEAEELQnksKEMADAQQKKIEHEKTVLQQ 2466
Cdd:COG4913 259 ELAERYAAARERLAELEYLRaaLRLWFAQRRLELLEAELEELRAELARLEAELERLE---ARLDALREELDELEAQIRGN 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2467 TFmTEKEMLLKKEKLIEDEKKRLE---SQFEEEVKKA-----------KALKDEQERQKQQMEQEKKTLQATMDAALSKQ 2532
Cdd:COG4913 336 GG-DRLEQLEREIERLERELEERErrrARLEALLAALglplpasaeefAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
170 180
....*....|....*....|.
gi 1988774686 2533 KEAEEEMLRKQKEMQELERQR 2553
Cdd:COG4913 415 RDLRRELRELEAEIASLERRK 435
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1767-1910 |
2.15e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1767 SKQLLEAEAAKMKDLAEEASRLRAISEEAKHQrqiAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENE 1846
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLE---AKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774686 1847 RLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKsseaEMERQKAIVDDTLKQR--RVVEEEIR 1910
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEAR 168
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3035-3070 |
2.28e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.28e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1988774686 3035 LNLLEAQAGTGYLVDPVHNQKYTVDEAVKAGVVGPE 3070
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2158-2595 |
2.28e-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: 47.32 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2158 EQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIeeeNQRLIKKDKDStqK 2237
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKF---LTEIKKKEKEL--E 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2238 LLAEEAENMRKLAEDaarlsVEAQEAARLRQIAE-----DDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKdla 2312
Cdd:TIGR04523 156 KLNNKYNDLKKQKEE-----LENELNLLEKEKLNiqkniDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQN--- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2313 qeqaQKLLEDKQLMQQRLEEETEEYHKSLEverkrqleimaeaerlrlQVSQLseaqaraeeeakkfKKQADKVATRLhe 2392
Cdd:TIGR04523 228 ----NQLKDNIEKKQQEINEKTTEISNTQT------------------QLNQL--------------KDEQNKIKKQL-- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2393 teiatQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKAR--LKKEAEELQNKSKEMADAQQKKIEHEKTVLQqtfMT 2470
Cdd:TIGR04523 270 -----SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQ---LN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2471 EKEMLLKKEKL-IEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQekktlqatmdaaLSKQKEAEEEMLRKQKEMQEL 2549
Cdd:TIGR04523 342 EQISQLKKELTnSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN------------LESQINDLESKIQNQEKLNQQ 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1988774686 2550 ERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDII 2595
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4363-4400 |
2.33e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.33e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1988774686 4363 QRFLEVQYLTGGLIEPDVEGRVSIDESIRKGTIDARTA 4400
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2290-2458 |
2.36e-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: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2290 QAIQEASRLKAEAEmlqKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQlEIMAEAERLRLQVSQlseAQ 2369
Cdd:COG2268 196 EIIRDARIAEAEAE---RETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKA-EERREAETARAEAEA---AY 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2370 ARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEferlntskeADDLRKAIADLENEKARLKKEAEELQNKSKEM 2449
Cdd:COG2268 269 EIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELE---------ADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAE 339
|
....*....
gi 1988774686 2450 ADAQQKKIE 2458
Cdd:COG2268 340 AEGKRALAE 348
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1663-1957 |
2.44e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1663 ESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKV 1742
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1743 RSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLA 1822
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1823 AISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQR 1902
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774686 1903 RVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKL 1957
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADL 342
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1529-1779 |
2.55e-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: 45.97 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1529 EAERQvkqaEIEKEKQIKVAHEAAqksaaaELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREE 1608
Cdd:pfam17045 5 EAELQ----ELMKQIDIMVAHKKS------EWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1609 AEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKR--AKAEESALKQKEMAEEELERQRKIAEST 1686
Cdd:pfam17045 75 LVAKYEQQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRlnGKLEEFRQKSLEWEQQRLQYQQQVASLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1687 AQQKLTAEQ-ELIRLRADFDNAEQQRSLLED---ELYRLKNEVAAAQQQRKQLEDELAKVRSEMDIL------IQLKTKA 1756
Cdd:pfam17045 155 AQRKALAEQsSLIQSAAYQVQLEGRKQCLEAsqsEIQRLRSKLERAQDSLCAQELELERLRMRVSELgdsnrkLLEEQQR 234
|
250 260
....*....|....*....|...
gi 1988774686 1757 EKETMSNTEKSKQLLEAEAAKMK 1779
Cdd:pfam17045 235 LLEELRMSQRQLQVLQNELMELK 257
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1743-2538 |
2.56e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1743 RSEMDILIQLKTKAEKETMS---NTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEeAARQR--------- 1810
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTsrrQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQT-ALRQQekieryqad 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1811 -AEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDeaYQRkALEDQ---ASQHKQEIE--EKIVQLKKSS 1884
Cdd:PRK04863 357 lEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAD--YQQ-ALDVQqtrAIQYQQAVQalERAKQLCGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1885 EAEMERQKAIVDDTLKQRRVVEEEIRIL--KLNFEKASSGKLDLELELnkLKNIADET-----QQSKIRAEEEAEKLRKL 1957
Cdd:PRK04863 434 DLTADNAEDWLEEFQAKEQEATEELLSLeqKLSVAQAAHSQFEQAYQL--VRKIAGEVsrseaWDVARELLRRLREQRHL 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1958 AleeekrrreaeekvkkiaaaeeEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQS 2037
Cdd:PRK04863 512 A----------------------EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLES 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2038 vLAQQIEDSITQKklkeeyekakklakeaeaakekaereaALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRkeAEF 2117
Cdd:PRK04863 570 -LSESVSEARERR---------------------------MALRQQLEQLQARIQRLAARAPAWLAAQDALARLR--EQS 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2118 EAAKRAQAEAAALMQKQQadtemakhKKLAEQTLkQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKD---------- 2187
Cdd:PRK04863 620 GEEFEDSQDVTEYMQQLL--------ERERELTV-ERDELAARKQALDEEIERLSQPGGSEDPRLNALAErfggvllsei 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2188 ----EVDDA---------------VKQRGQVEEEL-------------------FKVKVQMEELLKlKNKIEEENQRLIK 2229
Cdd:PRK04863 691 yddvSLEDApyfsalygparhaivVPDLSDAAEQLagledcpedlyliegdpdsFDDSVFSVEELE-KAVVVKIADRQWR 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2230 KDKDSTQKLLAEEAENMR---------KLAEDAARLSVEAQEAARLRQIAEDDLNQQRALA-----EKMLKEKMQAIQEA 2295
Cdd:PRK04863 770 YSRFPEVPLFGRAAREKRieqlraereELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVEL 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2296 SRLKAEAE----MLQKQKDLAQEQAQ---------KLLEDKQLmQQRLEEETEEYHKSLEVERK--------RQLEIMAE 2354
Cdd:PRK04863 850 ERALADHEsqeqQQRSQLEQAKEGLSalnrllprlNLLADETL-ADRVEEIREQLDEAEEAKRFvqqhgnalAQLEPIVS 928
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2355 A--------ERLRLQVSQLseaqaraEEEAKKFKKQADKVAtrlheteiatqekmTVVERLefERLNTSKEADDLRKAIA 2426
Cdd:PRK04863 929 VlqsdpeqfEQLKQDYQQA-------QQTQRDAKQQAFALT--------------EVVQRR--AHFSYEDAAEMLAKNSD 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2427 DLENEKARLkKEAEELQNKSKEMADAQQKKIEHEKTV---LQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEevkKAKAL 2503
Cdd:PRK04863 986 LNEKLRQRL-EQAEQERTRAREQLRQAQAQLAQYNQVlasLKSSYDAKRQMLQELKQELQDLGVPADSGAEE---RARAR 1061
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1988774686 2504 KDE-QER------QKQQMEQEKKTLQATMDAALSKQKEAEEE 2538
Cdd:PRK04863 1062 RDElHARlsanrsRRNQLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2317-2593 |
2.64e-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: 46.99 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2317 QKLLEDKQLMQQRLEEEteEYHKSLEVERKRQLeiMAEAERLRLQVSQLSEAQARAEEEAKKFKkQADKVATRLHEteia 2396
Cdd:pfam05622 3 SEAQEEKDELAQRCHEL--DQQVSLLQEEKNSL--QQENKKLQERLDQLESGDDSGTPGGKKYL-LLQKQLEQLQE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2397 tqekmtvverlEFERLNTSKeaDDLRKAIADLENEKARLKKEAEELQNKSKEmadAQQKKIEHEktVLQQTfmteKEMLL 2476
Cdd:pfam05622 74 -----------ENFRLETAR--DDYRIKCEELEKEVLELQHRNEELTSLAEE---AQALKDEMD--ILRES----SDKVK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2477 KKEKLIEDEKKRLES-----------------------QFEEEVKKAKALKDEQERQKQQMEQekktLQATMDAALSKQK 2533
Cdd:pfam05622 132 KLEATVETYKKKLEDlgdlrrqvklleernaeymqrtlQLEEELKKANALRGQLETYKRQVQE----LHGKLSEESKKAD 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2534 EAEEEMLRKQKEMQELERqrlEQERILAEENQkLREKLQQLEDAQKDQHTRETDKVLHKD 2593
Cdd:pfam05622 208 KLEFEYKKLEEKLEALQK---EKERLIIERDT-LRETNEELRCAQLQQAELSQADALLSP 263
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1321-2182 |
2.68e-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: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1321 DTQRRLDDEEKAAEKLkAEERKKMAEMQAELDKQKQLAEAH----AKAIAKAEK--------EAQELKLKMQEEVSK-RE 1387
Cdd:COG3096 296 GARRQLAEEQYRLVEM-ARELEELSARESDLEQDYQAASDHlnlvQTALRQQEKieryqedlEELTERLEEQEEVVEeAA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1388 IAAVDAEKQKTNIQLELQELKNlseqQIKDKSQQVDEaLHSRTkieeeirlirIQLETTEKQKYTAEsELKQLRDRAAEA 1467
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSLKS----QLADYQQALDV-QQTRA----------IQYQQAVQALEKAR-ALCGLPDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1468 eklrklAQDEAEKLRKQVSEETQKKRQAEEELkrkSEAEkEAAKQKQKALEDLEKL-----RMQAEEAERQVkqaeieke 1542
Cdd:COG3096 439 ------AEDYLAAFRAKEQQATEEVLELEQKL---SVAD-AARRQFEKAYELVCKIageveRSQAWQTAREL-------- 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1543 kqikVAHEAAQKSAAAELQSKHMSFAEktskLEESLKQEHGAVLQLQQEAERLKKQQEDA---ENSREEAEKELEKWRQK 1619
Cdd:COG3096 501 ----LRRYRSQQALAQRLQQLRAQLAE----LEQRLRQQQNAERLLEEFCQRIGQQLDAAeelEELLAELEAQLEELEEQ 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1620 ANEAL--RLRLQAEDEAHKktlaqeeaekqkeEAEREAKKRA----KAEESALKQKEMAEEELERQRKIAEsTAQQKLTA 1693
Cdd:COG3096 573 AAEAVeqRSELRQQLEQLR-------------ARIKELAARApawlAAQDALERLREQSGEALADSQEVTA-AMQQLLER 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1694 EQELIRLRadfDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVR-SEM--DILIqlktkaeketmsntekskql 1770
Cdd:COG3096 639 EREATVER---DELAARKQALESQIERLSQPGGAEDPRLLALAERLGGVLlSEIydDVTL-------------------- 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1771 leaeaakmkdlaEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAIS-------EATRLKTEAEIALKEKEA 1843
Cdd:COG3096 696 ------------EDAPYFSALYGPARHAIVVPDLSAVKEQLAGLEDCPEDLYLIEgdpdsfdDSVFDAEELEDAVVVKLS 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1844 ENE-RLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSS--EAEMERQKAIVDDTLKQRRVV------EEEIRILKl 1914
Cdd:COG3096 764 DRQwRYSRFPEVPLFGRAAREKRLEELRAERDELAEQYAKASfdVQKLQRLHQAFSQFVGGHLAVafapdpEAELAALR- 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1915 nfekASSGKLDLELElnklkNIADETQQSKIRAEEEAEKLRKLAleeekrrreaeekvKKIAAAEEEAARQRKAALEELE 1994
Cdd:COG3096 843 ----QRRSELERELA-----QHRAQEQQLRQQLDQLKEQLQLLN--------------KLLPQANLLADETLADRLEELR 899
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1995 RLRKKAEEAR---KQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQieDSITQKKLKEEYEKAKKLAKEAEAAKE 2071
Cdd:COG3096 900 EELDAAQEAQafiQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQ--RRLKQQIFALSEVVQRRPHFSYEDAVG 977
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2072 KAEREAAL---LRQQAEEAERQKTAAEEEAANQAKAQEDA-------------------ERLRKEAEFEAAKRAQAEAAA 2129
Cdd:COG3096 978 LLGENSDLnekLRARLEQAEEARREAREQLRQAQAQYSQYnqvlaslkssrdakqqtlqELEQELEELGVQADAEAEERA 1057
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 2130 LMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEEL 2182
Cdd:COG3096 1058 RIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1444-1865 |
2.70e-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: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1444 ETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKL 1523
Cdd:COG3064 30 EAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1524 RMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAE 1603
Cdd:COG3064 110 AEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1604 NSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIA 1683
Cdd:COG3064 190 VEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1684 ESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSN 1763
Cdd:COG3064 270 GAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1764 TEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEA 1843
Cdd:COG3064 350 AAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGA 429
|
410 420
....*....|....*....|..
gi 1988774686 1844 ENERLRRQAEDEAYQRKALEDQ 1865
Cdd:COG3064 430 AGAVVALLVKLVADLAGGLVGI 451
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2437-2579 |
2.79e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2437 KEAEELQNKSKEMADAQQKKiehEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQfEEEVKKAKALKDEQERQKQQMEQ 2516
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQR---KKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ-EQKKQAEEAAKQAALKQKQAEEA 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774686 2517 EKKTLQATMDAALSKQKEAEEemLRKQKEMQELERQRLEQERILAEENQKLRE---KLQQLEDAQK 2579
Cdd:PRK09510 138 AAKAAAAAKAKAEAEAKRAAA--AAKKAAAEAKKKAEAEAAKKAAAEAKKKAEaeaAAKAAAEAKK 201
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3405-3436 |
2.92e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.92e-04
10 20 30
....*....|....*....|....*....|..
gi 1988774686 3405 KLLSAEKAVTGYKDPFTGNKISLFEAMQKDLI 3436
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1509-1699 |
3.01e-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: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1509 AAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKekqikvaheAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQL 1588
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAEL---------AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1589 QQEAERLKKQQEDAENSRE--EAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESAL 1666
Cdd:COG1579 72 EARIKKYEEQLGNVRNNKEyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180 190
....*....|....*....|....*....|...
gi 1988774686 1667 KQKEMAEEELERQRKIAESTAQQKLTAEQELIR 1699
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 ... |
22-119 |
3.06e-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: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 22 QKKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 88
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1988774686 89 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 119
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1678-1904 |
3.49e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.86 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1678 RQRKiAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELyRLKnevAAAQQQRKQLEDE----LAKVRSEMDILIQLK 1753
Cdd:PRK05035 432 RQAK-AEIRAIEQEKKKAEEAKARFEARQARLEREKAAREA-RHK---KAAEARAAKDKDAvaaaLARVKAKKAAATQPI 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1754 TKAEKETMSNTEkskqllEAEAAKMKDLAEEASRLRAISEEAKHQRQiAEEEAARQRAEAERILKEKLAAISEATRLKTE 1833
Cdd:PRK05035 507 VIKAGARPDNSA------VIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKKAAQQAANAEAEEEVDPKK 579
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 1834 AEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDtlKQRRV 1904
Cdd:PRK05035 580 AAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDP--RKAAV 648
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2221-2361 |
3.75e-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: 46.48 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2221 EEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDdlnQQRALAEKMLKEKMQAIQEASRLKa 2300
Cdd:pfam15709 356 EQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEE---RKQRLQLQAAQERARQQQEEFRRK- 431
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 2301 eaeMLQKQKDLAQEQAQKLLEDKQlMQQRLEEETEEyhkslevERKRQLEiMAEAERLRLQ 2361
Cdd:pfam15709 432 ---LQELQRKKQQEEAERAEAEKQ-RQKELEMQLAE-------EQKRLME-MAEEERLEYQ 480
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1354-1545 |
3.78e-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: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1354 QKQLAEAHAKaIAKAEKEAQELKLK-----MQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQ---QIKDKSQQVDEA 1425
Cdd:COG3206 181 EEQLPELRKE-LEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAlraQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1426 LHSRTKIEEEIRLIRIQLE-TTEKQKYTAES-ELKQLRDRAAEAEK-LRKLAQDEAEKLRKQVSEETQKK---RQAEEEL 1499
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAElAELSARYTPNHpDVIALRAQIAALRAqLQQEAQRILASLEAELEALQAREaslQAQLAQL 339
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1988774686 1500 KRKSEAEKEAAkQKQKALE-DLEKLRMQAEEAERQVKQAEIEKEKQI 1545
Cdd:COG3206 340 EARLAELPELE-AELRRLErEVEVARELYESLLQRLEEARLAEALTV 385
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1464-1615 |
3.91e-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: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1464 AAEAEKLRKLAQ---------DEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQV 1534
Cdd:COG1579 3 PEDLRALLDLQEldseldrleHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1535 K-----------QAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAE 1603
Cdd:COG1579 83 GnvrnnkeyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|..
gi 1988774686 1604 NSREEAEKELEK 1615
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1205-1483 |
4.00e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1205 IADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKK 1284
Cdd:COG1340 24 IEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1285 TKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKaEERKKMAEMQAELDKQKQLAEAHAKA 1364
Cdd:COG1340 104 LNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKAL-EKNEKLKELRAELKELRKEAEEIHKK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1365 IAKAEKEAQELKLKMQEEVSKREiaavdaekqktniqlELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLE 1444
Cdd:COG1340 183 IKELAEEAQELHEEMIELYKEAD---------------ELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
250 260 270
....*....|....*....|....*....|....*....
gi 1988774686 1445 TTEKQKYTAEselkqlrdRAAEAEKLRKLAQDEAEKLRK 1483
Cdd:COG1340 248 KLRKKQRALK--------REKEKEELEEKAEEIFEKLKK 278
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1205-1431 |
4.01e-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: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1205 IADAKQRQEKIQAvpitdskTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKK 1284
Cdd:COG3883 25 LSELQAELEAAQA-------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1285 TKLDSASDNII---QEYVTLRTRYSelmtltsqYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAH 1361
Cdd:COG3883 98 SGGSVSYLDVLlgsESFSDFLDRLS--------ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 1362 AKAI--AKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTK 1431
Cdd:COG3883 170 KAELeaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1431-1548 |
4.06e-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: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1431 KIEEEIRLIRIQLETtEKQKYTAESELKQLRDRAAEAEklRKLAQDEAEKLRkQVSEETQKKRQAEEE-LKRKSEAEKEA 1509
Cdd:cd03406 159 KIPEAIRRNYEAMEA-EKTKLLIAEQHQKVVEKEAETE--RKRAVIEAEKDA-EVAKIQMQQKIMEKEaEKKISEIEDEM 234
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1988774686 1510 AKQKQKALEDLE--KLRMQAEEAERQVKQAEIEKEKQIKVA 1548
Cdd:cd03406 235 HLAREKARADAEyyRALREAEANKLKLTPEYLELKKYQAIA 275
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1112-1524 |
4.21e-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: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1112 AKLKKMRTEAEDeqpvfdsLEEELKKASAVSDKMVRVHSerdveldHFRQQLSSLQDRW-----KAVFTQIDLRQRELEq 1186
Cdd:COG3096 785 KRLEELRAERDE-------LAEQYAKASFDVQKLQRLHQ-------AFSQFVGGHLAVAfapdpEAELAALRQRRSELE- 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1187 lgRQLGYYResydwlirwiADAKQRQEKIQAvpitdsktLKEQLAQEKKLL------------EEIEQNKDKVDECQkYA 1254
Cdd:COG3096 850 --RELAQHR----------AQEQQLRQQLDQ--------LKEQLQLLNKLLpqanlladetlaDRLEELREELDAAQ-EA 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1255 KAYIDtikdyelQLVAYKAQVEPLVSPLKKTKLDSasDNIIQEYVTLrtrySELMTLTSQYIKFIT------------DT 1322
Cdd:COG3096 909 QAFIQ-------QHGKALAQLEPLVAVLQSDPEQF--EQLQADYLQA----KEQQRRLKQQIFALSevvqrrphfsyeDA 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1323 QRRLDDEEKAAEKLKAeerkKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKlkmqeevskreiAAVDAEKQktniql 1402
Cdd:COG3096 976 VGLLGENSDLNEKLRA----RLEQAEEARREAREQLRQAQAQYSQYNQVLASLK------------SSRDAKQQ------ 1033
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1403 ELQELKN-LSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAE-- 1479
Cdd:COG3096 1034 TLQELEQeLEELGVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqa 1113
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774686 1480 KLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQK----------QKALEDLEKLR 1524
Cdd:COG3096 1114 KAGWCAVLRLARDNDVERRLHRRELAYLSADELRsmsdkalgalRLAVADNEHLR 1168
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2422-2554 |
4.26e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2422 RKAIADLENEKARLKKEAE-ELQNKSKEM-----ADAQQKKIEHEKTV---------LQQTFMTEKEMLLKKEKLIEDEK 2486
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKkEAEAIKKEAlleakEEIHKLRNEFEKELrerrnelqkLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774686 2487 KRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATmdAALSKQkEAEEEMLRKQKEMQELERQRL 2554
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI--SGLTAE-EAKEILLEKVEEEARHEAAVL 174
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1570-1703 |
4.28e-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: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1570 KTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKtlAQEEAEKQKE 1649
Cdd:pfam05262 204 KERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKE--DKQVAENQKR 281
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774686 1650 EAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK-LTAEQELIRLRAD 1703
Cdd:pfam05262 282 EIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKeLEAQKKREPVAED 336
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1669-1891 |
4.42e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1669 KEMAEEELERQRKIAESTAQQKLTAEQELIRLRADfdnAEQQRSLLEDELyRLKNEV-AAAQQQRKQLEDE-LAKVRSEM 1746
Cdd:pfam00038 49 YSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLA---AEDFRQKYEDEL-NLRTSAeNDLVGLRKDLDEAtLARVDLEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1747 DI------LIQLKTKAE---KETMSNTEKSKQLLEAEAAKMKDLAeeasrlRAISEeakhQRQIAEEEAARQRAEAERIL 1817
Cdd:pfam00038 125 KIeslkeeLAFLKKNHEeevRELQAQVSDTQVNVEMDAARKLDLT------SALAE----IRAQYEEIAAKNREEAEEWY 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1818 KEKLAAISEATRLKTEAEIALKEKEAENERL--RRQAEDEAY--QRKALEDQ--------ASQHKQ------EIEEKIVQ 1879
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTiqSLEIELQSLkkQKASLERQlaeteeryELQLADyqelisELEAELQE 274
|
250
....*....|..
gi 1988774686 1880 LKksseAEMERQ 1891
Cdd:pfam00038 275 TR----QEMARQ 282
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1653-1937 |
4.44e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1653 REAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQR 1732
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1733 KQLEDELAKVRSEMDIL------IQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQ--RQIAEE 1804
Cdd:COG4372 83 EELNEQLQAAQAELAQAqeelesLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEleEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1805 EAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSS 1884
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 1885 EAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIA 1937
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALEL 295
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1871-2358 |
4.72e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1871 QEIEEKIVQLKksseaEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAdETQQSKIRAEEE 1950
Cdd:COG4717 71 KELKELEEELK-----EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ-ELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1951 AEKLRKLaleeEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSA 2030
Cdd:COG4717 145 PERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2031 AEQQVQSVLAqQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAER 2110
Cdd:COG4717 221 ELEELEEELE-QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2111 LRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQeltkVKLKLDETDKQKSVLdeELQRLKDEVD 2190
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE----LQELLREAEELEEEL--QLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2191 DAVKQRGQVEEELFKVKV-QMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENmrkLAEDAARLSVEAQEAARLRqi 2269
Cdd:COG4717 374 ALLAEAGVEDEEELRAALeQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE---LEEELEELEEELEELEEEL-- 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2270 aeDDLNQQRALAEKMLKEkMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLledkQLMQQRLEEETEEYHksleveRKRQL 2349
Cdd:COG4717 449 --EELREELAELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWAAL----KLALELLEEAREEYR------EERLP 515
|
....*....
gi 1988774686 2350 EIMAEAERL 2358
Cdd:COG4717 516 PVLERASEY 524
|
|
| 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 ... |
1803-1902 |
5.38e-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: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1803 EEEAARQRAEAERILKEKLAAISEAtrlkteaEIALKEKEAENERLRRQAEDEAYQ-RKALEDQASQHkqeieekIVQLK 1881
Cdd:pfam00430 32 RELIADEIAEAEERRKDAAAALAEA-------EQQLKEARAEAQEIIENAKKRAEKlKEEIVAAAEAE-------AERII 97
|
90 100
....*....|....*....|.
gi 1988774686 1882 KSSEAEMERQKAIVDDTLKQR 1902
Cdd:pfam00430 98 EQAAAEIEQEKDRALAELRQQ 118
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2254-2588 |
5.61e-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: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2254 ARLSVEAQEAARLRQIAE--DDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQR-L 2330
Cdd:pfam07888 67 DREQWERQRRELESRVAElkEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRvL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2331 EEETEEYHKSLEVERKRQLEIMAEAERLRLQvSQLSEAQARAEEEAKKFKK------QADKVATRLHETEIATQEKMTVV 2404
Cdd:pfam07888 147 ERETELERMKERAKKAGAQRKEEEAERKQLQ-AKLQQTEEELRSLSKEFQElrnslaQRDTQVLQLQDTITTLTQKLTTA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2405 ERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEEL-QNKSKEMADAQQKKIEHEKTVLQqtfMTEKEMLLKKEKlie 2483
Cdd:pfam07888 226 HRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMaAQRDRTQAELHQARLQAAQLTLQ---LADASLALREGR--- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2484 dekkrleSQFEeevkkakalkdeQERQ--KQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILA 2561
Cdd:pfam07888 300 -------ARWA------------QEREtlQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLS 360
|
330 340
....*....|....*....|....*..
gi 1988774686 2562 EENQKLREKLQQLEDAQKDQHTRETDK 2588
Cdd:pfam07888 361 ESRRELQELKASLRVAQKEKEQLQAEK 387
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1468-1690 |
5.65e-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: 46.53 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1468 EKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQikv 1547
Cdd:TIGR00927 628 GDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEA--- 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1548 ahEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLR 1627
Cdd:TIGR00927 705 --DHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGE 782
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774686 1628 LQA-EDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK 1690
Cdd:TIGR00927 783 IQAgEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAK 846
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1324-1488 |
5.67e-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: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1324 RRLDDEEKAAEKLKAEERKKMAEMQAELDKQKqlaeahaKAIAKAEKEAQELKLKMQEevSKREIAAVDAEKQKTNIQLE 1403
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLE-------KEIKRLELEIEEVEARIKK--YEEQLGNVRNNKEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1404 LQELKnlseQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQkytAESELKQLRDRAAEAEKLRKLAQDEAEKLRK 1483
Cdd:COG1579 98 IESLK----RRISDLEDEILELMERIEELEEELAELEAELAELEAE---LEEKKAELDEELAELEAELEELEAEREELAA 170
|
....*
gi 1988774686 1484 QVSEE 1488
Cdd:COG1579 171 KIPPE 175
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1607-1959 |
5.75e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1607 EEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQkemAEEELERQRKIAEST 1686
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQ---ARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1687 AQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEM--------DILIQLKTKAEK 1758
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIaereeelkELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1759 ETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIAL 1838
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1839 KEKEAENER-LRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFE 1917
Cdd:COG4372 246 EDKEELLEEvILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1988774686 1918 KASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLAL 1959
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
1512-1912 |
5.75e-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: 45.82 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1512 QKQKALEDLEkLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGavlQLQQE 1591
Cdd:pfam04747 50 QRKEAFASLE-LTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEARRAEAEAKKRAAQEEEHK---QWKAE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1592 AERLKKQQEdaenSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEM 1671
Cdd:pfam04747 126 QERIQKEQE----KKEADLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTPTNTP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1672 AEEELERQRKIAESTAQQKLTAEQELIRLRADFDN-AEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILI 1750
Cdd:pfam04747 202 AEPAEQVQEITGKKNKKNKKKSESEATAAPASVEQvVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASETPVEP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1751 -----------QLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASR--LRAISEEAKHQRQIAEEEAARQRAEAERIL 1817
Cdd:pfam04747 282 vvettppasenQKKNKKDKKKSESEKVVEEPVQAEAPKSKKPTADDNMdfLDFVTAKEEPKDEPAETPAAPVEEVVENVV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1818 KEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALED--QASQHKQEIEEKIVQLKKSSEAEMERQKAIV 1895
Cdd:pfam04747 362 ENVVEKSTTPPATENKKKNKKDKKKSESEKVTEQPVESAPAPPQVEQvvETTPPASENKKKNKKDKKKSESEKAVEEPVQ 441
|
410
....*....|....*..
gi 1988774686 1896 DDTLKQRRVVEEEIRIL 1912
Cdd:pfam04747 442 AAPSSKKPTADDNMDFL 458
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1806-2051 |
6.05e-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: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1806 AARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSsE 1885
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL-R 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1886 AEMERQKAIVDDTLkqrRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQqskiraeEEAEKLRKLALEEEKRR 1965
Cdd:COG4942 97 AELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR-------EQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1966 REAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIED 2045
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
....*.
gi 1988774686 2046 SITQKK 2051
Cdd:COG4942 247 GFAALK 252
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1457-1595 |
6.09e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.86 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1457 LKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEET------------QKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLR 1524
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAkelllrernqqrQEARREREELQREEERLVQKEEQLDARAEKLDNLE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 1525 MQAEEAERQVKQAEIE-KEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQ-LQQEAERL 1595
Cdd:PRK12705 105 NQLEEREKALSARELElEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEeADLEAERK 177
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3329-3365 |
6.10e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 6.10e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1988774686 3329 KYLQGSSSIAGLYLEPTKEKLSIYQAMKKKLLRHNTG 3365
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2134-2266 |
6.15e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2134 QQADTEMAKHKKLAEQTLKQKF-----QVEQELTKVKLKLDETDKQ----KSVLDEELQRLKDEVDDAVKQRGQVEEELF 2204
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIhklrnEFEKELRERRNELQKLEKRllqkEENLDRKLELLEKREEELEKKEKELEQKQQ 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 2205 KVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENmrKLAEDAARLSVEAQEAARL 2266
Cdd:PRK12704 125 ELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVEE--EARHEAAVLIKEIEEEAKE 184
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1323-1525 |
6.44e-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: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1323 QRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREiaavdaekqktnIQL 1402
Cdd:COG2268 225 EAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAERE------------REI 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1403 ELQELKnlseqqikdksqqvdealhsrtKIEEEIRLIRIQLETTEKQKYTAESElkqlrdRAAEAEKLRKLAQDEAEKLR 1482
Cdd:COG2268 293 ELQEKE----------------------AEREEAELEADVRKPAEAEKQAAEAE------AEAEAEAIRAKGLAEAEGKR 344
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1988774686 1483 KQVseETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRM 1525
Cdd:COG2268 345 ALA--EAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITI 385
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1587-1741 |
6.80e-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: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1587 QLQQEAERLKKQQEDAENSREEAEKELEKWRQ--KANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEES 1664
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTelEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774686 1665 ALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQrslLEDELYRLKNEVAAAQQQRKQLEDELAK 1741
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAKIPP 174
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1210-1514 |
6.96e-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: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1210 QRQEKIQAVPITDSKTLKEQLAQ-EKKLLE-EIEQNKDKVDECQKYakayiDTIKDYELQLVAYKAQVeplvSPLKKTKL 1287
Cdd:NF033838 158 QKEEDRRNYPTNTYKTLELEIAEsDVEVKKaELELVKEEAKEPRDE-----EKIKQAKAKVESKKAEA----TRLEKIKT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1288 D--SASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAE------LDKQKQLAE 1359
Cdd:NF033838 229 DreKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSVGEEtlpspsLKPEKKVAE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1360 AHaKAIAKAEKeaqelKLKMQEEVSKR------------EIAAVDAEKQKTNIQLELQELKnlsEQQIKDKSQQVDEALH 1427
Cdd:NF033838 309 AE-KKVEEAKK-----KAKDQKEEDRRnyptntyktlelEIAESDVKVKEAELELVKEEAK---EPRNEEKIKQAKAKVE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1428 SRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEA-----EKLRKQVSEETQKKRQAEEELKRK 1502
Cdd:NF033838 380 SKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKpapkpEKPAEQPKAEKPADQQAEEDYARR 459
|
330
....*....|..
gi 1988774686 1503 SEAEKEAAKQKQ 1514
Cdd:NF033838 460 SEEEYNRLTQQQ 471
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
161-242 |
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 1988774686 161 RCDNFTTSWRDGKLFNAVIHKHYPRLIN---MGKVYQQTNLE-NLEQAFSVAEKdLGVTRLLDPEDVDVPHPDEksIITY 236
Cdd:cd21218 32 RVTNFSSDLKDGEVYALLLHSLAPELCDkelVLEVLSEEDLEkRAEKVLQAAEK-LGCKYFLTPEDIVSGNPRL--NLAF 108
|
....*.
gi 1988774686 237 VSSLYD 242
Cdd:cd21218 109 VATLFN 114
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
24-143 |
7.63e-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: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 24 KTFTKWVNKHLIKAQrhVTDLYEDLRDGHNLISLLEVLSGE---TLPREKGR-------MRFHKLQNVQIALDFLRHRQV 93
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGF 459
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774686 94 KLVNIRNDDIADGNpKLTLGLIW-------TIILHFQVSSS--ISDIQVNGQSEDMTAK 143
Cdd:COG5069 460 SLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKDGcgLSDSDLCAWLGSLGLK 517
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1694-1953 |
7.75e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1694 EQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQlktkaeketmsNTEKSKQLLEA 1773
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNE-----------KVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1774 EAAKMKDLAEEASRLRAISEE--------AKHQRQIAEEEAARQRA----EAERILKEKLAAIS---EATRLKTEAEIAL 1838
Cdd:COG1340 83 LNEKLNELREELDELRKELAElnkaggsiDKLRKEIERLEWRQQTEvlspEEEKELVEKIKELEkelEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1839 KEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDdtlKQRRVVEEEIRILKLNFEK 1918
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVE---AQEKADELHEEIIELQKEL 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1988774686 1919 AssgklDLELELNKLKNIADETQQSKIRAEEEAEK 1953
Cdd:COG1340 240 R-----ELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
791-835 |
7.99e-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: 7.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1988774686 791 IQAVCDFK---QQEITVHKGDECALLNNSQPFKWKVLNRSGHEAMVPS 835
Cdd:cd11768 2 VVALYDFQpiePGDLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPS 49
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1439-1538 |
8.66e-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: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1439 IRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLA-QDEAEKLRKqvsEETQKKRQAEEeLKRKSEAEKEAAKQKQKAL 1517
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAsFERLAELRD---ELAELEEELEA-LKARWEAEKELIEEIQELK 477
|
90 100
....*....|....*....|.
gi 1988774686 1518 EDLEKLRMQAEEAERQVKQAE 1538
Cdd:COG0542 478 EELEQRYGKIPELEKELAELE 498
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2306-2538 |
9.01e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2306 QKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLE--IMAEAERLRLQVSQLSeaqaraeeeakkfKKQA 2383
Cdd:PRK05035 441 IEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAKDKdaVAAALARVKAKKAAAT-------------QPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2384 DKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKE-------------MA 2450
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEeevdpkkaavaaaIA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2451 DAQQKKIEHEKTVLQQTFMTEKEMLLK--------KEKLIEDEKKRLESQFEEE----------VKKAKALKDEQERQKQ 2512
Cdd:PRK05035 588 RAKAKKAAQQAASAEPEEQVAEVDPKKaavaaaiaRAKAKKAEQQANAEPEEPVdprkaavaaaIARAKARKAAQQQANA 667
|
250 260
....*....|....*....|....*...
gi 1988774686 2513 QMEQEKKTLQATMDAALS--KQKEAEEE 2538
Cdd:PRK05035 668 EPEEAEDPKKAAVAAAIAraKAKKAAQQ 695
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2214-2353 |
9.04e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 9.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2214 LKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQ 2293
Cdd:PRK00409 497 LGLPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ 576
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 2294 EA-SRLKAEAEMLQKQKDLAQEQAQKLLEDKQL--MQQRLEEETEEYHKSLEVERKRQLEIMA 2353
Cdd:PRK00409 577 QAiKEAKKEADEIIKELRQLQKGGYASVKAHELieARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2749-2779 |
9.13e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 9.13e-04
10 20 30
....*....|....*....|....*....|.
gi 1988774686 2749 LLAERAVVGYKDPYTGGKISVFEAMKKGLIE 2779
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2384-2584 |
9.14e-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: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2384 DKVATRLHETEIATQEKMTVVERLEFERlNTSKEADDLRKAIADLE-NEKARLKKEAEelqnKSKEMADAQQKKIEHEKT 2462
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRRER-EKAERYQALLKEKREYEgYELLKEKEALE----RQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2463 vlqqtfmtekemllKKEKLIEDEKKRLESqfeeevkKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRK 2542
Cdd:TIGR02169 255 --------------KLTEEISELEKRLEE-------IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEK 313
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1988774686 2543 QKEMQELErqrlEQERILAEENQKLREKLQQLEDAQKDQHTR 2584
Cdd:TIGR02169 314 ERELEDAE----ERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2199-2548 |
9.22e-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: 45.33 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2199 VEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAE------- 2271
Cdd:COG5185 188 LLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEqntdlrl 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2272 DDLNQQRALAEKMLKEKMQAIQEASRLKAE-AEMLQKQKDLA-----QEQAQKLLEDKQLMQQRLEEETEEYHKSLEVEr 2345
Cdd:COG5185 268 EKLGENAESSKRLNENANNLIKQFENTKEKiAEYTKSIDIKKateslEEQLAAAEAEQELEESKRETETGIQNLTAEIE- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2346 KRQLEIMAEAERLRLQVSQLSEAQARAEEEAK--KFKKQADKVATRLHETEIATQEKMTVVER-LEFERLNTSKEADDLR 2422
Cdd:COG5185 347 QGQESLTENLEAIKEEIENIVGEVELSKSSEEldSFKDTIESTKESLDEIPQNQRGYAQEILAtLEDTLKAADRQIEELQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2423 KAIADLENEKARLKKEAEELQNkskEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKA 2502
Cdd:COG5185 427 RQIEQATSSNEEVSKLLNELIS---ELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEK 503
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1988774686 2503 LKDEQERQKQQMEQEKKTLQATMDAALSKQKEA---EEEMLRKQKEMQE 2548
Cdd:COG5185 504 LRAKLERQLEGVRSKLDQVAESLKDFMRARGYAhilALENLIPASELIQ 552
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1129-1476 |
9.67e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1129 DSLEEELKKASAVSDKMVRVHserdvelDHFRQQLSSLQDRWKAVFTQIDLR--QRELEQLGRQLGYYREsydwlirwia 1206
Cdd:PRK04863 796 EELAERYATLSFDVQKLQRLH-------QAFSRFIGSHLAVAFEADPEAELRqlNRRRVELERALADHES---------- 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1207 daKQRQEKIQAvpitdsKTLKEQLAQEKKLL------------EEIEQNKDKVDECQKyAKAYIDtikdyelQLVAYKAQ 1274
Cdd:PRK04863 859 --QEQQQRSQL------EQAKEGLSALNRLLprlnlladetlaDRVEEIREQLDEAEE-AKRFVQ-------QHGNALAQ 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1275 VEPLVSPLKktkldsaSDNiiQEYVTLRTRYSELMTLTSQYIKFI---------------TDTQRRLDDEEKAAEKLKAe 1339
Cdd:PRK04863 923 LEPIVSVLQ-------SDP--EQFEQLKQDYQQAQQTQRDAKQQAfaltevvqrrahfsyEDAAEMLAKNSDLNEKLRQ- 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1340 erkKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKlkmqeevskreiAAVDAEKQktNIQLELQELKNL-------SE 1412
Cdd:PRK04863 993 ---RLEQAEQERTRAREQLRQAQAQLAQYNQVLASLK------------SSYDAKRQ--MLQELKQELQDLgvpadsgAE 1055
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 1413 QQIKDKSQQVDEALHS----RTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEK----LRKLAQD 1476
Cdd:PRK04863 1056 ERARARRDELHARLSAnrsrRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAgwcaVLRLVKD 1127
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1291-1663 |
9.76e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1291 SDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEK 1370
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1371 EAQELKLKMQEEVSKREiaavDAEKQKTNIQLELQELknlsEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQK 1450
Cdd:COG4372 81 ELEELNEQLQAAQAELA----QAQEELESLQEEAEEL----QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1451 YTAESELKQLRDRAAEAEK-----LRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRM 1525
Cdd:COG4372 153 KELEEQLESLQEELAALEQelqalSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1526 QAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENS 1605
Cdd:COG4372 233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774686 1606 REEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEE 1663
Cdd:COG4372 313 LEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2430-2581 |
9.91e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2430 NEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKL--IEDEKKRLESQFEEEVKKAKALKDEQ 2507
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIraLEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2508 ERQKQQMEQEKKTLQ-----------------------ATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQER-ILAEE 2563
Cdd:COG4942 100 EAQKEELAELLRALYrlgrqpplalllspedfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERaELEAL 179
|
170
....*....|....*...
gi 1988774686 2564 NQKLREKLQQLEDAQKDQ 2581
Cdd:COG4942 180 LAELEEERAALEALKAER 197
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1501-1695 |
1.02e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1501 RKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKtsklEESLKQ 1580
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK----EENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1581 EHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAL-RL-RLQAEdEAHKKTLaqeeaekqkeeaeREAKKR 1658
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELeRIsGLTAE-EAKEILL-------------EKVEEE 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 1988774686 1659 AKAEESAL-KQKEM-AEEELERQRKIAESTAQQKLTAEQ 1695
Cdd:PRK12704 167 ARHEAAVLiKEIEEeAKEEADKKAKEILAQAIQRCAADH 205
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1653-2051 |
1.10e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1653 REAKKRAKAEESALKqkemAEEELERQRKiaestaqqKLTAEQE-LIRLRADFDNAEQQRSLLEDELYRLK---NEVAAA 1728
Cdd:PRK04863 276 RHANERRVHLEEALE----LRRELYTSRR--------QLAAEQYrLVEMARELAELNEAESDLEQDYQAASdhlNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1729 QQQRKQLEdelakvRSEMDILiQLKTKAEKETMSNTEKSKQLLEAEAAKmkDLAEEaSRLRAISEEAKHQRQIaeeEAAR 1808
Cdd:PRK04863 344 LRQQEKIE------RYQADLE-ELEERLEEQNEVVEEADEQQEENEARA--EAAEE-EVDELKSQLADYQQAL---DVQQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1809 QRAEAERilkEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHK--QEIEEKIVQLKKSSEA 1886
Cdd:PRK04863 411 TRAIQYQ---QAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQaaHSQFEQAYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1887 EMERQKAivDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNK---LKNIADETQQSKIRAEEEAEKLRKLALEEEK 1963
Cdd:PRK04863 488 EVSRSEA--WDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEA 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1964 RRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEkQIVVAQQAAQKCSAAEQQVQSVL--AQ 2041
Cdd:PRK04863 566 RLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLRE-QSGEEFEDSQDVTEYMQQLLEREreLT 644
|
410
....*....|
gi 1988774686 2042 QIEDSITQKK 2051
Cdd:PRK04863 645 VERDELAARK 654
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1475-1554 |
1.11e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.33 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1475 QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAK------QKQKALE-DLEKLRMQAEEAERQvkqaeiEKEKQIKV 1547
Cdd:PRK11448 148 QQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGlaaeleEKQQELEaQLEQLQEKAAETSQE------RKQKRKEI 221
|
....*..
gi 1988774686 1548 AHEAAQK 1554
Cdd:PRK11448 222 TDQAAKR 228
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2266-2457 |
1.13e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2266 LRQIAEDDLNQQRALAEKMLKEKmqaiqeasrlKAEAEMLQKQKDL-AQEQAQKLledkqlmQQRLEEETEEYHKSLEve 2344
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEA----------KKEAEAIKKEALLeAKEEIHKL-------RNEFEKELRERRNELQ-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2345 rkrQLEimaeaERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETE--IATQEKMTVVERLEFERLN--TSKEADD 2420
Cdd:PRK12704 86 ---KLE-----KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEkkEEELEELIEEQLQELERISglTAEEAKE 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1988774686 2421 --LRKAIADLENEKARLKKEAEElqnKSKEMADAQQKKI 2457
Cdd:PRK12704 158 ilLEKVEEEARHEAAVLIKEIEE---EAKEEADKKAKEI 193
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2417-2518 |
1.16e-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: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2417 EADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKkeklIEDEKKRLESQFEEE 2496
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEE----IQELKEELEQRYGKI 487
|
90 100
....*....|....*....|..
gi 1988774686 2497 VKKAKALKDEQERQKQQMEQEK 2518
Cdd:COG0542 488 PELEKELAELEEELAELAPLLR 509
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2134-2287 |
1.24e-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: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2134 QQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVK------ 2207
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2208 -VQME-ELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKML 2285
Cdd:COG1579 93 aLQKEiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
..
gi 1988774686 2286 KE 2287
Cdd:COG1579 173 PP 174
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1590-1813 |
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 1988774686 1590 QEAERLKKQQEDAENSREEAEKELEkwrQKANEalrlrLQAEDEAHkktlaqeeaekqkeeaeRE-----AKKRAKAEES 1664
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRKKKEQ---QQAEE-----LQQKQAAE-----------------QErlkqlEKERLAAQEQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1665 ALKQKEMAEEELERQRKIAESTAQQ----KLTAEQELIRLRADFDNAEQQrslledelyrlKNEVAAAQQQRKQLEDELA 1740
Cdd:PRK09510 117 KKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAAKKAAAE-----------AKKKAEAEAAKKAAAEAKK 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 1741 KVRSEMdiliqlKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEA 1813
Cdd:PRK09510 186 KAEAEA------AAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1910-2336 |
1.28e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1910 RILKLNFEKASSGKLDLELELNKLKNIADETQQ-SKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKA 1988
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1989 ALEELERLRKKAEEaRKQKDEADKEAEKQIvvaQQAAQKCSAAEQQVQSVLAQQIEDsitqkkLKEEYEKAKKLAKEAEA 2068
Cdd:COG4717 144 LPERLEELEERLEE-LRELEEELEELEAEL---AELQEELEELLEQLSLATEEELQD------LAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2069 AKEKAEREAALLRQQAEEAERQKTaaeeeaanqakAQEDAERLrKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLA- 2147
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELE-----------AAALEERL-KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2148 ---------EQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKN 2218
Cdd:COG4717 282 vlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2219 KI-----EEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLsveAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQ 2293
Cdd:COG4717 362 ELqleelEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELE 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1988774686 2294 EA-SRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEE 2336
Cdd:COG4717 439 EElEELEEELEELREELAELEAELEQLEEDGELAELLQELEELK 482
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1607-1852 |
1.30e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1607 EEAE-KELEKWRQKANEAlRLRLQA-----EDEAhkktlaqeeaekqkeeAEREAKKRAKAEESALKQKEMAEEELER-Q 1679
Cdd:PRK05035 434 AKAEiRAIEQEKKKAEEA-KARFEArqarlEREK----------------AAREARHKKAAEARAAKDKDAVAAALARvK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1680 RKIAESTAQQKLTAEQE--------LIRLRADFDNAEQQRSLLEDELYRLKNEVAAA----QQQRKQLEDELAKVRSEMD 1747
Cdd:PRK05035 497 AKKAAATQPIVIKAGARpdnsaviaAREARKAQARARQAEKQAAAAADPKKAAVAAAiaraKAKKAAQQAANAEAEEEVD 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1748 iliQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEE-AKHQRQIAEEEAARQRAEAERILKEKLAAISE 1826
Cdd:PRK05035 577 ---PKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKAAVAAAIA 653
|
250 260
....*....|....*....|....*.
gi 1988774686 1827 ATRLKTEAEIALKEKEAENERLRRQA 1852
Cdd:PRK05035 654 RAKARKAAQQQANAEPEEAEDPKKAA 679
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2377-2557 |
1.31e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2377 KKFKKQADKVATRLHETEIATQEKmtvVERLEFERLntskEADDLRKAIADLENEKARLKKEAEELQNKSKEM----ADA 2452
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQER---LKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAakakAEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2453 QQK-------KIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQfeeevKKAKALKDEQERQKQQMEQEKKTLQATM 2525
Cdd:PRK09510 152 EAKraaaaakKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAE-----AKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
170 180 190
....*....|....*....|....*....|..
gi 1988774686 2526 DAALSKQKEAEEEMLRKQKEMQELERQRLEQE 2557
Cdd:PRK09510 227 AAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2394-2515 |
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 1988774686 2394 EIATQ----EKMTVVERLEFErlntSKEADDLRKAIADLENEKAR---LKKEAE----ELQNKSKEMADAQQK--KIEHE 2460
Cdd:PTZ00491 658 EITTKsqeaAARHQAELLEQE----ARGRLERQKMHDKAKAEEQRtklLELQAEsaavESSGQSRAEALAEAEarLIEAE 733
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 2461 KTVlQQTFMTEKEMLLKKEKLIEDEKKRLE-------SQFEEEVKKAKALKD-EQERQKQQME 2515
Cdd:PTZ00491 734 AEV-EQAELRAKALRIEAEAELEKLRKRQEleleyeqAQNELEIAKAKELADiEATKFERIVE 795
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1799-1975 |
1.36e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1799 RQIAEEEAARQRAEAERILKEklaAISEATRLKTEAEIALKEkeaENERLRRQAEDEAYQRKA----LEDQASQHKQEIE 1874
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEE---AKKEAEAIKKEALLEAKE---EIHKLRNEFEKELRERRNelqkLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1875 EKIVQLKKSsEAEMERQKAIVDDTLKQRRVVEEEIRILKLnfekassgKLDLELE--------------LNKLKNIADET 1940
Cdd:PRK12704 100 RKLELLEKR-EEELEKKEKELEQKQQELEKKEEELEELIE--------EQLQELErisgltaeeakeilLEKVEEEARHE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1988774686 1941 QQSKIR-----AEEEAEKlrklaleeekrrreaeeKVKKI 1975
Cdd:PRK12704 171 AAVLIKeieeeAKEEADK-----------------KAKEI 193
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1458-1558 |
1.39e-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: 42.08 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1458 KQLRDRAAEAEKLRKlaqdEAEKLRKQVSEETQK-KRQAEEELKrksEAEKEAAKQKQKALEDLEklrmqaEEAERQVKQ 1536
Cdd:COG0711 34 EKIADGLAEAERAKE----EAEAALAEYEEKLAEaRAEAAEIIA---EARKEAEAIAEEAKAEAE------AEAERIIAQ 100
|
90 100
....*....|....*....|..
gi 1988774686 1537 AEIEKEKQIKVAHEAAQKSAAA 1558
Cdd:COG0711 101 AEAEIEQERAKALAELRAEVAD 122
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1684-1787 |
1.47e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.94 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1684 ESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEmdiLIQLKTKAEKETMSN 1763
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQ---LEQLQEKAAETSQER 214
|
90 100
....*....|....*....|....
gi 1988774686 1764 TEKSKQLLEaEAAKMKDLAEEASR 1787
Cdd:PRK11448 215 KQKRKEITD-QAAKRLELSEEETR 237
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1708-1844 |
1.49e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1708 EQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSemdiliqLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASR 1787
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEA-------LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ 577
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774686 1788 LR--AISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAE 1844
Cdd:PRK00409 578 AIkeAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2185-2584 |
1.51e-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: 44.83 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2185 LKDEVDDAVKQRGQVEEELFKVKVQMEELLK---LKNKIEEENQRLIKKDKDSTQKLLAE-EAENMRKLAEDAARLSVEA 2260
Cdd:pfam12128 198 VKSMIVAILEDDGVVPPKSRLNRQQVEHWIRdiqAIAGIMKIRPEFTKLQQEFNTLESAElRLSHLHFGYKSDETLIASR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2261 QEAarlRQIAEDDLNQQRALAEKMLKEKMQAI-QEASRLKAEAEMLQKQKDLAQEQAQklledkqlmqQRLEEETEEYHk 2339
Cdd:pfam12128 278 QEE---RQETSAELNQLLRTLDDQWKEKRDELnGELSAADAAVAKDRSELEALEDQHG----------AFLDADIETAA- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2340 sleverkrqleimAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRlheTEIATQEKMTVVERLEfERLNTSKEAD 2419
Cdd:pfam12128 344 -------------ADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRR---RSKIKEQNNRDIAGIK-DKLAKIREAR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2420 DLRKAIA--DLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLK--KEKLIEDEKKRLESQFEE 2495
Cdd:pfam12128 407 DRQLAVAedDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLenFDERIERAREEQEAANAE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2496 ------EVKKAKALKDEQERQKQQMEQEKKTLQATMDAA--------------LSKQKEAEEEMLRKQKEMQELERQ--- 2552
Cdd:pfam12128 487 verlqsELRQARKRRDQASEALRQASRRLEERQSALDELelqlfpqagtllhfLRKEAPDWEQSIGKVISPELLHRTdld 566
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 2553 -----------------RLEQERILAEE----NQKLREKLQQLEDAQKDQHTR 2584
Cdd:pfam12128 567 pevwdgsvggelnlygvKLDLKRIDVPEwaasEEELRERLDKAEEALQSAREK 619
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3778-3811 |
1.52e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.52e-03
10 20 30
....*....|....*....|....*....|....
gi 1988774686 3778 LEAQTATGGIIDPEFQFHLPTDVAMQRGYINKET 3811
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1351-1507 |
1.54e-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: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1351 LDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQEL---KNLSEQQIKDKSQQVDEAlh 1427
Cdd:pfam08614 13 LDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELyrsRGELAQRLVDLNEELQEL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1428 srtkiEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEE--------L 1499
Cdd:pfam08614 91 -----EKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKEnrelverwM 165
|
....*....
gi 1988774686 1500 KRKS-EAEK 1507
Cdd:pfam08614 166 KRKGqEAEA 174
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2402-2581 |
1.54e-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: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2402 TVVERLEFERLNTSKE----------ADDLRK--------AIADLENEK-----------ARLKKEAEELQN---KSKEM 2449
Cdd:COG2268 135 AVAAQMTVEELNEDREkfaekvqevaGTDLAKnglelesvAITDLEDENnyldalgrrkiAEIIRDARIAEAeaeRETEI 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2450 ADAQQKKIEHEKTVLQQTfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAK---ALKDEQERQKQQMEQEKKTLQATMD 2526
Cdd:COG2268 215 AIAQANREAEEAELEQER---EIETARIAEAEAELAKKKAEERREAETARAEaeaAYEIAEANAEREVQRQLEIAERERE 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2527 AALsKQKEAEEEMLRKQKEMQ---ELERQRLEQE------------RILAEENQKLREKLQQLEDAQKDQ 2581
Cdd:COG2268 292 IEL-QEKEAEREEAELEADVRkpaEAEKQAAEAEaeaeaeairakgLAEAEGKRALAEAWNKLGDAAILL 360
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1477-1606 |
1.55e-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: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1477 EAEKLRKQVSEETQK--KRQAEEELKR-KSEAEKEAakqkqkaleDLEKLRMQA--EEAERQVKQAEIEKEkqikvAHEA 1551
Cdd:cd03406 172 EAEKTKLLIAEQHQKvvEKEAETERKRaVIEAEKDA---------EVAKIQMQQkiMEKEAEKKISEIEDE-----MHLA 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774686 1552 AQKSAAAelqskhmsfAEKTSKleesLKQEHGAVLQLQQEAERLKKQQEDAENSR 1606
Cdd:cd03406 238 REKARAD---------AEYYRA----LREAEANKLKLTPEYLELKKYQAIANNTK 279
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2212-2365 |
1.58e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.62 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2212 ELLKLKNKIEEENQRlikkdkdstQKLLAEEAENmrklaedaarLSVEAQEAARlrqiaeddlnqqrALAEkmlkekmqA 2291
Cdd:PTZ00491 684 ERQKMHDKAKAEEQR---------TKLLELQAES----------AAVESSGQSR-------------AEAL--------A 723
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774686 2292 IQEASRLKAEAEMLQKQkdlAQEQAQKLLEDKQLMQQRLEEETE-EYHKS---LEVERKRQLEiMAEAERLRLQVSQL 2365
Cdd:PTZ00491 724 EAEARLIEAEAEVEQAE---LRAKALRIEAEAELEKLRKRQELElEYEQAqneLEIAKAKELA-DIEATKFERIVEAL 797
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1834-2575 |
1.59e-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: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1834 AEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILK 1913
Cdd:pfam07111 7 SDIPLVQSPGHQDVLERRLDTQRPTVTMWEQDVSGDGQGPGRRGRSLELEGSQALSQQAELISRQLQELRRLEEEVRLLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1914 lnfekassgkldlelelnklkniaDETQQSKIRAEEEAEKLRKLAleeekrrreaeekvkkiaaaeeeaaRQRKAALEEL 1993
Cdd:pfam07111 87 ------------------------ETSLQQKMRLEAQAMELDALA-------------------------VAEKAGQAEA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1994 ERLRKK---AEEARKQKDEAD-KEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDsiTQKKLKEeyekakklakeaeaa 2069
Cdd:pfam07111 118 EGLRAAlagAEMVRKNLEEGSqRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEG--LEKSLNS--------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2070 kekaereaaLLRQQAEEAERqktaaeeeaanQAKAQEDAERLRKEaefeaakraqaeaaalMQKQQADTEmakhkklAEQ 2149
Cdd:pfam07111 181 ---------LETKRAGEAKQ-----------LAEAQKEAELLRKQ----------------LSKTQEELE-------AQV 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2150 TLKQ---KFQVEQELTKVKLKLDETDKQKsvLDEELQRLKDEVDDAvkqrgQVEEELFKVKVQmeellklknkieeenqr 2226
Cdd:pfam07111 218 TLVEslrKYVGEQVPPEVHSQTWELERQE--LLDTMQHLQEDRADL-----QATVELLQVRVQ----------------- 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2227 likkdkDSTQKLLAEEAENMRKLAEDAarlSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQ 2306
Cdd:pfam07111 274 ------SLTHMLALQEEELTRKIQPSD---SLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQ 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2307 KQ-KDLAQEQA--QKLLEDK--QLMQQRLEEET--EEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKF 2379
Cdd:pfam07111 345 EQvTSQSQEQAilQRALQDKaaEVEVERMSAKGlqMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRV 424
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2380 KKQADKVATRLHETEIATQEKMTV---------VERLEFERLNTSKEA----DDLRKAIADLENEKARLKKE----AEEL 2442
Cdd:pfam07111 425 EQAVARIPSLSNRLSYAVRKVHTIkglmarkvaLAQLRQESCPPPPPAppvdADLSLELEQLREERNRLDAElqlsAHLI 504
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2443 QN---KSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKK 2519
Cdd:pfam07111 505 QQevgRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVA 584
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 2520 TLQATMDAALSKQKEAEEEMLRKQ------------KEMQELERQ---RLEQERILAEENQKLREKLQQLE 2575
Cdd:pfam07111 585 EVETRLREQLSDTKRRLNEARREQakavvslrqiqhRATQEKERNqelRRLQDEARKEEGQRLARRVQELE 655
|
|
| Mcm10 |
pfam09332 |
Mcm10 replication factor; Mcm10 is a eukaryotic DNA replication factor that regulates the ... |
1465-1579 |
1.62e-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: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1465 AEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQ 1544
Cdd:pfam09332 133 AEAAKLAAIAKLKAKGGVLEKEDPNAVKRKRSDSGEIKERVEKNLESSSSSSPDEEEPALKKRREQLAYLKSEEFQKILN 212
|
90 100 110
....*....|....*....|....*....|....*
gi 1988774686 1545 IKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLK 1579
Cdd:pfam09332 213 AKSKHTGELKEAEAEMQERYFEPLVKKEQMEEKMR 247
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2130-2294 |
1.71e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2130 LMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQ 2209
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2210 MEELLKLKNKIEEENQRLIKKDKDSTQKLlaEEAENMRK---LAEDAARLSVEAQE--AARLRQIAEDDLNQQRALAEKM 2284
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDNEL--YRVAGLTPeqaRKLLLKLLDAELEEekAQRVKKIEEEADLEAERKAQNI 181
|
170
....*....|
gi 1988774686 2285 LKEKMQAIQE 2294
Cdd:PRK12705 182 LAQAMQRIAS 191
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1661-2005 |
1.73e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.47 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1661 AEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQ---QQRKQLED 1737
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREerrQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1738 ELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEAS---RLRAISEEAKHQ--RQIAE--EEAARQR 1810
Cdd:pfam02029 84 ERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEEteiREKEYQENKWSTevRQAEEegEEEEDKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1811 AEAERILKE-------KLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKS 1883
Cdd:pfam02029 164 EEAEEVPTEnfakeevKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1884 SEAEMERQKaivddtLKQRRVVEEEirilkLNFEKASSGKLDLELELNKLKNIADEtqQSKIRAEEEaeklrklaleeek 1963
Cdd:pfam02029 244 LEAEQKLEE------LRRRRQEKES-----EEFEKLRQKQQEAELELEELKKKREE--RRKLLEEEE------------- 297
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1988774686 1964 RRREAEEKVKKIaaAEEEAARQRKaalEELERLRKKAEEARK 2005
Cdd:pfam02029 298 QRRKQEEAERKL--REEEEKRRMK---EEIERRRAEAAEKRQ 334
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1381-1538 |
1.75e-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: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1381 EEVSKREIAAVDAEKQKTNIQLELQELKNLS--EQQIKDKSQQVDEalhsrtkIEEEIRLIRIQLETTEKQKYTAESELK 1458
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHEERELTeeEEEIRRLEEQVER-------LEAEVEELEAELEEKDERIERLERELS 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1459 QLRDRA-AEAEKLRKLA--QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQA-EEAERQV 1534
Cdd:COG2433 452 EARSEErREIRKDREISrlDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEAiRRLEEEY 531
|
....
gi 1988774686 1535 KQAE 1538
Cdd:COG2433 532 GLKE 535
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3330-3368 |
1.75e-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: 1.75e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1988774686 3330 YLQGSSSIAGLYLEPTKEKLSIYQAMKKKLLRHNTGLSL 3368
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1326-1624 |
1.78e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.46 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1326 LDDEEKAAEKLKAEERKKMAEMQAELDK-QKQLAEAHAKAIAKAEKEAQELKLKMQEEvskreiaaVDAEKQKTNIQLEL 1404
Cdd:PLN03229 413 VDPERKVNMKKREAVKTPVRELEGEVEKlKEQILKAKESSSKPSELALNEMIEKLKKE--------IDLEYTEAVIAMGL 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1405 QE-LKNLSEQQIKDKSQqvDEALHSRTKIEEEIRLIRIQLETTEKQKYTAeseLKQLRDRAAEAEKLRKLAQ--DEAEKL 1481
Cdd:PLN03229 485 QErLENLREEFSKANSQ--DQLMHPVLMEKIEKLKDEFNKRLSRAPNYLS---LKYKLDMLNEFSRAKALSEkkSKAEKL 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1482 RKQVSEETqKKRQAEEELKRKSEAEK-EAAKQKQKALEDLEK-LRMQAEEA--ERQVKQAEIEKEKQIKVAHEAAQKSAA 1557
Cdd:PLN03229 560 KAEINKKF-KEVMDRPEIKEKMEALKaEVASSGASSGDELDDdLKEKVEKMkkEIELELAGVLKSMGLEVIGVTKKNKDT 638
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774686 1558 AElQSKHMSFAEKTSKLEESLKQEHGAVLQ---LQQEAERLKKQQEDAENSREEAEKE-LEKWRQKANEAL 1624
Cdd:PLN03229 639 AE-QTPPPNLQEKIESLNEEINKKIERVIRssdLKSKIELLKLEVAKASKTPDVTEKEkIEALEQQIKQKI 708
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
2085-2253 |
1.82e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 44.75 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2085 EEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQ-KQQADTEMAKHKKLAEQT---LKQKFQVEQE 2160
Cdd:COG1193 521 EELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKaREEAEEILREARKEAEELireLREAQAEEEE 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2161 LTKVKLKLDETDKQksvLDEELQRLKD-----------EVDDAVK-----QRGQVEEE-----------LFKVKVQMEEL 2213
Cdd:COG1193 601 LKEARKKLEELKQE---LEEKLEKPKKkakpakppeelKVGDRVRvlslgQKGEVLEIpkggeaevqvgILKMTVKLSDL 677
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1988774686 2214 LKLKNKIEEENQRLIKKDKDSTQKLLAEEAE-NMR-KLAEDA 2253
Cdd:COG1193 678 EKVEKKKPKKPKKRPAGVSVSVSKASTVSPElDLRgMRVEEA 719
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1379-1632 |
1.89e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1379 MQEEVSKREIAAVDAEKQKTniqleLQELKNLSEQQIKDKSQQVD-----EALHSRTKIEEEIRLIRiQLETTEKqkyTA 1453
Cdd:PRK05771 2 APVRMKKVLIVTLKSYKDEV-----LEALHELGVVHIEDLKEELSnerlrKLRSLLTKLSEALDKLR-SYLPKLN---PL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1454 ESELKQLRDRaaEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKsEAEKEAAKqKQKALE-DLEKLRM------- 1525
Cdd:PRK05771 73 REEKKKVSVK--SLEELIKDVEEELEKIEKEIKELEEEISELENEIKEL-EQEIERLE-PWGNFDlDLSLLLGfkyvsvf 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1526 -------QAEEAERQVKQAEIEKEKQIK-------VAHEAAQKSAAAELQSkhMSFAEKTSKLEESLKQehgAVLQLQQE 1591
Cdd:PRK05771 149 vgtvpedKLEELKLESDVENVEYISTDKgyvyvvvVVLKELSDEVEEELKK--LGFERLELEEEGTPSE---LIREIKEE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1988774686 1592 AERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAED 1632
Cdd:PRK05771 224 LEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAE 264
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
1462-1546 |
1.94e-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: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1462 DRAAEAEKLRKLAQDEAEKLRKQVSEETQKkrQAEEElkrKSEAEKEAAKQKQKALEDLEKLRMQAEEaerQVKQAEIEK 1541
Cdd:pfam07946 246 DKLAKRAKLRPEALKKAKKTREEEIEKIKK--AAEEE---RAEEAQEKKEEAKKKEREEKLAKLSPEE---QRKYEEKER 317
|
....*
gi 1988774686 1542 EKQIK 1546
Cdd:pfam07946 318 KKEQR 322
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1673-1893 |
2.03e-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: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1673 EEELERQRKIAESTAQQKLTAEQELI-RLRADfdNAEQQRslLEDELYRLKNEVAAAQQQRKQLEDElaKVRSEMDILIQ 1751
Cdd:pfam15709 310 ESEEERSEEDPSKALLEKREQEKASRdRLRAE--RAEMRR--LEVERKRREQEEQRRLQQEQLERAE--KMREELELEQQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1752 LKTKAEKETMSNTEKSKQLLEAEAAKmKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKlaaiseatRLK 1831
Cdd:pfam15709 384 RRFEEIRLRKQRLEEERQRQEEEERK-QRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEK--------QRQ 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774686 1832 TEAEIALKEkeaENERLRRQAEDE--AYQRKaledqasqhKQEIEEKIVQlkkssEAEMERQKA 1893
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 ... |
2482-2563 |
2.07e-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: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2482 IEDEKKRLES---QFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEM--LRKQKEMQELERQRLEQ 2556
Cdd:pfam20492 4 AEREKQELEErlkQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKerLEESAEMEAEEKEQLEA 83
|
....*..
gi 1988774686 2557 ERILAEE 2563
Cdd:pfam20492 84 ELAEAQE 90
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1575-1809 |
2.10e-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: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1575 EESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQaedeahkktlaqeeaekqkeeaere 1654
Cdd:pfam15709 340 AERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQ------------------------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1655 akkraKAEESALKQkemaeEELERQRKIAESTAQQKLTAEQELIRLRAdfdnAEQQRSLLEDELYRlkneVAAAQQQRKQ 1734
Cdd:pfam15709 395 -----RLEEERQRQ-----EEEERKQRLQLQAAQERARQQQEEFRRKL----QELQRKKQQEEAER----AEAEKQRQKE 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774686 1735 LEDELA---KVRSEMDILIQLKTKAEKEtmsnTEKSKQLLEAEAAKMKdlAEEASRLraISEEAKHQRQiaeeEAARQ 1809
Cdd:pfam15709 457 LEMQLAeeqKRLMEMAEEERLEYQRQKQ----EAEEKARLEAEERRQK--EEEAARL--ALEEAMKQAQ----EQARQ 522
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
504-598 |
2.12e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.39 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 504 LRYVQDLLAWVEENQRRIDNAEWGSDLPSMESQLGSHRGLHQTVEDFKSKIERAKADETQL---SPVSKGTYREYLGKLD 580
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1988774686 581 LQYGKLLNSSKSRLRNLE 598
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1580-1843 |
2.14e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1580 QEHGAVLQLQQEAER--LKKQQEDAENSREEAEKELEKWRQKANEAlrlRLQAEDEAHKKtlaqeeaekqkeeaerEAKK 1657
Cdd:PRK05035 433 QAKAEIRAIEQEKKKaeEAKARFEARQARLEREKAAREARHKKAAE---ARAAKDKDAVA----------------AALA 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1658 RAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQ----RK 1733
Cdd:PRK05035 494 RVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAAnaeaEE 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1734 QLEDELAKVRSEMdiliqLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEA-SRLRAISEEAKHQRQIAEEEAARQRAE 1812
Cdd:PRK05035 574 EVDPKKAAVAAAI-----ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKAAV 648
|
250 260 270
....*....|....*....|....*....|.
gi 1988774686 1813 AERILKEKlAAISEATRLKTEAEIALKEKEA 1843
Cdd:PRK05035 649 AAAIARAK-ARKAAQQQANAEPEEAEDPKKA 678
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2410-2587 |
2.14e-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: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2410 ERLNTSKEADDLRKAIADLEN-----EKARLKKEA-EELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIE 2483
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERahealEDAREQIELlEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2484 DEkkrlesqfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEA-EEEMLRKQKEMQELERQRLEQER---- 2558
Cdd:COG4913 299 EL--------RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEAllaa 370
|
170 180 190
....*....|....*....|....*....|....*....
gi 1988774686 2559 ----------ILAEENQKLREKLQQLEDAQKDQHTRETD 2587
Cdd:COG4913 371 lglplpasaeEFAALRAEAAALLEALEEELEALEEALAE 409
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
21-123 |
2.14e-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: 41.13 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 21 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLRHRQVKLV 96
Cdd:cd21337 20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 99
|
90 100
....*....|....*....|....*..
gi 1988774686 97 NIRNDDIADGNPKLTLGLIWTIILHFQ 123
Cdd:cd21337 100 KPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
1461-1538 |
2.24e-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: 41.18 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1461 RDRAAEAEKLRKLA---QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALedLEKLRMQAEEAERQVKQA 1537
Cdd:pfam00836 57 RRKSLEAQKLKQLAekrEKEEEALQKADEENNNFSKMAEEKLKQKMEAYKENREAQIAAL--KEKLKEKEKHVEEVRKNK 134
|
.
gi 1988774686 1538 E 1538
Cdd:pfam00836 135 E 135
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2114-2433 |
2.27e-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: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2114 EAEFEAAKRAQAEAAALMQKQQADTE-----MAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDE 2188
Cdd:pfam19220 82 EGELEELVARLAKLEAALREAEAAKEelrieLRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2189 VDDAVKQRGQVEEELFKVKVQMEE----LLKLKNKIEEENQRLikkdkdstqkllaeeAENMRKLAEDAARLSVEAQEAA 2264
Cdd:pfam19220 162 LATARERLALLEQENRRLQALSEEqaaeLAELTRRLAELETQL---------------DATRARLRALEGQLAAEQAERE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2265 RLRQIAEDDLNQQRAlAEKMLKEKMQAIQE----ASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEyhks 2340
Cdd:pfam19220 227 RAEAQLEEAVEAHRA-ERASLRMKLEALTAraaaTEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAG---- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2341 LEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLhETEIATQEKMTVVERLEFERLNtskeadd 2420
Cdd:pfam19220 302 LEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASL-SDRIAELTKRFEVERAALEQAN------- 373
|
330
....*....|...
gi 1988774686 2421 lRKAIADLENEKA 2433
Cdd:pfam19220 374 -RRLKEELQRERA 385
|
|
| V-ATPase_G_2 |
pfam16999 |
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ... |
1781-1879 |
2.30e-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: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1781 LAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKE---KLAAISEATRLKTEAEIALKEKEAenerlRRQAEDEAy 1857
Cdd:pfam16999 7 LSELAEREAALDQQIEAARKEAEREVEAAEAEAARILREaeaKAKALQAEYRQELAAETARIREEA-----RARAEAEA- 80
|
90 100
....*....|....*....|..
gi 1988774686 1858 qrKALEDQASQHKQEIEEKIVQ 1879
Cdd:pfam16999 81 --QAVRTRAEGRLQQAVELILR 100
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2300-2538 |
2.34e-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: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2300 AEAEMLQKQKDL--AQEQAQKLLEDKQLMQQRLEEETEEYhKSLEVERKrqlEIMAEAERLRLQVSQLSeaqaraeeeaK 2377
Cdd:COG3883 14 ADPQIQAKQKELseLQAELEAAQAELDALQAELEELNEEY-NELQAELE---ALQAEIDKLQAEIAEAE----------A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2378 KFKKQADKVATRLHeteiATQEKMTVVERLEFerLNTSKEADDLRKAIADLENEKARLKKEAEELQnkskemadAQQKKI 2457
Cdd:COG3883 80 EIEERREELGERAR----ALYRSGGSVSYLDV--LLGSESFSDFLDRLSALSKIADADADLLEELK--------ADKAEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2458 EHEKTVLQQtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEE 2537
Cdd:COG3883 146 EAKKAELEA----KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
.
gi 1988774686 2538 E 2538
Cdd:COG3883 222 A 222
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
2179-2334 |
2.39e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 44.21 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2179 DEELQRLKDEVDDAVkQRGQVEEELFKvkvQMEELlklknkieeenqrlikkdKDSTQKLLAEEAENMRKLAEDAARLSV 2258
Cdd:pfam13779 488 ERRLRAAQERLSEAL-ERGASDEEIAK---LMQEL------------------REALDDYMQALAEQAQQNPQDLQQPDD 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2259 EAQEAAR-------LRQIAEDDLNQQRALAEKMLKEkMQAIQEasRLKAeAEMlQKQKDLAQEQAQKLLEDKQLM---QQ 2328
Cdd:pfam13779 546 PNAQEMTqqdlqrmLDRIEELARSGRRAEAQQMLSQ-LQQMLE--NLQA-GQP-QQQQQQGQSEMQQAMDELGDLlreQQ 620
|
....*.
gi 1988774686 2329 RLEEET 2334
Cdd:pfam13779 621 QLLDET 626
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4253-4286 |
2.49e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.49e-03
10 20 30
....*....|....*....|....*....|....
gi 1988774686 4253 EETGPVAGILDIDTLEKVSVTEAIHRNLVDNITG 4286
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1372-1823 |
2.51e-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: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1372 AQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKY 1451
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1452 TAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEE--ELKRKSEAEKEAAKQKQKALEDLEKLRMQAEE 1529
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRkaEEEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1530 AERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEA 1609
Cdd:COG3064 162 AAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1610 EKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQ 1689
Cdd:COG3064 242 EAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1690 KLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQ 1769
Cdd:COG3064 322 AAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1988774686 1770 LLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAA 1823
Cdd:COG3064 402 GLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKAL 455
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
163-240 |
2.54e-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: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 163 DNFTTSWRDGKLFNAVIHK------HYPRLInmgkvyQQTNLENLEQAFSvAEKDLGVTRLLDPEDVDVPHPDEKSIITY 236
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNAlggsvpGWPNLD------PEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAY 92
|
....
gi 1988774686 237 VSSL 240
Cdd:cd21185 93 AAQL 96
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1569-1681 |
2.56e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1569 EKTSKLEESLKQEHGAVLQLQQEAERLKKQQED-AENSREEAEKELEKWRQKANEALRlrlQAEDEAHK--KTLAQEEAE 1645
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEkKEKLQEEEDKLLEEAEKEAQQAIK---EAKKEADEiiKELRQLQKG 599
|
90 100 110
....*....|....*....|....*....|....*.
gi 1988774686 1646 KQKEEAEREAKKRAKAEESALKQKEMAEEELERQRK 1681
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1351-1523 |
2.88e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1351 LDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNiqLELQELKNLSEQQIKDKSQQVDEAlhsrt 1430
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEAR--REREELQREEERLVQKEEQLDARA----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1431 kieEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEaeKLRKLAQDEAEKLRKQVSEETQKKrqAEEELKrkseaeKEAA 1510
Cdd:PRK12705 98 ---EKLDNLENQLEEREKALSARELELEELEKQLDN--ELYRVAGLTPEQARKLLLKLLDAE--LEEEKA------QRVK 164
|
170
....*....|...
gi 1988774686 1511 KQKQKALEDLEKL 1523
Cdd:PRK12705 165 KIEEEADLEAERK 177
|
|
| SH3_Eps8 |
cd11764 |
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ... |
800-835 |
2.90e-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: 2.90e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1988774686 800 QEITVHKGDECALLNNSQPFkWKVLNRSGHEAMVPS 835
Cdd:cd11764 14 KELSVLKGEYLEVLDDSRQW-WKVRNSRGQVGYVPH 48
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2106-2318 |
2.92e-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: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2106 EDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRL 2185
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2186 KdevdDAVKQRGQVEEELFKVK----VQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAEnmrkLAEDAARLSVEAQ 2261
Cdd:COG4942 110 L----RALYRLGRQPPLALLLSpedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE----LEAERAELEALLA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774686 2262 EAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQK 2318
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1491-1581 |
2.97e-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: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1491 KKRQA--EEELKRKSEAEKEAAKQKQKALEDLEKLRmqaEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFA 1568
Cdd:cd06503 29 DEREEkiAESLEEAEKAKEEAEELLAEYEEKLAEAR---AEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIE 105
|
90
....*....|...
gi 1988774686 1569 EKTSKLEESLKQE 1581
Cdd:cd06503 106 QEKEKALAELRKE 118
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2172-2357 |
2.97e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2172 DKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKL--KNKIEEENQRLIKKdkdstQKLLAEEAenmRKL 2249
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAqeQKKQAEEAAKQAAL-----KQKQAEEA---AAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2250 AEDAARLSVEAQE---AARLRQIAEDDLNQQRALAEKMLKEKMQAIQEA-SRLKAEAEMLQKQKDLAQEQAQKLLEDKQL 2325
Cdd:PRK09510 141 AAAAAKAKAEAEAkraAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAeAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|..
gi 1988774686 2326 MQQRLEEETEEYHKSLEVERKRQLEIMAEAER 2357
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1991-2581 |
3.02e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1991 EELERLRKKAEEARKQKDeadkeaekQIVVAQQAAQKCSAAEQQVQsvLAQQIEDSITQKKLKEEYEkakklakeaeaak 2070
Cdd:COG4913 235 DDLERAHEALEDAREQIE--------LLEPIRELAERYAAARERLA--ELEYLRAALRLWFAQRRLE------------- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2071 ekaereaaLLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALmQKQQADTEmakhKKLAEQT 2150
Cdd:COG4913 292 --------LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL-EREIERLE----RELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2151 LKQKfQVEQELTKVKLKLDETDKQksvLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLikk 2230
Cdd:COG4913 359 RRRA-RLEALLAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL--- 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2231 dkDSTQKLLAEEAENMRKLAEDAARLS-VEAQEAARLRQIAEDDLNQQRAlAEKML--------------KEKMQAIqEA 2295
Cdd:COG4913 432 --ERRKSNIPARLLALRDALAEALGLDeAELPFVGELIEVRPEEERWRGA-IERVLggfaltllvppehyAAALRWV-NR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2296 SRLKAEAEMLQKQKDLAQEQAQKLLED-----------------KQLMQQRL-------EEETEEYHKSL---------- 2341
Cdd:COG4913 508 LHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfrawlEAELGRRFdyvcvdsPEELRRHPRAItragqvkgng 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2342 ---------EVERKRQLEIMAEA--ERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLH---------ETEIATQEKM 2401
Cdd:COG4913 588 trhekddrrRIRSRYVLGFDNRAklAALEAELAELEEELAEAEERLEALEAELDALQERREalqrlaeysWDEIDVASAE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2402 TVVERLEFERLNTSKEADDLRKA---IADLENEKARLKKEAEELQNK----SKEMADAQQkKIEHEKTVLQQtfMTEKEM 2474
Cdd:COG4913 668 REIAELEAELERLDASSDDLAALeeqLEELEAELEELEEELDELKGEigrlEKELEQAEE-ELDELQDRLEA--AEDLAR 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2475 LLKKEKLieDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELER--Q 2552
Cdd:COG4913 745 LELRALL--EERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLAllD 822
|
650 660
....*....|....*....|....*....
gi 1988774686 2553 RLEQERiLAEENQKLREKLQQLEDAQKDQ 2581
Cdd:COG4913 823 RLEEDG-LPEYEERFKELLNENSIEFVAD 850
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2140-2523 |
3.06e-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: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2140 MAKHKKLAEQtlkqkfqvEQELTKVKLKLDETDKQKSVLDEELQRLKDE---VDDAVKQRGQVEEelfkvkvQMEELLKL 2216
Cdd:COG3096 295 FGARRQLAEE--------QYRLVEMARELEELSARESDLEQDYQAASDHlnlVQTALRQQEKIER-------YQEDLEEL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2217 KNKIEEenqrlikkdkdstQKLLAEEAENMRKLAEDAARLSVEaqEAARLR-QIAED----DLNQQRALAekmLKEKMQA 2291
Cdd:COG3096 360 TERLEE-------------QEEVVEEAAEQLAEAEARLEAAEE--EVDSLKsQLADYqqalDVQQTRAIQ---YQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2292 IQEASRLKAEAEMLQKQKDLAQEQAQKllEDKQLMQQRLEEET---------EEYHKSL--------EVER----KRQLE 2350
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRA--KEQQATEEVLELEQklsvadaarRQFEKAYelvckiagEVERsqawQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2351 IMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADkvATRLHEtEIATQEKMTVVERLEFERLNTSKEA--DDLRKAIADL 2428
Cdd:COG3096 500 LLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQN--AERLLE-EFCQRIGQQLDAAEELEELLAELEAqlEELEEQAAEA 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2429 ENEKARLKKEAEELQNKSKEMAD------AQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKrlesqfeeevkkAKA 2502
Cdd:COG3096 577 VEQRSELRQQLEQLRARIKELAArapawlAAQDALERLREQSGEALADSQEVTAAMQQLLERERE------------ATV 644
|
410 420
....*....|....*....|.
gi 1988774686 2503 LKDEQERQKQQMEQEKKTLQA 2523
Cdd:COG3096 645 ERDELAARKQALESQIERLSQ 665
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
1413-1524 |
3.13e-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: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1413 QQIKDKSQQVDEALHSRTKIEEEIRL-----------IRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQdeAEKL 1481
Cdd:cd12926 15 QQYQDKSREYDQLYEEYTRTSQELQMkrtaieafnetIKIFEEQGQTQEKCSKEYLERFRREGNEKEMQRILLN--SERL 92
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1988774686 1482 RKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLR 1524
Cdd:cd12926 93 KSRIAEIHESRTKLEQDLRAQASDNREIDKRMNSLKPDLMQLR 135
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2408-2590 |
3.17e-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: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2408 EFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKskeMADAQQKKI-----EHEKTVLQQTFMTEKEMLLKKEKLI 2482
Cdd:COG3206 160 AYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAA---LEEFRQKNGlvdlsEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2483 EDEKKR--LESQFEEEVKKAKALKdeQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERIL 2560
Cdd:COG3206 237 EAEARLaaLRAQLGSGPDALPELL--QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
|
170 180 190
....*....|....*....|....*....|
gi 1988774686 2561 AEENQKLREKLQQLEDAQKDQHTRETDKVL 2590
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLA 344
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1539-1856 |
3.20e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.69 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1539 IEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEhgAVLQLQQEAERLKKQ--------------QEDAEN 1604
Cdd:PLN03229 413 VDPERKVNMKKREAVKTPVRELEGEVEKLKEQILKAKESSSKP--SELALNEMIEKLKKEidleyteaviamglQERLEN 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1605 SREEAEKELEKwRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEeSALKQKEMAEE-ELERQRKIA 1683
Cdd:PLN03229 491 LREEFSKANSQ-DQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAK-ALSEKKSKAEKlKAEINKKFK 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1684 ESTAQQKLTAEQELIRlradfDNAEQQRSLLEDELYR-LKNEVAAAqqqRKQLEDELAKVRSEMDILIQLKTKAEKETMS 1762
Cdd:PLN03229 569 EVMDRPEIKEKMEALK-----AEVASSGASSGDELDDdLKEKVEKM---KKEIELELAGVLKSMGLEVIGVTKKNKDTAE 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1763 NT------EKSKQLLEAEAAKMKDLAeEASRLRAISEEAKhqRQIAEEEAARQRAEAERI------LKEKLAAISEATRL 1830
Cdd:PLN03229 641 QTpppnlqEKIESLNEEINKKIERVI-RSSDLKSKIELLK--LEVAKASKTPDVTEKEKIealeqqIKQKIAEALNSSEL 717
|
330 340 350
....*....|....*....|....*....|...
gi 1988774686 1831 KT-----EAEIALKEK--EAENERLRRQAEDEA 1856
Cdd:PLN03229 718 KEkfeelEAELAAAREtaAESNGSLKNDDDKEE 750
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2151-2610 |
3.28e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2151 LKQKFQVEQ-ELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFkvkvQMEELLKLKNKIEEEnqrliK 2229
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN----ELSSLEDMKNRYESE-----I 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2230 KDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQK 2309
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2310 DlaqEQAQKLLEDKQLMQQRLEEETEE-----YHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKK--- 2381
Cdd:PRK01156 339 N---DYIKKKSRYDDLNNQILELEGYEmdynsYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNein 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2382 -------------QADKVATRLHETEIatQEKMTVVE-RLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSK 2447
Cdd:PRK01156 416 vklqdisskvsslNQRIRALRENLDEL--SRNMEMLNgQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVK 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2448 EMAD--AQQKKIEH-------EKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQK------- 2511
Cdd:PRK01156 494 DIDEkiVDLKKRKEyleseeiNKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKrtswlna 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2512 --QQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHT-RETDK 2588
Cdd:PRK01156 574 laVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKlRGKID 653
|
490 500
....*....|....*....|..
gi 1988774686 2589 VLHKDIIHLTTIETTKTVYNGQ 2610
Cdd:PRK01156 654 NYKKQIAEIDSIIPDLKEITSR 675
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
17-125 |
3.31e-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: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 17 ERDRVQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 87
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1988774686 88 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQVS 125
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1589-1817 |
3.50e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1589 QQEAERLKKQQEDAENSREEAE----KELEKWRQKANEAlrlRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEES 1664
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQKQAAEqerlKQLEKERLAAQEQ---KKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1665 ALkqKEMAEEELERQRKIAESTAQQKLTAEQelirlradfdnaeqqrslledelyRLKNEVAAAQQQrkqleDELAKVRS 1744
Cdd:PRK09510 155 RA--AAAAKKAAAEAKKKAEAEAAKKAAAEA------------------------KKKAEAEAAAKA-----AAEAKKKA 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 1745 EMDIliqlKTKAEKEtmsntEKSKQLLEAEAAKMKDLAEEAsrlrAISEEAKHQRQIAEEEAARQRAEAERIL 1817
Cdd:PRK09510 204 EAEA----KKKAAAE-----AKKKAAAEAKAAAAKAAAEAK----AAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
1343-1576 |
3.54e-03 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 43.41 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1343 KMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIA---AVDAEKQKTNIQLELQELK----NLSEQQI 1415
Cdd:PRK15374 107 RLAVWQAMIESQKEMGIQVSKEFQTALGEAQEATDLYEASIKKTDTAksvYDAAEKKLTQAQNKLQSLDpadpGYAQAEA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1416 KdKSQQVDEALHSRTKIEeeirliriqlettekQKYTAESelKQLRDRAAEAEKlrklAQDEAEKLRKQVSEETQkkrqa 1495
Cdd:PRK15374 187 A-VEQAGKEATEAKEALD---------------KATDATV--KAGTDAKAKAEK----ADNILTKFQGTANAASQ----- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1496 eeelkrkseaeKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLE 1575
Cdd:PRK15374 240 -----------NQVSQGEQDNLSNVARLTMLMAMFIEIVGKNTEESLQNDLALFNALQEGRQAEMEKKSAEFQEETRKAE 308
|
.
gi 1988774686 1576 E 1576
Cdd:PRK15374 309 E 309
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1753-1855 |
3.61e-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: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1753 KTKaeKETMSNT-EKSKqLLEAEAAKMKDLAEE------------ASRLRAISEEAKHQRQIAEEEAARQRAEAE--RIL 1817
Cdd:pfam04147 162 KSK--KEVMEEViAKSK-LHKYERQKAKEEDEElreeldkelkdlRSLLSGSKRPKPEQAKKPEEKPDRKKPDDDydKLV 238
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1988774686 1818 KE----KLAAISEatRLKTEAEIALKEKE----AENERLRR-QAEDE 1855
Cdd:pfam04147 239 RElafdKRAKPSD--RTKTEEELAEEEKErlekLEEERLRRmRGEED 283
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
2391-2511 |
3.63e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2391 HETEIATQEKMTVVERLEferlntsKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVlqQTFMT 2470
Cdd:COG2433 402 EHEERELTEEEEEIRRLE-------EQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREI--SRLDR 472
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1988774686 2471 EKEMLlkkEKLIEDEKKRLEsQFEEEVKKAKALKDEQERQK 2511
Cdd:COG2433 473 EIERL---ERELEEERERIE-ELKRKLERLKELWKLEHSGE 509
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1660-1827 |
3.63e-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: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1660 KAEESALKQKEMAEEELerQRKIAESTAQQkltAEQELIRLRADfdnAEQQRSLLEDElyrlknevAAAQQQRKQLEDEL 1739
Cdd:pfam12037 46 KALELMKKQEQTRQAEL--QAKIKEYEAAQ---EQLKIERQRVE---YEERRKTLQEE--------TKQKQQRAQYQDEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1740 AKVRSEMDILIQLKTKAE-----------KETMSNTEKSKQLLEAEAakmkDLAEEASRLRAISE-EAK-HQRQIAEE-- 1804
Cdd:pfam12037 110 ARKRYQDQLEAQRRRNEEllrkqeesvakQEAMRIQAQRRQTEEHEA----ELRRETERAKAEAEaEARaKEERENEDln 185
|
170 180
....*....|....*....|....
gi 1988774686 1805 -EAARQRAEAERilKEKLAAISEA 1827
Cdd:pfam12037 186 lEQLREKANEER--ETVLESINTA 207
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1946-2442 |
3.77e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1946 RAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEK--QIVVAQQ 2023
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2024 AAQKCSAAEQQVQSvLAQQIEdsitqkKLKEEYEKAKKLAKEAEAAKEKAEReaalLRQQAEEAERQKTaaEEEAANQAK 2103
Cdd:COG4717 130 LYQELEALEAELAE-LPERLE------ELEERLEELRELEEELEELEAELAE----LQEELEELLEQLS--LATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2104 AQEDAERLRKE-AEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEEL 2182
Cdd:COG4717 197 LAEELEELQQRlAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2183 QRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKL--KNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEA 2260
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLGKEAEELQALpaLEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2261 QEAARLRQIAEDDLNQQRALA------EKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLmqQRLEEET 2334
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEEL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2335 EEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEaqaraeeeakkfkkqadkvATRLHETEIATQEKMTVVERLEFERLNT 2414
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEE-------------------DGELAELLQELEELKAELRELAEEWAAL 495
|
490 500
....*....|....*....|....*....
gi 1988774686 2415 SKEADDLRKAIADLENEKA-RLKKEAEEL 2442
Cdd:COG4717 496 KLALELLEEAREEYREERLpPVLERASEY 524
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1591-1867 |
3.82e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1591 EAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEahkktlaqeeaekqkeeaEREAKKRAKAEESALKQke 1670
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE------------------LEALQAEIDKLQAEIAE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1671 mAEEELERQRKIAESTAQQKLTAEQELIRLRA-----DFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSE 1745
Cdd:COG3883 77 -AEAEIEERREELGERARALYRSGGSVSYLDVllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1746 MDILIQLKTKAEKETmsnTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAIS 1825
Cdd:COG3883 156 LAELEALKAELEAAK---AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1988774686 1826 EATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQAS 1867
Cdd:COG3883 233 AAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1307-1613 |
3.87e-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: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1307 ELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELdkqKQLAEAHAKaIAKAEKEAQELKLKMQEEvsKR 1386
Cdd:pfam07888 45 ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEEL---RQSREKHEE-LEEKYKELSASSEELSEE--KD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1387 EIAAVDAEKQktniqlelQELKNLsEQQIKDKSQQVDEalhsrtkIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAE 1466
Cdd:pfam07888 119 ALLAQRAAHE--------ARIREL-EEDIKTLTQRVLE-------RETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1467 AEK-LRKLAQD-------------EAEKLRKQVSEETQKKRQAEeelkrKSEAEKEAAKQKQKALEDLEKLRMQAEEA-E 1531
Cdd:pfam07888 183 TEEeLRSLSKEfqelrnslaqrdtQVLQLQDTITTLTQKLTTAH-----RKEAENEALLEELRSLQERLNASERKVEGlG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1532 RQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSK---------LEESLKQEHGAVLQLQQEAERLKKQQEDA 1602
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRarwaqeretLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
330
....*....|.
gi 1988774686 1603 ENSREEAEKEL 1613
Cdd:pfam07888 338 RMEREKLEVEL 348
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
2479-2579 |
4.00e-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: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2479 EKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLqATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQER 2558
Cdd:pfam14817 65 DKGKAESRQSAAARRLELQKEIERLRAEISRLDKQLEARELEL-SREEAERERALDEISDSRHRQLLLEAYDQQCEEARK 143
|
90 100
....*....|....*....|.
gi 1988774686 2559 ILAEENQKLREKLQQLEDAQK 2579
Cdd:pfam14817 144 ILAEDHQRLQGQLQQLRDAAR 164
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1303-1540 |
4.18e-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: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1303 TRYSELMtltSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEahakaiaKAEKEAQELkLKMQEE 1382
Cdd:cd16269 44 AHYEEQM---EQRVQLPTETLQELLDLHAACEKEALEVFMKRSFKDEDQKFQKKLME-------QLEEKKEEF-CKQNEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1383 VSK-------REIAAVDAEKQKTNI-------QLELQELKNLSE--QQIKDKSQQVDEALH----SRTKIEEEIRLIRIQ 1442
Cdd:cd16269 113 ASSkrcqallQELSAPLEEKISQGSysvpggyQLYLEDREKLVEkyRQVPRKGVKAEEVLQeflqSKEAEAEAILQADQA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1443 LETTEKQKytaeselKQLRDRAAEAEKLRKLAQDEAEKLRKQVseETQKKRQAE--EELKRKSEAEKE-AAKQKQKALED 1519
Cdd:cd16269 193 LTEKEKEI-------EAERAKAEAAEQERKLLEEQQRELEQKL--EDQERSYEEhlRQLKEKMEEEREnLLKEQERALES 263
|
250 260
....*....|....*....|...
gi 1988774686 1520 L--EKLRMQAEEAERQVKQAEIE 1540
Cdd:cd16269 264 KlkEQEALLEEGFKEQAELLQEE 286
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1432-1522 |
4.74e-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: 40.54 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1432 IEEEIRLIRIQLETTEKQKYTAESELKQLRDR----AAEAEKLRKLAQDEAEKLRKqvseetQKKRQAEEELKR-KSEAE 1506
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKlaeaRAEAAEIIAEARKEAEAIAE------EAKAEAEAEAERiIAQAE 102
|
90
....*....|....*.
gi 1988774686 1507 KEAAKQKQKALEDLEK 1522
Cdd:COG0711 103 AEIEQERAKALAELRA 118
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1472-1890 |
4.76e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.25 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1472 KLAQDEAEKLRKQVS------EETQKkrQAEEELKRKSEAEKEAAKQKQKALEDLEKL------------RMQAEEAERQ 1533
Cdd:PRK10246 194 KSARTELEKLQAQASgvalltPEQVQ--SLTASLQVLTDEEKQLLTAQQQQQQSLNWLtrldelqqeasrRQQALQQALA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1534 VKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEK-- 1611
Cdd:PRK10246 272 AEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNtw 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1612 --ELEKWRQKANEALRLRL----QAEDEAHKKTLAQEEAEKQkeeaereaKKRAKAEESALkqkEMAEEELERQRkiAES 1685
Cdd:PRK10246 352 laEHDRFRQWNNELAGWRAqfsqQTSDREQLRQWQQQLTHAE--------QKLNALPAITL---TLTADEVAAAL--AQH 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1686 TAQQKLtaEQELIRLRAdfdnaeqQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEM----DILIQLKTKAEKE-T 1760
Cdd:PRK10246 419 AEQRPL--RQRLVALHG-------QIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYkektQQLADVKTICEQEaR 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1761 MSNTEKSKQLLEA---------------EAAKMKDLAEEASRLRAISEEAKhqrQIAEEEAA-------------RQRAE 1812
Cdd:PRK10246 490 IKDLEAQRAQLQAgqpcplcgstshpavEAYQALEPGVNQSRLDALEKEVK---KLGEEGAAlrgqldaltkqlqRDESE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1813 AERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAY-----QRKALEDQASQHKQEI---EEKIVQLKKSS 1884
Cdd:PRK10246 567 AQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQlrllsQRHELQGQIAAHNQQIiqyQQQIEQRQQQL 646
|
....*.
gi 1988774686 1885 EAEMER 1890
Cdd:PRK10246 647 LTALAG 652
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2133-2361 |
4.85e-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: 42.60 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2133 KQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFK-VKVQME 2211
Cdd:pfam13868 58 EEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREeIDEFNE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2212 ELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARlsvEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQA 2291
Cdd:pfam13868 138 EQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEE---KEREIARLRAQQEKAQDEKAERDELRAKLYQEE 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 2292 IQEASRLKAEAEMLQKQK---DLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQ 2361
Cdd:pfam13868 215 QERKERQKEREEAEKKARqrqELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMK 287
|
|
| PRK01558 |
PRK01558 |
V-type ATP synthase subunit E; Provisional |
1468-1559 |
4.93e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 179302 Cd Length: 198 Bit Score: 41.28 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1468 EKLRKLAQDEAEKLRKQVSEETQKKRqaeEELKRKseAEKEAAKQKQKALEDLEKLRMQAEEAERQ-VKQAEIEKEKQIK 1546
Cdd:PRK01558 10 NKIKKDGLEEAERLANEIILEAKEEA---EEIIAK--AEEEAKELKAKAEKEANDYKRHALEASRQaGRDLLISFEKSIK 84
|
90
....*....|...
gi 1988774686 1547 VAHEAAQKSAAAE 1559
Cdd:PRK01558 85 SLFKAALKDEVAE 97
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
2405-2573 |
4.94e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.38 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2405 ERLEFERLN-TSKE------ADDLRkaiADLENEKARLKKEAEELQNKSK---EMADAQQKKIE-HEKTVLQQTFMTEKE 2473
Cdd:PLN03188 1047 KKLEQERLRwTEAEskwislAEELR---TELDASRALAEKQKHELDTEKRcaeELKEAMQMAMEgHARMLEQYADLEEKH 1123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2474 MLL-----KKEKLIEDEKKRL--------ESQFEEEVK-KAKALKDEQERQKQQMEQEKKTLQATM-DAA---------L 2529
Cdd:PLN03188 1124 IQLlarhrRIQEGIDDVKKAAaragvrgaESKFINALAaEISALKVEREKERRYLRDENKSLQAQLrDTAeavqaagelL 1203
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1988774686 2530 SKQKEAEEEMLRKQKEMQELERQrleqerilAEENQKLREKLQQ 2573
Cdd:PLN03188 1204 VRLKEAEEALTVAQKRAMDAEQE--------AAEAYKQIDKLKR 1239
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
16-119 |
5.10e-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: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 16 DERDRVQkktFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETL-------PREKGRM--RFHK 77
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIdervlnkPPRKNKPlnNFQM 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1988774686 78 LQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 119
Cdd:cd21294 81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1779-1908 |
5.18e-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: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1779 KDLAEEASRLRAISE-EAKHQRQIAEEEAARQRAEAErilKEKLAAISEATRLKTEAEIALK--EKEAENERLRRQAEDE 1855
Cdd:COG2268 191 RRKIAEIIRDARIAEaEAERETEIAIAQANREAEEAE---LEQEREIETARIAEAEAELAKKkaEERREAETARAEAEAA 267
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774686 1856 AYQRKALEDQASQHKQEIEEKIVQLK---KSSEAEMERQKAIVDDTLK-QRRVVEEE 1908
Cdd:COG2268 268 YEIAEANAEREVQRQLEIAEREREIElqeKEAEREEAELEADVRKPAEaEKQAAEAE 324
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
22-119 |
5.37e-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: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 22 QKKTFTKWVNKHL---------IKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 87
Cdd:cd21293 2 EKGSYVDHINRYLgddpflkqfLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1988774686 88 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 119
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2257-2536 |
5.66e-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: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2257 SVEAQEAARLRQIAEDDLNQQRALAEKmlkekmqAIQEASRLKAEAEMLQKQKDLAQEQAQklLEDKQlmQQRLEEETEE 2336
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK-------ERAEADRQRLEQEKQQQLAAISGSQSQ--LESTD--QNALETNGQA 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2337 YHKSLEVERKrqlEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQ-----ADKVATRLHETEIATQEKMTVVERLEFER 2411
Cdd:NF012221 1607 QRDAILEESR---AVTKELTTLAQGLDALDSQATYAGESGDQWRNPfagglLDRVQEQLDDAKKISGKQLADAKQRHVDN 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2412 LNTSKEAddLRKAIADLENEKaRLKKEAEelQNKSKEMADAQQKKiehektvlqqtfmteKEMLLKKEkliedEKKRLES 2491
Cdd:NF012221 1684 QQKVKDA--VAKSEAGVAQGE-QNQANAE--QDIDDAKADAEKRK---------------DDALAKQN-----EAQQAES 1738
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1988774686 2492 QFEEEVKKAKalkdeQERQKQQMEQEKKTLQATMDAALSKQKEAE 2536
Cdd:NF012221 1739 DANAAANDAQ-----SRGEQDASAAENKANQAQADAKGAKQDESD 1778
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1469-1696 |
5.67e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1469 KLRKLAQDEAEKlRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVA 1548
Cdd:PRK11637 48 QLKSIQQDIAAK-EKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1549 heaAQKSAAAELQSKHmsfaektSKLEESLKQEHGavlqlqQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLrL 1628
Cdd:PRK11637 127 ---AAQLDAAFRQGEH-------TGLQLILSGEES------QRGERILAYFGYLNQARQETIAELKQTREELAAQKAE-L 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774686 1629 QAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAE-ESALKQK-----EMAEEELERQRKIAESTAQQKLTAEQE 1696
Cdd:PRK11637 190 EEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGlESSLQKDqqqlsELRANESRLRDSIARAEREAKARAERE 263
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3662-3698 |
5.86e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.08 E-value: 5.86e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1988774686 3662 KQYLYGTGCVAGIT-TDSSSKLSIYQAMKRGFIKPEIG 3698
Cdd:smart00250 1 QRLLEAQSAIGGIIdPETGQKLSVEEALRRGLIDPETG 38
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2215-2362 |
5.90e-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: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2215 KLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQ---IAEDDLNQQRALAEKMLKEKMQA 2291
Cdd:pfam05262 181 KVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQkadFAQDNADKQRDEVRQKQQEAKNL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2292 ------------IQEASRLKAEAEMLQKQKDLAQEQAQKLLEDK--QLMQQRLEEETEEYHKSLEVERKRqLEIMAEAER 2357
Cdd:pfam05262 261 pkpadtsspkedKQVAENQKREIEKAQIEIKKNDEEALKAKDHKafDLKQESKASEKEAEDKELEAQKKR-EPVAEDLQK 339
|
....*
gi 1988774686 2358 LRLQV 2362
Cdd:pfam05262 340 TKPQV 344
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2309-2573 |
5.92e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2309 KDLAQEQAQKLLEDKQLMQQRleeeteeyhKSLEVERKRQLEIMAEAER-LRLQVSQLSeaqaraeeeakKFKKQADKVA 2387
Cdd:PRK11637 50 KSIQQDIAAKEKSVRQQQQQR---------ASLLAQLKKQEEAISQASRkLRETQNTLN-----------QLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2388 TRLH--ETEIATQEKMTvverleferlntskeADDLRKAIADLENEKARLKKEAEELQNKSKEMA------DAQQKKIEH 2459
Cdd:PRK11637 110 ASIAklEQQQAAQERLL---------------AAQLDAAFRQGEHTGLQLILSGEESQRGERILAyfgylnQARQETIAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2460 ektvLQQTfmtekemllkKEKLIEdEKKRLESQFEEEvkkaKALKDEQERQKQQMEQ----EKKTLqATMDAALSKQKE- 2534
Cdd:PRK11637 175 ----LKQT----------REELAA-QKAELEEKQSQQ----KTLLYEQQAQQQKLEQarneRKKTL-TGLESSLQKDQQq 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1988774686 2535 -----AEEEMLRKQKEMQELE-RQRLEQErilAEENQKLREKLQQ 2573
Cdd:PRK11637 235 lselrANESRLRDSIARAEREaKARAERE---AREAARVRDKQKQ 276
|
|
| MRP-S27 |
pfam10037 |
Mitochondrial 28S ribosomal protein S27; Members of this family of small ribosomal proteins ... |
1666-1819 |
5.99e-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: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1666 LKQKEMAEEELERQRKIAESTAQQKLTAE--QELIRLRADFDNAEqqrsllEDELYRLKNEVAAAQQQRKQLEdELAKVR 1743
Cdd:pfam10037 259 LGKVGYLDRALSVMEKVASSPGDLKLHKEvlDVLQDILETLDELE------ESEQSKLPEYVKSFQELLSKLQ-SLGKVE 331
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774686 1744 SEmdILIQLKTKAEKETMSNTEKskQLLEAEAAKMKDLAEEasRLRAISEEAKHQrqiaeeEAARQRAEAERILKE 1819
Cdd:pfam10037 332 SE--SLLTLLENLVKESLPACEE--KDLANYEQLYQEWEEE--RRQLIQREKEMR------EKAEREDEARKALKE 395
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1433-1540 |
6.07e-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: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1433 EEEIRLIRIQLETTEKQKYTAESE----LKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKE 1508
Cdd:pfam05672 17 AEKRRQAREQREREEQERLEKEEEerlrKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQ 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1988774686 1509 AAKQKQK------ALEDLEKLR------MQAEEAERQVKQAEIE 1540
Cdd:pfam05672 97 ERLQKQKeeaeakAREEAERQRqerekiMQQEEQERLERKKRIE 140
|
|
| iSH2_PIK3R1 |
cd12924 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
1413-1543 |
6.18e-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: 40.45 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1413 QQIKDKSQQVDEALHSRTKIEEEIRLIRIQLET-TEKQKYTAESELKQLRDRAAEAEKLRKLAQDEA--------EKLRK 1483
Cdd:cd12924 15 TQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAfNETIKIFEEQCQTQERYSKEYIEKFKREGNEKEiqrimhnyEKLKS 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1484 QVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEK 1543
Cdd:cd12924 95 RISEIVDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKK 154
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
1341-1509 |
6.43e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 41.02 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1341 RKKMAEmqaeldkqKQLAEAHAKA---IAKAEKEAQELK----LKMQEEVSKREiaaVDAEKQKTNIQLELQELKNL--- 1410
Cdd:pfam12072 21 RKSIAE--------AKIGSAEELAkriIEEAKKEAETKKkealLEAKEEIHKLR---AEAERELKERRNELQRQERRllq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1411 SEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLEttEKQKYTAESELKQLrdraAEAEKLRKLAQDEAEK-LRKQVSEET 1489
Cdd:pfam12072 90 KEETLDRKDESLEKKEESLEKKEKELEAQQQQLE--EKEEELEELIEEQR----QELERISGLTSEEAKEiLLDEVEEEL 163
|
170 180
....*....|....*....|....*
gi 1988774686 1490 QKK-----RQAEEELKRksEAEKEA 1509
Cdd:pfam12072 164 RHEaavmiKEIEEEAKE--EADKKA 186
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2209-2356 |
6.47e-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: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2209 QMEELLKLKNKIEEENQRLIKKdKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEK 2288
Cdd:COG2268 193 KIAEIIRDARIAEAEAERETEI-AIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIA 271
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774686 2289 MQAIQEASRLKAEAEMLQKQKDLAQEQAQKlledkqlmqqRLEEETEEYHKSLEVERKRQlEIMAEAE 2356
Cdd:COG2268 272 EANAEREVQRQLEIAEREREIELQEKEAER----------EEAELEADVRKPAEAEKQAA-EAEAEAE 328
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1465-1544 |
6.51e-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: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1465 AEAEKLRKlaqdEAEKLRKQVSEETQK-KRQAEEELKrksEAEKEAAKQKQKALEDLEklrmqaEEAERQVKQA--EIEK 1541
Cdd:cd06503 40 EEAEKAKE----EAEELLAEYEEKLAEaRAEAQEIIE---EARKEAEKIKEEILAEAK------EEAERILEQAkaEIEQ 106
|
...
gi 1988774686 1542 EKQ 1544
Cdd:cd06503 107 EKE 109
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2469-2584 |
6.57e-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: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2469 MTEKEMLLKKEKlieDEKKRLESQFEEEVKKAKALKDEQERQ-KQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQ 2547
Cdd:pfam13868 28 IAEKKRIKAEEK---EEERRLDEMMEEERERALEEEEEKEEErKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMD 104
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774686 2548 ELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTR 2584
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAE 141
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2428-2585 |
6.84e-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: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2428 LENEKARLKKEAEELQNKSKEMADAQQKKIE-----HEKTVLQQTFMTEKEMLLKKEKLIEDE--KKRLESQ--FEEEVK 2498
Cdd:cd16269 108 KQNEEASSKRCQALLQELSAPLEEKISQGSYsvpggYQLYLEDREKLVEKYRQVPRKGVKAEEvlQEFLQSKeaEAEAIL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2499 KAKALKDEQERQKQqmEQEKKTLQATMDAALSKQKEAEEEMLRKQ-----KEMQELERQRLEQER--ILAEENQKLREKL 2571
Cdd:cd16269 188 QADQALTEKEKEIE--AERAKAEAAEQERKLLEEQQRELEQKLEDqersyEEHLRQLKEKMEEERenLLKEQERALESKL 265
|
170
....*....|....
gi 1988774686 2572 QQLEDAQKDQHTRE 2585
Cdd:cd16269 266 KEQEALLEEGFKEQ 279
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1323-1591 |
6.92e-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: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1323 QRRLDDEEKAAEKLKAEERKKMAEMQAELDK-----QKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQK 1397
Cdd:pfam15905 75 QKELEKEIRALVQERGEQDKRLQALEEELEKveaklNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGTQKKM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1398 TNIQLELQELKNLSEQQIKdksqqvdEALHSRTKIEeeirlirIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDE 1477
Cdd:pfam15905 155 SSLSMELMKLRNKLEAKMK-------EVMAKQEGME-------GKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1478 AEKLRKQVSEETQKKRQAeEELKRKSEAEKEAAKQKQKALEDL--------EKLRMQAEEAERQVKQAEIEKEKQIKVAH 1549
Cdd:pfam15905 221 TEKLLEYITELSCVSEQV-EKYKLDIAQLEELLKEKNDEIESLkqsleekeQELSKQIKDLNEKCKLLESEKEELLREYE 299
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1988774686 1550 EAAQkSAAAELQSkhmsfaektskLEESLKQEHGAVLQLQQE 1591
Cdd:pfam15905 300 EKEQ-TLNAELEE-----------LKEKLTLEEQEHQKLQQK 329
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1328-1451 |
6.93e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1328 DEEKAAEKLKAEE-RKKMAEMQAeldkQKQLAEAHAKAIAKAEKEAQELKLKMQEEVskrEIAAVDAEKQKTNIQLELQE 1406
Cdd:PTZ00491 684 ERQKMHDKAKAEEqRTKLLELQA----ESAAVESSGQSRAEALAEAEARLIEAEAEV---EQAELRAKALRIEAEAELEK 756
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1988774686 1407 LKNLSEQQIKdksqqvdealHSRTKIEEEIRLIRiQLETTEKQKY 1451
Cdd:PTZ00491 757 LRKRQELELE----------YEQAQNELEIAKAK-ELADIEATKF 790
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1657-1890 |
7.03e-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: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1657 KRAKAEESALKQkemaeeELErqrkiaeSTAQQKLTAEQELIRLRADFDNAEQQ-RSLLEDELYRLKNEVAAAQQQ---- 1731
Cdd:pfam05911 20 EKAEAEALALKQ------QLE-------SVTLQKLTAEERAAHLDGALKECMQQlRNVKEEQEQKIHDVVLKKTKEweki 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1732 RKQLEDELAkvrsemdiliqlktkaeketmsntEKSKQLLEAEAakmkdlaeEASRL-RAISEEAKHQRQIAEEEAarqR 1810
Cdd:pfam05911 87 KAELEAKLV------------------------ETEQELLRAAA--------ENDALsRSLQERENLLMKLSEEKS---Q 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1811 AEAE-RILKEKLAAIS-EATRLKTEAEIALKEKEAENERL---RRQAEdeayqrkaledqaSQHKQEIE--EKIVQLkks 1883
Cdd:pfam05911 132 AEAEiEALKSRLESCEkEINSLKYELHVLSKELEIRNEEKnmsRRSAD-------------AAHKQHLEsvKKIAKL--- 195
|
....*..
gi 1988774686 1884 sEAEMER 1890
Cdd:pfam05911 196 -EAECQR 201
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
1708-1873 |
7.05e-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: 40.03 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1708 EQQRSLLEDELYRLKNEVAaaqqqRKQLEDELAKVRSEMDILIQLKTKAEKETMsntekskqlleaeaakMKDLAEEASR 1787
Cdd:pfam15346 2 EAESKLLEEETARRVEEAV-----AKRVEEELEKRKDEIEAEVERRVEEARKIM----------------EKQVLEELER 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1788 LRAISEEAKHQRqiaEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEaenerlrRQAEDEAYQRKALEDQAS 1867
Cdd:pfam15346 61 EREAELEEERRK---EEEERKKREELERILEENNRKIEEAQRKEAEERLAMLEEQ-------RRMKEERQRREKEEEERE 130
|
....*.
gi 1988774686 1868 QHKQEI 1873
Cdd:pfam15346 131 KREQQK 136
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2403-2508 |
7.24e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2403 VVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQN-KSKEMADAQQK--------KIEHEKTVLQQTFMTEKE 2473
Cdd:PRK00409 521 LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeEDKLLEEAEKEaqqaikeaKKEADEIIKELRQLQKGG 600
|
90 100 110
....*....|....*....|....*....|....*
gi 1988774686 2474 MLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQE 2508
Cdd:PRK00409 601 YASVKAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4259-4289 |
7.36e-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: 7.36e-03
10 20 30
....*....|....*....|....*....|.
gi 1988774686 4259 AGILDIDTLEKVSVTEAIHRNLVDNITGQRL 4289
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1673-1849 |
7.41e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1673 EEELER-QRKIAEST------AQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAkvrSE 1745
Cdd:PRK09039 52 DSALDRlNSQIAELAdllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELD---SE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1746 mdiliqlktkaeketmsnteksKQLLEAEAAKMKDLAEEASRLRaiseeakhqRQIAEEEAARQRAEAERilKEKLAAIS 1825
Cdd:PRK09039 129 ----------------------KQVSARALAQVELLNQQIAALR---------RQLAALEAALDASEKRD--RESQAKIA 175
|
170 180
....*....|....*....|....
gi 1988774686 1826 EatrLKTEAEIALKEKEAENERLR 1849
Cdd:PRK09039 176 D---LGRRLNVALAQRVQELNRYR 196
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1447-1534 |
7.55e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 39.99 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1447 EKQKYTAESElKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEElkrksEAEKEAAKQKQKALEDLEKlrmQ 1526
Cdd:PRK07353 54 EAEKLEAQYE-QQLASARKQAQAVIAEAEAEADKLAAEALAEAQAEAQASKE-----KARREIEQQKQAALAQLEQ---Q 124
|
....*...
gi 1988774686 1527 AEEAERQV 1534
Cdd:PRK07353 125 VDALSRQI 132
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
2163-2495 |
7.57e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.53 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2163 KVKLKLDETDKQKSV-LDEELQRLKDEVDDAVKQRGQVEEELFKvkvqmEELLKLKNKIEEENQRLIKKdKDSTQKLLAE 2241
Cdd:PLN03229 418 KVNMKKREAVKTPVReLEGEVEKLKEQILKAKESSSKPSELALN-----EMIEKLKKEIDLEYTEAVIA-MGLQERLENL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2242 EAENMRKLAEDAARLSVEAQEAARLRQiaEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLE 2321
Cdd:PLN03229 492 REEFSKANSQDQLMHPVLMEKIEKLKD--EFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKE 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2322 --DKQLMQQRLEEETEEYHKSleverkrqlEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQE 2399
Cdd:PLN03229 570 vmDRPEIKEKMEALKAEVASS---------GASSGDELDDDLKEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTAE 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2400 KMTVVE-RLEFERLN--TSKEADDLRKAiADLENEKARLKKeaeELQNKSKEMADAQQKKIEHEKTVLQQTF---MTEKE 2473
Cdd:PLN03229 641 QTPPPNlQEKIESLNeeINKKIERVIRS-SDLKSKIELLKL---EVAKASKTPDVTEKEKIEALEQQIKQKIaeaLNSSE 716
|
330 340
....*....|....*....|..
gi 1988774686 2474 MLLKKEKLIEDEKKRLESQFEE 2495
Cdd:PLN03229 717 LKEKFEELEAELAAARETAAES 738
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1575-1924 |
7.57e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 42.40 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1575 EESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELekwrQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAERE 1654
Cdd:pfam03528 3 DEDLQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKEL----YLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1655 AKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIR--LRADFDNAE--QQRSLLEDELYRLKNEVAAAQQ 1730
Cdd:pfam03528 79 NIKAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVREYEVQfhRRLEQERAQwnQYRESAEREIADLRRRLSEGQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1731 QrKQLEDELAKVRSEMDILIQLKTKAEKETMS----NTEKSKQLLEAEAAKMKDL-----AEEASR--LRAISEEAKHQR 1799
Cdd:pfam03528 159 E-ENLEDEMKKAQEDAEKLRSVVMPMEKEIAAlkakLTEAEDKIKELEASKMKELnhyleAEKSCRtdLEMYVAVLNTQK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1800 QIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIAlKEKEAENERLRRQaedeAYQRKALEDQASQHKQEIEEKivq 1879
Cdd:pfam03528 238 SVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKA-NDQFLESQRLLMR----DMQRMESVLTSEQLRQVEEIK--- 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1988774686 1880 lKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKL 1924
Cdd:pfam03528 310 -KKDQEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVETSAPL 353
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
2448-2566 |
7.87e-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: 40.16 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2448 EMADAQQKKIEHEKTVLQQtfMTEKEmllkKEKLIEDEKKRLESQFEEEvkkakALKDEQERQKQQMEQEKKtlqatmda 2527
Cdd:pfam15236 46 ERERKRQKALEHQNAIKKQ--LEEKE----RQKKLEEERRRQEEQEEEE-----RLRREREEEQKQFEEERR-------- 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1988774686 2528 alsKQKEAEEEMLRKQKEM-QELER-----QRLEQERILAEENQK 2566
Cdd:pfam15236 107 ---KQKEKEEAMTRKTQALlQAMQKaqelaQRLKQEQRIRELAEK 148
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1885-2452 |
7.91e-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: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1885 EAEMERQKAI---VDDTLKQRRVVEEEIRILKLNfeKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEE 1961
Cdd:pfam05557 1 RAELIESKARlsqLQNEKKQMELEHKRARIELEK--KASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1962 EKRRREAEEKVKKIAAAEEEAA-----------------RQRKAALEELERLRKKAEEARKQKDEADK---EAEKQIVVA 2021
Cdd:pfam05557 79 RLKKKYLEALNKKLNEKESQLAdarevisclknelselrRQIQRAELELQSTNSELEELQERLDLLKAkasEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2022 QQAAQKCSAAEQQVQSV---LAQQIEDSITQKKLKEEyekakklakeaeaaKEKAEREAALLRQQAEEAERQKTAAEEEA 2098
Cdd:pfam05557 159 EKQQSSLAEAEQRIKELefeIQSQEQDSEIVKNSKSE--------------LARIPELEKELERLREHNKHLNENIENKL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2099 ANQAKAQEDAERLRKEAEfeaakraqaeaaalMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVK-----LKLDETDK 2173
Cdd:pfam05557 225 LLKEEVEDLKRKLEREEK--------------YREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpedlsRRIEQLQQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2174 QKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQ-----KLLAEEAENMRK 2248
Cdd:pfam05557 291 REIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKerdgyRAILESYDKELT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2249 LAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQ--------EQAQKLL 2320
Cdd:pfam05557 371 MSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADpsyskeevDSLRRKL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2321 EDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEiATQEK 2400
Cdd:pfam05557 451 ETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLE-DDLEQ 529
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 2401 MTVVERLEFERLNtsKEADDLRKaiaDLENEKARLKKEAEELQNKSKEMADA 2452
Cdd:pfam05557 530 VLRLPETTSTMNF--KEVLDLRK---ELESAELKNQRLKEVFQAKIQEFRDV 576
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1475-1734 |
7.92e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1475 QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAeRQVKQAEIEKEKQIKvaheaAQK 1554
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQEL-REKRDELNEKVKELK-----EER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1555 SAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEA 1634
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1635 HKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAE--EELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRS 1712
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIElyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260
....*....|....*....|..
gi 1988774686 1713 LLEDELYRLKNEVAAAQQQRKQ 1734
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEK 262
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
28-86 |
8.06e-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: 8.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774686 28 KWVNKHLikAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALD 86
Cdd:cd21184 8 EWVNSKI--PEYKVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPLENATKAMD 64
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2320-2552 |
8.20e-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: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2320 LEDKQLMQQRLEEETEEyHKSLEVERKRQleimAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRlheteiatqe 2399
Cdd:pfam15709 328 REQEKASRDRLRAERAE-MRRLEVERKRR----EQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLR---------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2400 kmtvVERLEFERLNTSKEAddlRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKiEHEKTVLQQTFMTEKEMLLKke 2479
Cdd:pfam15709 393 ----KQRLEEERQRQEEEE---RKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQE-EAERAEAEKQRQKELEMQLA-- 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 2480 klieDEKKRLESQFEEEvkkakalKDEQERQKQqmEQEKKTLQatmDAALSKQKEAEEEMLRKQKEMQELERQ 2552
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 ... |
1408-1690 |
8.38e-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: 41.72 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1408 KNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSE 1487
Cdd:pfam15905 54 RKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1488 ETQkkrqAEEELKRKSEAEKEAAKQKQKALEdLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAA--AELQSKHM 1565
Cdd:pfam15905 134 LTR----VNELLKAKFSEDGTQKKMSSLSME-LMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGkvAQLEEKLV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1566 SFA-EKTSKLEESLKQEHgAVLQLQQEAERLKKQQEDAENSREEAEKelekwRQKANEALRLRLQAEDEAHKKTLAQEEA 1644
Cdd:pfam15905 209 STEkEKIEEKSETEKLLE-YITELSCVSEQVEKYKLDIAQLEELLKE-----KNDEIESLKQSLEEKEQELSKQIKDLNE 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1988774686 1645 EKQKEEAEREAKKRAKAEESALKQKEMAE-EELERQRKIAESTAQQK 1690
Cdd:pfam15905 283 KCKLLESEKEELLREYEEKEQTLNAELEElKEKLTLEEQEHQKLQQK 329
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2410-2570 |
8.44e-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: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2410 ERLNTSKEAD-DLRKAIADLeneKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQtfmteKEMLLKKEKLIEDEKKR 2488
Cdd:pfam05262 184 EALREDNEKGvNFRRDMTDL---KERESQEDAKRAQQLKEELDKKQIDADKAQQKADF-----AQDNADKQRDEVRQKQQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2489 LESQFEE--EVKKAKALKDEQERQKQ-----QMEQEKKT---LQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEqer 2558
Cdd:pfam05262 256 EAKNLPKpaDTSSPKEDKQVAENQKReiekaQIEIKKNDeeaLKAKDHKAFDLKQESKASEKEAEDKELEAQKKREP--- 332
|
170
....*....|..
gi 1988774686 2559 iLAEENQKLREK 2570
Cdd:pfam05262 333 -VAEDLQKTKPQ 343
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2466-2586 |
8.63e-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: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2466 QTFMTEKEMLLKKEKLIEDEKKRLESQFEEE--------VKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEE 2537
Cdd:pfam15709 301 QTFVVTGNMESEEERSEEDPSKALLEKREQEkasrdrlrAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELEL 380
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1988774686 2538 EMLRKQKEMQeLERQRLEQERILAEE---NQKLREKLQQLEDAQKDQHTRET 2586
Cdd:pfam15709 381 EQQRRFEEIR-LRKQRLEEERQRQEEeerKQRLQLQAAQERARQQQEEFRRK 431
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
2323-2517 |
8.72e-03 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 41.86 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2323 KQLMQQRLEEETEEYHKSLEVERKRQLEI-MAEAERLRLQVSQLSeaqaraeeeakkfKKQADKVATRLHETEIATQEKM 2401
Cdd:COG4487 21 ADIVKQRRAEFEKELAERLADAAKREAALeLAEAKAKAQLQEQVA-------------EKDAEIAELRARLEAEERKKAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 2402 TVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQ-QTFMTEKEMLLKKEK 2480
Cdd:COG4487 88 AVAEEKEKELAALQEALAEKDAKLAELQAKELELLKKERELEDAKREAELTVEKERDEELDELKeKLKKEEEEKQLAEKS 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1988774686 2481 LIEDEKkrlESQFEEEVKKAKALKDEQERQKQQMEQE 2517
Cdd:COG4487 168 LKVAEY---EKQLKDMQEQIEELKRKKEQGSTQLQGE 201
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3939-3973 |
8.95e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 36.69 E-value: 8.95e-03
10 20 30
....*....|....*....|....*....|....*
gi 1988774686 3939 LLESQAATGYVIDPIKNLKLTVNEAVKMGIVGPEF 3973
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1653-1744 |
8.99e-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: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1653 REAKKRAKAEESALKQKE-MAEEELERQRKIAEsTAQQKLTAE--------QELIRLRADFDNAEQQRSLLEDELYRLKN 1723
Cdd:pfam07926 7 QSEIKRLKEEAADAEAQLqKLQEDLEKQAEIAR-EAQQNYERElvlhaediKALQALREELNELKAEIAELKAEAESAKA 85
|
90 100
....*....|....*....|....*
gi 1988774686 1724 EVAAAQ----QQRKQLEDELAKVRS 1744
Cdd:pfam07926 86 ELEESEesweEQKKELEKELSELEK 110
|
|
| SPFH_like_u4 |
cd03407 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1716-1864 |
9.07e-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: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1716 DELYRLKNEVAaaqqqrKQLEDELAKVRSEMDILIqlktkaeketmsntekskqlleaEAAKMKDLAEEASRLRAISEEA 1795
Cdd:cd03407 106 DEVFESKDEIA------KAVKEELAKVMSEYGYEI-----------------------VKTLVTDIEPDASVKAAMNEIN 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774686 1796 KHQRqiaEEEAARQRAEAERILKEKLAaiseatrlkteaeialkekEAENERLRRQAEDEAYQRKALED 1864
Cdd:cd03407 157 AAQR---LREAAEEKAEAEKILQVKAA-------------------EAEAEAKRLQGVGIAEQRKAIVD 203
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
1443-1581 |
9.38e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 41.54 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774686 1443 LETTEKQKYTAESELKQlrdraaeaEKLRKLAQDEAEKLRKQVSEETQKKRQAEEElkrksEAEKEAAKQKQKALEDLEK 1522
Cdd:PRK06669 30 LSIKEKERLREEEEEQV--------EQLREEANDEAKEIIEEAEEDAFEIVEAAEE-----EAKEELLKKTDEASSIIEK 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774686 1523 LRMQaeeAERQVKQAEIEKEKQIKVA----HEAAQKSAAAELQSKHMSFAEKTSKLEESLKQE 1581
Cdd:PRK06669 97 LQMQ---IEREQEEWEEELERLIEEAkaegYEEGYEKGREEGLEEVRELIEQLNKIIEKLIKK 156
|
|
| |
