|
Name |
Accession |
Description |
Interval |
E-value |
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
176-281 |
3.29e-71 |
|
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: 234.14 E-value: 3.29e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 176 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 255
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1207141765 256 PEDVDVPHPDEKSIITYVSSMYDVMP 281
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
42-163 |
7.02e-70 |
|
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: 230.37 E-value: 7.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 42 DRVQKKTFTKWVNKHLVKHWkaeaqRHITDLYEDLRDGHNLISLLEVLSGETLPRERdvvrnsrlprekGRMRFHKLQNV 121
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKAR-----RRVVDLFEDLRDGHNLISLLEVLSGESLPRER------------GRMRFHRLQNV 63
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207141765 122 QIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 163
Cdd:cd21188 64 QTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
39-174 |
1.50e-67 |
|
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: 224.52 E-value: 1.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 39 DERDRVQKKTFTKWVNKHLVKhwkaeAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlpreKGRMRFHKL 118
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK-----AQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE------------KGRMRFHKL 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141765 119 QNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQSD 174
Cdd:cd21235 64 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
177-281 |
1.07e-65 |
|
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: 218.41 E-value: 1.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 256
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1207141765 257 EDVDVPHPDEKSIITYVSSMYDVMP 281
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
38-172 |
4.90e-64 |
|
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: 214.85 E-value: 4.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 38 KDERDRVQKKTFTKWVNKHLVKhwkaeAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlpreKGRMRFHK 117
Cdd:cd21236 11 KDERDKVQKKTFTKWINQHLMK-----VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPRE------------KGRMRFHR 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141765 118 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQ 172
Cdd:cd21236 74 LQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
177-281 |
9.37e-59 |
|
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: 198.67 E-value: 9.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 256
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1207141765 257 EDVDVPHPDEKSIITYVSSMYDVMP 281
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
39-173 |
1.41e-56 |
|
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: 192.94 E-value: 1.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 39 DERDRVQKKTFTKWVNKHLVKhwkaeAQRHITDLYEDLRDGHNLISLLEVLSGetlprerdvvrnSRLPREKGRMRFHKL 118
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMK-----VRKHINDLYEDLRDGHNLISLLEVLSG------------VKLPREKGRMRFHRL 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141765 119 QNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQS 173
Cdd:cd21237 64 QNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
175-281 |
6.89e-51 |
|
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: 176.39 E-value: 6.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 175 DMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLL 254
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1207141765 255 DPEDVDVPHPDEKSIITYVSSMYDVMP 281
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
177-277 |
7.46e-48 |
|
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: 167.59 E-value: 7.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 256
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1207141765 257 EDVDVPHPDEKSIITYVSSMY 277
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
177-277 |
6.67e-46 |
|
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: 161.79 E-value: 6.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 256
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1207141765 257 EDVDVPHPDEKSIITYVSSMY 277
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
44-164 |
1.56e-45 |
|
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: 161.01 E-value: 1.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 44 VQKKTFTKWVNKHLVKHWKAeaqrHITDLYEDLRDGHNLISLLEVLSGEtlprerdvvrnsRLPREKGRMRFHKLQNVQI 123
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKP----PIKDLFEDLRDGTRLLALLEVLTGK------------KLKPEKGRMRVHHLNNVNR 65
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207141765 124 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 164
Cdd:cd21186 66 ALQVLEQNNVKLVNISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
39-160 |
3.24e-45 |
|
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: 160.23 E-value: 3.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 39 DERDRVQKKTFTKWVNKHLVKHwkaeaQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlprEKGRMRFHKL 118
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHLARV-----GCRINDLYTDLRDGRMLIKLLEVLSGERLPKP-----------TKGKMRIHCL 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207141765 119 QNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 160
Cdd:cd21246 75 ENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
40-164 |
8.22e-42 |
|
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: 150.60 E-value: 8.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 40 ERDRVQKKTFTKWVNKHLVKHwkaEAQRHITDLYEDLRDGHNLISLLEVLSGEtlprerdvvrnsRLPREKGRM--RFHK 117
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKR---KPPMKVEDLFEDIKDGTKLLALLEVLSGE------------KLPCEKGRRlkRVHF 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207141765 118 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 164
Cdd:cd21241 66 LSNINTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
43-277 |
1.68e-41 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 164.73 E-value: 1.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 43 RVQKKTFTKWVNKHLVKhwkaEAQRHITDLYEDLRDGHNLISLLEVLSGETLprerdvVRNSRLPRekgrMRFHKLQNVQ 122
Cdd:COG5069 8 KVQKKTFTKWTNEKLIS----GGQKEFGDLDTDLKDGVKLAQLLEALQKDNA------GEYNETPE----TRIHVMENVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 123 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQsddMTAKEKLLLWSQRMVEGYQ-GLRCDNF 201
Cdd:COG5069 74 GRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGE---LTKHINLLLWCDEDTGGYKpEVDTFDF 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141765 202 TTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLE--NLEQAFSIAERDLGVTRLLDPEDV-DVPHPDEKSIITYVSSMY 277
Cdd:COG5069 151 FRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
38-160 |
2.49e-40 |
|
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: 146.29 E-value: 2.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 38 KDERDRVQKKTFTKWVNKHLVKHwkaeaQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlprEKGRMRFHK 117
Cdd:cd21193 10 QEERINIQKKTFTKWINSFLEKA-----NLEIGDLFTDLSDGKLLLKLLEIISGEKLGKP-----------NRGRLRVQK 73
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141765 118 LQNVQIALDFLkHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 160
Cdd:cd21193 74 IENVNKALAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
164-277 |
7.02e-40 |
|
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: 145.20 E-value: 7.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 164 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 243
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141765 244 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 277
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYY 111
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
176-281 |
9.33e-40 |
|
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: 144.38 E-value: 9.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 176 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 255
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1207141765 256 PEDVDVPHPDEKSIITYVSSMYDVMP 281
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
177-277 |
2.17e-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: 143.61 E-value: 2.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 256
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
|
90 100
....*....|....*....|.
gi 1207141765 257 EDVDVPHPDEKSIITYVSSMY 277
Cdd:cd21319 85 EDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
40-164 |
9.14e-39 |
|
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: 141.94 E-value: 9.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 40 ERDRVQKKTFTKWVNKHLVKHWKAEAqrhITDLYEDLRDGHNLISLLEVLSGETLPRERDVVRNsrlprekgrmRFHKLQ 119
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPIV---INDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQ----------RAHKLS 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1207141765 120 NVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 164
Cdd:cd21190 68 NIRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
39-160 |
1.24e-38 |
|
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: 142.47 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 39 DERDRVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlprEKGRMRFHKL 118
Cdd:cd21318 33 DEREAVQKKTFTKWVNSHL-----ARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKP-----------TRGRMRIHSL 96
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207141765 119 QNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 160
Cdd:cd21318 97 ENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
923-1000 |
2.35e-38 |
|
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: 139.28 E-value: 2.35e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 923 LSWQYLMRDITLINSWNFIMFKTLRVEEYRLTLKNLEQHYQAFLRDSQDSGLFGADDRMQAENSYNKATQHYDNLLRS 1000
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
176-277 |
3.92e-38 |
|
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: 140.00 E-value: 3.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 176 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 255
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1207141765 256 PEDVDVPHPDEKSIITYVSSMY 277
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
38-160 |
6.00e-38 |
|
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: 140.19 E-value: 6.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 38 KDERDRVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlprEKGRMRFHK 117
Cdd:cd21317 25 ADEREAVQKKTFTKWVNSHL-----ARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKP-----------TKGRMRIHC 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141765 118 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 160
Cdd:cd21317 89 LENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
173-277 |
8.18e-38 |
|
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: 139.42 E-value: 8.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 173 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTR 252
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1207141765 253 LLDPEDVDVPHPDEKSIITYVSSMY 277
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
180-281 |
9.15e-37 |
|
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: 135.63 E-value: 9.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 180 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 258
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1207141765 259 VDVPHPDEKSIITYVSSMYDVMP 281
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
40-164 |
1.99e-36 |
|
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: 134.96 E-value: 1.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 40 ERDRVQKKTFTKWVNKHLVKHWKAEAqrhITDLYEDLRDGHNLISLLEVLSGEtlprerdvvrnsRLPREKGRMRFHKLQ 119
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSV---VSDLFTDIQDGHRLLDLLEVLSGQ------------QLPREKGHNVFQCRS 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1207141765 120 NVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 164
Cdd:cd21242 66 NIETALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
161-277 |
5.91e-36 |
|
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: 134.41 E-value: 5.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 161 HFQISDIQVNGQSDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQA 240
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141765 241 FSIAERDLGVTRLLDPEDVDVPHPDEKSIITYVSSMY 277
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
177-277 |
4.19e-35 |
|
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: 131.37 E-value: 4.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 256
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1207141765 257 EDVDVPHPDEKSIITYVSSMY 277
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1806-2651 |
5.37e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 149.14 E-value: 5.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1806 QQKSKAEKETmsnTEKSKQLLESEAAKMRELAEEATKLRSV---AEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEA 1882
Cdd:PTZ00121 1083 AKEDNRADEA---TEEAFGKAEEAKKTETGKAEEARKAEEAkkkAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1883 TRLKTEAEIALKEKEAENDRLKRKAEEegyQRKVLEDQAAQHKQAIEE--------KIGQLKKSSDTELDRQKKIVEETL 1954
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEAarkaeeerKAEEARKAEDAKKAEAVKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1955 KQ----RKVVEEEIHILKLNFEKASSGKQELELELKKlkgiADETQKSKAkaeeeaekFRKLALEEEKKRKEAEAKVKQI 2030
Cdd:PTZ00121 1237 KDaeeaKKAEEERNNEEIRKFEEARMAHFARRQAAIK----AEEARKADE--------LKKAEEKKKADEAKKAEEKKKA 1304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2031 QAAEEEAARQHKAAQeevgrLMKLAEEAKKQKEIAEKEAEkqvilvqEAAQKCSAAEQKAQnvlvqqnkdsmaqdKLKEE 2110
Cdd:PTZ00121 1305 DEAKKKAEEAKKADE-----AKKKAEEAKKKADAAKKKAE-------EAKKAAEAAKAEAE--------------AAADE 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2111 FEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakaqedAEKLRKEAEKEasrraeaeaaalKLKQE 2190
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK------------------ADEAKKKAEED------------KKKAD 1408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2191 ADSEMAKYKKLAEKtLKQKSSVEEELVKVKVQLDETDKQKsvldvELKRLKQEVSDA--IKQKAQVEDELSKVKIQMEDL 2268
Cdd:PTZ00121 1409 ELKKAAAAKKKADE-AKKKAEEKKKADEAKKKAEEAKKAD-----EAKKKAEEAKKAeeAKKKAEEAKKADEAKKKAEEA 1482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2269 LKLklkiekenQELMKKDKDNTKKlleeeAENMKKLAEEAARlnieAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQ 2348
Cdd:PTZ00121 1483 KKA--------DEAKKKAEEAKKK-----ADEAKKAAEAKKK----ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2349 EAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQE--------TEGFQKSLEAERKRQLEITAEAEKLKVKVTQL 2420
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakkaeearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2421 SdaqsKAEEEAKK---FKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEkeklkkeAADL 2497
Cdd:PTZ00121 1626 K----KAEEEKKKveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA-------AEAL 1694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2498 QKQSKEMANVQQEQLQQEKTIlqqsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQ 2577
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEK------KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141765 2578 SAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAE---ENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEE 2651
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFAniiEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEE 1845
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
42-160 |
7.50e-35 |
|
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: 130.20 E-value: 7.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 42 DRVQKKTFTKWVNKHLVKhwkaeAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerdvvrnsrlPREKGRMRFHKLQNV 121
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRK-----AGTQIENIEEDFRDGLKLMLLLEVISGERLP-----------KPERGKMRFHKIANV 66
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141765 122 QIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 160
Cdd:cd21214 67 NKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1645-2437 |
1.68e-34 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 147.21 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1645 EEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQ- 1723
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEi 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1724 -KEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVldDELQRLKNDVNSAVKQKKELEEELIKVRKEME 1802
Cdd:PTZ00121 1157 aRKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKA--EAARKAEEERKAEEARKAEDAKKAEAVKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1803 ILLQQKSKAEKETMSNTEKSKQLLESEAAKM--RELAEEATKLRSvAEEAKKQRQIAEEEAARQRAEAEKI--LKEKLTA 1878
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFarRQAAIKAEEARK-ADELKKAEEKKKADEAKKAEEKKKAdeAKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1879 INEATRLKTEAEIALKEKEAendrLKRKAEEEGYQ---RKVLEDQAAQHKQAIEEKigqlKKSSDTELDRQKKIVEETLK 1955
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADA----AKKKAEEAKKAaeaAKAEAEAAADEAEAAEEK----AEAAEKKKEEAKKKADAAKK 1385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1956 QRKVVEEEIHILKlnfeKASSGKQElelelkklkgiADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEE 2035
Cdd:PTZ00121 1386 KAEEKKKADEAKK----KAEEDKKK-----------ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2036 EAARQHKAAQEevgrLMKLAEEAKKQKEIAEKEAEKQVilVQEAAQKCSAAEQKAQNVlvqqnKDSMAQDKLKEEFEKAK 2115
Cdd:PTZ00121 1451 KKAEEAKKAEE----AKKKAEEAKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADEA-----KKAAEAKKKADEAKKAE 1519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2116 KlAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEM 2195
Cdd:PTZ00121 1520 E-AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM 1598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2196 AKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVldvelKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKI 2275
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV-----EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2276 EKENQELMKKDKDNTKK--LLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAiQEAAKL 2353
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAaeALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA-EEAKKD 1752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2354 KAEAEKLQKQKDQAQVEAQKLLEAKKE-MQQRLDQETE---------------GFQKSLEAERKRQLEITAEAEKLKVKV 2417
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAvIEEELDEEDEkrrmevdkkikdifdNFANIIEGGKEGNLVINDSKEMEDSAI 1832
|
810 820
....*....|....*....|
gi 1207141765 2418 TQLSDAQSKAEEEAKKFKKQ 2437
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKH 1852
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
44-162 |
2.86e-34 |
|
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: 128.67 E-value: 2.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 44 VQKKTFTKWVNKHLVKhwkaeAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERdvvrnsrlprEKGRMRFHKLQNVQI 123
Cdd:cd21215 4 VQKKTFTKWLNTKLSS-----RGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYN----------KNPKMRVQKLENVNK 68
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141765 124 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 162
Cdd:cd21215 69 ALEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
164-277 |
1.96e-32 |
|
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: 123.79 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 164 ISDIQVNGqsddMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 243
Cdd:cd21291 1 IADINEEG----LTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141765 244 AERDLGVTRLLDPEDV-DVPHPDEKSIITYVSSMY 277
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYF 111
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
176-274 |
2.31e-32 |
|
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: 123.30 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 176 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 255
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1207141765 256 PEDVDVPHPDEKSIITYVS 274
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
39-164 |
3.54e-32 |
|
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: 123.11 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 39 DERDRVQKKTFTKWVNKHLVKHWKaeaqRHITDLYEDLRDGHNLISLLEVLSGEtlprerdvvrnsRLPREKGRMRFHKL 118
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGK----PPIEDLFTDLQDGRRLLELLEGLTGQ------------KLVKEKGSTRVHAL 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1207141765 119 QNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 164
Cdd:cd21231 65 NNVNKALQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
180-282 |
4.86e-32 |
|
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: 122.73 E-value: 4.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 180 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN-LENLEQAFSIAERDLGVTRLLDPE 257
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1207141765 258 DVDVPHPDEKSIITYVSSMYDVMPR 282
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
176-274 |
1.95e-31 |
|
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: 120.71 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 176 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 255
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1207141765 256 PEDVDVPHPDEKSIITYVS 274
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1385-2261 |
3.00e-31 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 136.42 E-value: 3.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1385 QDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQE 1464
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1465 LKTLSEQEIKAKSQQVEEAllsrtRIEEEIHiirlqlettmkqkntaetELLQLRaKAVDADKLRNAaqEEAEKLRKqvA 1544
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAA-----RKAEEVR------------------KAEELR-KAEDARKAEAA--RKAEEERK--A 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1545 EETqkkRKAEEELKRKSEAEkdaakekkkaledLEKFKLQAEEAERHLKQAELEKQRQIQ--VVEEVAKKTAATQLESKQ 1622
Cdd:PTZ00121 1215 EEA---RKAEDAKKAEAVKK-------------AEEAKKDAEEAKKAEEERNNEEIRKFEeaRMAHFARRQAAIKAEEAR 1278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1623 VALTAR-LEESLKNEQVMVIQLQEEAEHLKKQQAEADKArEQAEKELETWRQKANEALRlrlqAEEEANKKtaaqeeaek 1701
Cdd:PTZ00121 1279 KADELKkAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAAKK----KAEEAKKA--------- 1344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1702 qKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEEtAKQKLAAEQELIRLRADFEHAEQQRtvldDELQRLKNDVN 1781
Cdd:PTZ00121 1345 -AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA-AKKKAEEKKKADEAKKKAEEDKKKA----DELKKAAAAKK 1418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1782 SAVKQKKELEEelikVRKEMEIllqqKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKlrsvAEEAKKQRQIAEE-E 1860
Cdd:PTZ00121 1419 KADEAKKKAEE----KKKADEA----KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK----ADEAKKKAEEAKKaD 1486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1861 AARQRAEAEKILKEKLTAINEAtrlKTEAEIALKEKEAENDRLKRKAEEegyQRKVLEDQAAQHKQAIEE--KIGQLKKS 1938
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEA---KKKADEAKKAEEAKKADEAKKAEE---AKKADEAKKAEEKKKADElkKAEELKKA 1560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1939 SDTELDRQKKIVEETLKQ--------RKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKaeeeaekfR 2010
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMalrkaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE--------K 1632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2011 KLALEEEKKRKEAEAKVKQIQAAEEE----AARQHKAAQEEVGRL--MKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCS 2084
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEEnkikAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2085 AAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEkaKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAE 2164
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK--KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2165 KLRKEAEKEASRRAEAEAAAlklkQEADSEMAKYKKLAEKTlkQKSSVEEELVKVKVQLDETD---KQKSVLDVELKRLK 2241
Cdd:PTZ00121 1791 KRRMEVDKKIKDIFDNFANI----IEGGKEGNLVINDSKEM--EDSAIKEVADSKNMQLEEADafeKHKFNKNNENGEDG 1864
|
890 900
....*....|....*....|
gi 1207141765 2242 QEVSDAIKQKAQVEDELSKV 2261
Cdd:PTZ00121 1865 NKEADFNKEKDLKEDDEEEI 1884
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1354-1930 |
4.66e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 135.06 E-value: 4.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1354 QEYVTLRTRYSEL-MTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANE 1432
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1433 LKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKsQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAE 1512
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE-EELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1513 TELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRkseaekdaakekkkaledLEKFKLQAEEAERHL 1592
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER------------------LEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1593 KQAELEKQRQIQvvEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWR 1672
Cdd:COG1196 434 EEEEEEEEEALE--EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1673 QKANEALRLRL------QAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKM----AEETA 1742
Cdd:COG1196 512 AALLLAGLRGLagavavLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIraraALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1743 KQKLAAEQELIRLRADFEHAEQQRTVLDDEL---QRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsnT 1819
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLlgrTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS----R 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1820 EKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE 1899
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
570 580 590
....*....|....*....|....*....|.
gi 1207141765 1900 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE 1930
Cdd:COG1196 748 LEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
180-281 |
8.15e-31 |
|
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: 118.91 E-value: 8.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 180 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 258
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1207141765 259 VDVPHPDEKSIITYVSSMYDVMP 281
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
182-277 |
1.86e-30 |
|
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: 117.83 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 182 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED-VD 260
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1207141765 261 VPHPDEKSIITYVSSMY 277
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
39-160 |
2.28e-30 |
|
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: 119.38 E-value: 2.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 39 DERDRVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlprEKGRMRFHKL 118
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHL-----ARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKP-----------TKGRMRIHCL 111
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207141765 119 QNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 160
Cdd:cd21316 112 ENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1403-2605 |
3.02e-29 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 129.56 E-value: 3.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1403 AEMQAELEkqkqlAETHAKAIAKAEQEANEL-------KTKMKDEVSKRQDVAVDSEKQKhniQRELQELKTLSEQEIKA 1475
Cdd:NF041483 111 AEHQARLQ-----AELHTEAVQRRQQLDQELaerrqtvESHVNENVAWAEQLRARTESQA---RRLLDESRAEAEQALAA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1476 KSQQVEeallsrtRIEEEIHIiRLQLETtmkQKNTAETELLQLRAKAvDADKLRNAAQEEA-------EKLRKQVAEETQ 1548
Cdd:NF041483 183 ARAEAE-------RLAEEARQ-RLGSEA---ESARAEAEAILRRARK-DAERLLNAASTQAqeatdhaEQLRSSTAAESD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1549 KKRKAEEELKRKSEAekdaakekkkaledlekfklQAEEAERHLKQAELEKQRqiqVVEEvAKKTAATQLESKQVALTAR 1628
Cdd:NF041483 251 QARRQAAELSRAAEQ--------------------RMQEAEEALREARAEAEK---VVAE-AKEAAAKQLASAESANEQR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1629 LEESLKNEQVMVIQLQEEAEHLKkqqAEADKAREQAEKELETWRQKANEALRlRLQAEEEANKKTAAQEEAEKQKEEAKR 1708
Cdd:NF041483 307 TRTAKEEIARLVGEATKEAEALK---AEAEQALADARAEAEKLVAEAAEKAR-TVAAEDTAAQLAKAARTAEEVLTKASE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1709 EAKK--RAKAEEAALKQKEAaEMELGNQRKMAEETAKQ-KLAA--------------EQELIRLRADfehAEQQRTVLDD 1771
Cdd:NF041483 383 DAKAttRAAAEEAERIRREA-EAEADRLRGEAADQAEQlKGAAkddtkeyraktvelQEEARRLRGE---AEQLRAEAVA 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1772 ELQRLKNDV-NSAVKQKKE----LEEELIKVRKEMEILLQQ-KSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRS 1845
Cdd:NF041483 459 EGERIRGEArREAVQQIEEaartAEELLTKAKADADELRSTaTAESERVRTEAIERATTLRRQAEETLERTRAEAERLRA 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1846 VAEE-AKKQRQIAEEEAARQRAEAEK-ILKEKLTAINEATRLKTEAE-------IALKEKEAENDRLKRKAEEEGYQrkv 1916
Cdd:NF041483 539 EAEEqAEEVRAAAERAARELREETERaIAARQAEAAEELTRLHTEAEerltaaeEALADARAEAERIRREAAEETER--- 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1917 LEDQAAqhkqaieEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHIlKLNFEKASSGKQelelelkklkgIADETQ 1996
Cdd:NF041483 616 LRTEAA-------ERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAV-RLRSEAAAEAER-----------LKSEAQ 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1997 KSKAkaeeeaekfRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQE-----------EVGRLMKLAEE--AKKQKE 2063
Cdd:NF041483 677 ESAD---------RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEEtlgsaraeadqERERAREQSEEllASARKR 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2064 IAEKEAEKQViLVQEAAQKC----SAAEQKAQNVlvqqnKDSMA--QDKLKEEFekaKKLAQEAEKAKDNAEKEAAllhk 2137
Cdd:NF041483 748 VEEAQAEAQR-LVEEADRRAtelvSAAEQTAQQV-----RDSVAglQEQAEEEI---AGLRSAAEHAAERTRTEAQ---- 814
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2138 kaEEAERQKKaaeaeaakqakaqeDAEKLRKEAEKEASrraeaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELv 2217
Cdd:NF041483 815 --EEADRVRS--------------DAYAERERASEDAN----------RLRREAQEETEAAKALAERTVSEAIAEAERL- 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2218 kvkvQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVK----IQMEDLLKLKLKIEKENQELMKKDKDNTKKL 2293
Cdd:NF041483 868 ----RSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDE 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2294 LEEEAENMK-KLAEEAARLNIEAQ-EAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAklkAEAEKLqkqKDQAQVEA 2371
Cdd:NF041483 944 ARAEAERVRaDAAAQAEQLIAEATgEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAA---AEAERL---RTEAREEA 1017
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2372 QKLL-EAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTqlSDAQSKAEEEAKKFKKQADEIkirlqeTEK 2450
Cdd:NF041483 1018 DRTLdEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTT--TEAEAQADTMVGAARKEAERI------VAE 1089
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2451 HTSEKHTVVEK----------------------LEVQRLQSKQEADGLH-KAIADLEKEKEKLKKEAADLQKQSKEManv 2507
Cdd:NF041483 1090 ATVEGNSLVEKartdadellvgarrdatairerAEELRDRITGEIEELHeRARRESAEQMKSAGERCDALVKAAEEQ--- 1166
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2508 QQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKlqsAMDAAIKKQ 2587
Cdd:NF041483 1167 LAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKAELVREAEKIKAEAEAEAKRTVEEGKR---ELDVLVRRR 1243
|
1290
....*....|....*...
gi 1207141765 2588 KEAEEEMNGKQKEMQDLE 2605
Cdd:NF041483 1244 EDINAEISRVQDVLEALE 1261
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
40-166 |
4.90e-29 |
|
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: 114.21 E-value: 4.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 40 ERDRVQKKTFTKWVNKHLVKhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDVVRNsrlprekgrmRFHKLQ 119
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEK---CNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSH----------RIFRLN 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207141765 120 NVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 166
Cdd:cd21191 68 NIAKALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
43-165 |
1.02e-28 |
|
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: 113.70 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 43 RVQKKTFTKWVNKHLVKhwkaeAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERdvvrnsrlprEKGRMRFHKLQNVQ 122
Cdd:cd21311 14 RIQQNTFTRWANEHLKT-----ANKHIADLETDLSDGLRLIALVEVLSGKKFPKFN----------KRPTFRSQKLENVS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1207141765 123 IALDFLKHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 165
Cdd:cd21311 79 VALKFLEEDEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
44-164 |
1.60e-28 |
|
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: 112.41 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 44 VQKKTFTKWVNKHLVKHWKAEaqrhITDLYEDLRDGHNLISLLEVLSGETLPRERdvvrnsrlprekGRMRFHKLQNVQI 123
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKPP----IKDMFTDLRDGRKLLDLLEGLTGKSLPKER------------GSTRVHALNNVNR 65
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207141765 124 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 164
Cdd:cd21232 66 VLQVLHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
44-164 |
2.16e-28 |
|
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: 112.00 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 44 VQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRerdVVRNSRlprekgrMRFHKLQNVQI 123
Cdd:cd21227 4 IQKNTFTNWVNEQL-----KPTGMSVEDLATDLEDGVKLIALVEILQGRKLGR---VIKKPL-------NQHQKLENVTL 68
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207141765 124 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 164
Cdd:cd21227 69 ALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
180-279 |
1.03e-27 |
|
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: 110.07 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 180 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED- 258
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1207141765 259 VDVPHPDEKSIITYVSSMYDV 279
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1580-2172 |
1.04e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 124.28 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1580 KFKLQAEEAERHLKQA------------ELEKQR---QIQVveEVAKK--TAATQLESKQVALTA----RLEESLKNEQV 1638
Cdd:COG1196 169 KYKERKEEAERKLEATeenlerledilgELERQLeplERQA--EKAERyrELKEELKELEAELLLlklrELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1639 MVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEE 1718
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1719 AALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVR 1798
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1799 KEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTA 1878
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1879 INEATRLKTEAEiALKEKEAENDRLKRKAEEEGYQRK-----VLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEET 1953
Cdd:COG1196 487 AEAAARLLLLLE-AEADYEGFLEGVKAALLLAGLRGLagavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1954 LKQRKvvEEEIHILKLNFEKASSGKQELELELKKLKGIADEtqkskakaeEEAEKFRKLALEEEKKRKEAEAKVKQIQAA 2033
Cdd:COG1196 566 LKAAK--AGRATFLPLDKIRARAALAAALARGAIGAAVDLV---------ASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2034 EEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKcsAAEQKAQNVLVQQNKDSMAQDKLKEEFEK 2113
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE--LAERLAEEELELEEALLAEEEEERELAEA 712
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141765 2114 AKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEK 2172
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
162-277 |
3.50e-27 |
|
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: 109.40 E-value: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 162 FQISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAF 241
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141765 242 SIAERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 277
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFY 114
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
43-162 |
3.87e-27 |
|
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: 108.34 E-value: 3.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 43 RVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDvvrnsrlprEKGRMRFHKLQNVQ 122
Cdd:cd21183 3 RIQANTFTRWCNEHL-----KERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYN---------RRPAFQQHYLENVS 68
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1207141765 123 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 162
Cdd:cd21183 69 TALKFIEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1378-1997 |
7.56e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 122.17 E-value: 7.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1378 IETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHN 1457
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1458 IQRELQELKTLseQEIKAKSQQVEEALLSRTRIEEeihiirlqlettmkQKNTAEtellQLRAKAVDADKLRNAAQEEAE 1537
Cdd:PTZ00121 1294 EAKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEE--------------AKKKAD----AAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1538 KLRKQvAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAER---HLKQAELEKQRQIQVVEEVAKKTA 1614
Cdd:PTZ00121 1354 AAADE-AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkadELKKAAAAKKKADEAKKKAEEKKK 1432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1615 ATQLESKqvALTARLEESLKNEQvmviQLQEEAEHLKKQQAEADKAREQAEKELEtwRQKANEALRlrlqAEEEANKKTA 1694
Cdd:PTZ00121 1433 ADEAKKK--AEEAKKADEAKKKA----EEAKKAEEAKKKAEEAKKADEAKKKAEE--AKKADEAKK----KAEEAKKKAD 1500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1695 aqeeaekqkeeakrEAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRtvlddelq 1774
Cdd:PTZ00121 1501 --------------EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK-------- 1558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1775 rlKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQR 1854
Cdd:PTZ00121 1559 --KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1855 QIAEEEA--------ARQRAEAEKILKEKLTAINEATRLKTE-----------AEIALKEKEAEN---DRLKRKAEEEgy 1912
Cdd:PTZ00121 1637 QLKKKEAeekkkaeeLKKAEEENKIKAAEEAKKAEEDKKKAEeakkaeedekkAAEALKKEAEEAkkaEELKKKEAEE-- 1714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1913 QRKVLEDQAAQHKQAIeeKIGQLKKSSDTELDRQKKIVEETLKQRKV----VEEEIHILKLNFEKASSGKQELELELKKL 1988
Cdd:PTZ00121 1715 KKKAEELKKAEEENKI--KAEEAKKEAEEDKKKAEEAKKDEEEKKKIahlkKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792
|
....*....
gi 1207141765 1989 KGIADETQK 1997
Cdd:PTZ00121 1793 RMEVDKKIK 1801
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1407-1972 |
2.90e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 119.27 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1407 AELEKQ-KQLAEthaKAiAKAEQeANELKTKMKDevsKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEALL 1485
Cdd:COG1196 196 GELERQlEPLER---QA-EKAER-YRELKEELKE---LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1486 SRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEK 1565
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1566 DAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQvvEEVAKKTAATQLESKQVALTARLEESLKNEQvmviQLQE 1645
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE--ELLEALRAAAELAAQLEELEEAEEALLERLE----RLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1646 EAEHLKKQQAEADKAREQAEKELETwRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKE 1725
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEE-AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1726 AAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILL 1805
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1806 QQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEakkqRQIAEEEAARQRAEAEKILKEKLTAINEATRL 1885
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG----RTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1886 KTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIH 1965
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
....*..
gi 1207141765 1966 ILKLNFE 1972
Cdd:COG1196 737 LLEELLE 743
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1378-1962 |
2.97e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 120.25 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1378 IETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHN 1457
Cdd:PTZ00121 1130 AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAE 1209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1458 IQRELQELKTLSEQEIKAKSQQVEEALLSRT---RIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQ- 1533
Cdd:PTZ00121 1210 EERKAEEARKAEDAKKAEAVKKAEEAKKDAEeakKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEk 1289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1534 EEAEKLRK----QVAEETQKK----RKAEE------ELKRKSEAEKD----AAKEKKKALEDLEKFKLQAEEAERHLKQA 1595
Cdd:PTZ00121 1290 KKADEAKKaeekKKADEAKKKaeeaKKADEakkkaeEAKKKADAAKKkaeeAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1596 ELEKQRQIQVVEEVAKKT----AATQLESKQVALTARLEESLKNEQVmviqlQEEAEHLKKQQAE---ADKAREQAE--K 1666
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAeekkKADEAKKKAEEDKKKADELKKAAAA-----KKKADEAKKKAEEkkkADEAKKKAEeaK 1444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1667 ELETWRQKANEALR---LRLQAEE-----EANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMA 1738
Cdd:PTZ00121 1445 KADEAKKKAEEAKKaeeAKKKAEEakkadEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1739 EETAKQKLAAEQELIRLRADFEHAEQQRTVldDELQrlKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSN 1818
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKA--EELK--KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1819 TEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEA 1898
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 1899 ENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE----KIGQLKKSSDTELDRQKKIVEETLKQRKVVEE 1962
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAeekkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
164-277 |
9.27e-26 |
|
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: 105.17 E-value: 9.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 164 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 243
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141765 244 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 277
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFY 111
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
182-277 |
1.06e-25 |
|
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: 104.16 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 182 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED-VD 260
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1207141765 261 VPHPDEKSIITYVSSMY 277
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
164-277 |
2.60e-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: 104.04 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 164 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 243
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141765 244 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 277
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFY 111
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
28-164 |
8.51e-25 |
|
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: 102.53 E-value: 8.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 28 QGMLRAMDERkdeRDRVQKKTFTKWVNKHLVKHwkaEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlp 107
Cdd:cd21247 7 KGHIRKLQEQ---RMTMQKKTFTKWMNNVFSKN---GAKIEITDIYTELKDGIHLLRLLELISGEQLPRP---------- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 108 rEKGRMRFHKLQNVQIALDFLKHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 164
Cdd:cd21247 71 -SRGKMRVHFLENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1708-2394 |
1.81e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.49 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1708 REAKK----RAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSA 1783
Cdd:COG1196 207 RQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1784 VKQKKELEEELIKVRKEmEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAAR 1863
Cdd:COG1196 287 QAEEYELLAELARLEQD-IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1864 QRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEegyqrkvLEDQAAQHKQAIEEKIGQLKKSSDTEL 1943
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA-------LLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1944 DRQKKIVEETLKQRKVVEEEIHILKLnfekassgkqelelelkklkgIADETQKskakaeeeaekfRKLALEEEKKRKEA 2023
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLEL---------------------LAELLEE------------AALLEAALAELLEE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2024 EAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEkeaEKQVILVQEAAQKCSAAEQKAQNVLvqqnkdsma 2103
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV---LIGVEAAYEAALEAALAAALQNIVV--------- 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2104 qdklkeefEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAA 2183
Cdd:COG1196 554 --------EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2184 ALklkQEADSEMAKYkkLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKI 2263
Cdd:COG1196 626 TL---VAARLEAALR--RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2264 QMEDLLKLKLKIEKENQELmKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEK 2343
Cdd:COG1196 701 AEEEEERELAEAEEERLEE-ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141765 2344 K----QAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEA----KKEMQQRLdQET-----EGFQK 2394
Cdd:COG1196 780 GpvnlLAIEEYEELEERYDFLSEQREDLEEARETLEEAieeiDRETRERF-LETfdavnENFQE 842
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
178-277 |
1.85e-24 |
|
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: 100.71 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 178 AKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPE 257
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1207141765 258 D-VDVPHPDEKSIITYVSSMY 277
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1538-2442 |
2.83e-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: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1538 KLRKqvaEETQKK-RKAEEELKRkseaekdAAKEKKKALEDLEKFKLQAEEAERH--LKQAELEKQRQIQVVEEVAKKTA 1614
Cdd:TIGR02168 171 KERR---KETERKlERTRENLDR-------LEDILNELERQLKSLERQAEKAERYkeLKAELRELELALLVLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1615 ATQLESKQvaltARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEA-LRLRLQAEEEANkkt 1693
Cdd:TIGR02168 241 LEELQEEL----KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLAN--- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1694 aaqeeaekqkeeAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDEL 1773
Cdd:TIGR02168 314 ------------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1774 QRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEketmsnTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQ 1853
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ------QEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1854 RQIAEEEAARQRAEaekilkekltaINEATRLKTEAEIALKEKEAENDRLKRKAEE-EGYQRKVLedQAAQHKQAIEEKI 1932
Cdd:TIGR02168 456 LERLEEALEELREE-----------LEEAEQALDAAERELAQLQARLDSLERLQENlEGFSEGVK--ALLKNQSGLSGIL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1933 GQLKKSSDTELDRQKKIV---EETLKQRKVVEEEIHILKLNF-EKASSGKQELELELKKLkgiADETQKSKAKAEEEAEK 2008
Cdd:TIGR02168 523 GVLSELISVDEGYEAAIEaalGGRLQAVVVENLNAAKKAIAFlKQNELGRVTFLPLDSIK---GTEIQGNDREILKNIEG 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2009 FRKLALEEEKKRKEAEAK----------VKQIQAAEEEAARQH---------------------KAAQEEVGRLMKLAEE 2057
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRpgyrivtldgdlvrpggvitgGSAKTNSSILERRREI 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2058 AKKQKEIAekeaekqvilvqEAAQKCSAAEQKAQNVLVQqnkdsmaQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHK 2137
Cdd:TIGR02168 680 EELEEKIE------------ELEEKIAELEKALAELRKE-------LEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2138 KAEEAERqkkaaeaeaakqakAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELV 2217
Cdd:TIGR02168 741 EVEQLEE--------------RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2218 KVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekenqelmkkdkdntKKLLEEE 2297
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL----------------------AAEIEEL 864
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2298 AENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEA 2377
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141765 2378 KKEMQQRLDQETEGFQKSLEAERKrqlEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2442
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIEDDEE---EARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLT 1006
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
177-277 |
2.99e-24 |
|
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: 100.19 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 256
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1207141765 257 EDV---DVphPDEKSIITYVSSMY 277
Cdd:cd21198 80 ADMvllSV--PDKLSVMTYLHQIR 101
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
164-277 |
4.36e-24 |
|
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: 100.53 E-value: 4.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 164 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 243
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141765 244 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 277
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFY 111
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
43-162 |
5.19e-24 |
|
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: 99.48 E-value: 5.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 43 RVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDvvrnsrlprEKGRMRFHKLQNVQ 122
Cdd:cd21228 3 KIQQNTFTRWCNEHL-----KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYN---------KRPTFRQMKLENVS 68
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1207141765 123 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 162
Cdd:cd21228 69 VALEFLERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
822-888 |
6.28e-24 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 97.72 E-value: 6.28e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141765 822 QLKPRNpaQPIKGKLPVQAVCDFKQMEITVHKGDECALVNNSQPYKWKVRDSSGNEAVVPSICFIVP 888
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
176-282 |
6.85e-24 |
|
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: 99.28 E-value: 6.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 176 MTAKEKLLLWSQRMVEGY-QGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVY--RQTNLENLEQAFSIAERDLGVTR 252
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1207141765 253 -LLDPEDVDvpHPDEKSIITYVSSMYDVMPR 282
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1166-1891 |
7.52e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 112.16 E-value: 7.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1166 EASQTQLQKLRSEAEGKQATFD----RLEEELQRATEVNKRMSQLHSERDVELEHYRQlVGNLRERWQAVFAQ----IEL 1237
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKKaedaRKAEEARKAEDARKAEEARKAEDAKRVEIARK-AEDARKAEEARKAEdakkAEA 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1238 RQRELDLlnRQMQAYRESYDwlIRWIADAKQRQDKLHAVPIggSKGLQEQLTQEKKLLEEIEKNK------DKVEDCQKF 1311
Cdd:PTZ00121 1181 ARKAEEV--RKAEELRKAED--ARKAEAARKAEEERKAEEA--RKAEDAKKAEAVKKAEEAKKDAeeakkaEEERNNEEI 1254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1312 AKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMESASDDIIQeyvTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAA 1391
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK---AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1392 EKLKEEERKkmAEMQAELEKQKQLAETHAKAIAKAEQEANELKTkmkDEVSKRQDVAvdseKQKHNIQRELQELKTLSEq 1471
Cdd:PTZ00121 1332 DAAKKKAEE--AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK---EEAKKKADAA----KKKAEEKKKADEAKKKAE- 1401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1472 EIKAKSQQVEEALLSRTRIEEeihiirlqlettMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKR 1551
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADE------------AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1552 KAEEELKRKSEAEKDAAKEKKKAledlEKFKLQAEEAERhlKQAELEKQRQIQVVEEVAKKTAATQLESKQVAltarlEE 1631
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKA----EEAKKKADEAKK--AAEAKKKADEAKKAEEAKKADEAKKAEEAKKA-----DE 1538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1632 SLKNEQVMVIQLQEEAEHLKKqqAEADKAREQAEKELE---TWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKR 1708
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKK--AEEKKKAEEAKKAEEdknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1709 EAKKRA----KAEE-----AALKQKEAAEMELGNQRKMAEETAKQKlaAEQELIRLRADFEHAEQQRTVLDDELQRLKND 1779
Cdd:PTZ00121 1617 EAKIKAeelkKAEEekkkvEQLKKKEAEEKKKAEELKKAEEENKIK--AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1780 VNSAVKQKKelEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEE 1859
Cdd:PTZ00121 1695 KKEAEEAKK--AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
730 740 750
....*....|....*....|....*....|..
gi 1207141765 1860 eaarQRAEAEKILKEKLTAINEATRLKTEAEI 1891
Cdd:PTZ00121 1773 ----IRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
177-281 |
1.64e-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: 97.94 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGYqGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 256
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1207141765 257 EDVDVPHPDEKSIITYVSSMYDVMP 281
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
43-165 |
2.68e-23 |
|
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: 98.18 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 43 RVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDvvrnsrlPREKgrMRFHKLQNVQ 122
Cdd:cd21310 15 KIQQNTFTRWCNEHL-----KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYH-------PRPN--FRQMKLENVS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141765 123 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 165
Cdd:cd21310 81 VALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
180-280 |
7.23e-23 |
|
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: 96.00 E-value: 7.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 180 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPEDV 259
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1207141765 260 DVPHPDEKSIITYVSSMYDVM 280
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1827-2711 |
1.03e-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: 108.14 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1827 ESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRK 1906
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1907 AEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDtELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELK 1986
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE-KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1987 KLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAE 2066
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2067 KEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQE-AEKAKDNAEKEAALLHKKAEEAERQ 2145
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGkLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2146 kkaaeaeaakqakaqedaEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDE 2225
Cdd:pfam02463 471 ------------------EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2226 tDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLA 2305
Cdd:pfam02463 533 -DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2306 E-EAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQR 2384
Cdd:pfam02463 612 TlEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2385 LDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEKLEV 2464
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEE---EEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2465 QRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQ--EKTILQQSFFAEKETLLKKEKAIEEEKK 2542
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEeeQLLIEQEEKIKEEELEELALELKEEQKL 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2543 KLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQsamdaaiKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNL 2622
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQK-------LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEE 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2623 REKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMTMVETTKKVLNGSTEVDGvKKDVPLAFDGIREKVPASRLHEIGVLS 2702
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG-KVNLMAIEEFEEKEERYNKDELEKERL 1000
|
....*....
gi 1207141765 2703 KKEYDKLKK 2711
Cdd:pfam02463 1001 EEEKKKLIR 1009
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1658-2517 |
1.76e-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: 107.36 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1658 DKAREQAEKELetwRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKM 1737
Cdd:pfam02463 168 KRKKKEALKKL---IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1738 AEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNdvnsavKQKKELEEELIKVRKEMEILLQQKSKAEKETmS 1817
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE------EELKLLAKEEEELKSELLKLERRKVDDEEKL-K 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1818 NTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKE 1897
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1898 AENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSG 1977
Cdd:pfam02463 398 ELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1978 KQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGrlmKLAEE 2057
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV---IVEVS 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2058 AKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAAlLHK 2137
Cdd:pfam02463 555 ATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILK-DTE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2138 KAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELV 2217
Cdd:pfam02463 634 LTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELK 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2218 KVKVQLDETDKQKsvLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEE 2297
Cdd:pfam02463 714 KLKLEAEELLADR--VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2298 A-ENMKKLAEEAARLNIEAQEAA---RLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQK 2373
Cdd:pfam02463 792 KeEKLKAQEEELRALEEELKEEAellEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2374 LLEAKKEMQQrLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQE-TEKHT 2452
Cdd:pfam02463 872 LLLKEEELEE-QKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEaDEKEK 950
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141765 2453 SEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKT 2517
Cdd:pfam02463 951 EENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEET 1015
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1762-2625 |
2.55e-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: 106.59 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1762 AEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKS-----KAEKETMSNTEKSKQL--LESEAAKMR 1834
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQelklkEQAKKALEYYQLKEKLelEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1835 ELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKI-LKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQ 1913
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLaQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1914 RKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIAD 1993
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1994 ETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQV 2073
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2074 ILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEfEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEA 2153
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS-GLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2154 AKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKL-------AEKTLKQKSSVEEELVKVKVQLDET 2226
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLeidpilnLAQLDKATLEADEDDKRAKVVEGIL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2227 DKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEkenQELMKKDKDNTKKLLEEEAENMKKLAE 2306
Cdd:pfam02463 630 KDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ---ELQEKAESELAKEEILRRQLEIKKKEQ 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2307 EAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQ-KLLEAKKEMQQRL 2385
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKeKELAEEREKTEKL 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2386 DQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQ 2465
Cdd:pfam02463 787 KVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKE 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2466 RLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIlqqsffAEKETLLKKEKAIEEEKKKLE 2545
Cdd:pfam02463 867 ELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEI------EERIKEEAEILLKYEEEPEEL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2546 KQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDA-AIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLRE 2624
Cdd:pfam02463 941 LLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLmAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
.
gi 1207141765 2625 K 2625
Cdd:pfam02463 1021 E 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2100-2678 |
3.73e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 106.76 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2100 DSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAallhKKAEEAERQKKAAEAEAAKQAkaqedAEKLRK-E----AEKEA 2174
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEA----RKAEEAKKKAEDARKAEEARK-----AEDARKaEearkAEDAK 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2175 SRRAEAEAAALKLKQEA-DSEMAKYKKLAEKTLKQKSSVE----EELVKVKV--QLDETDKQKSVLDVELKRLKQEVSDA 2247
Cdd:PTZ00121 1153 RVEIARKAEDARKAEEArKAEDAKKAEAARKAEEVRKAEElrkaEDARKAEAarKAEEERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2248 --IKQKAQVEDELSKVKIQMEDLLKLKLKIEKEN--------QELMKKDK----DNTKKLLEEEAENMKKLAEEAARLNI 2313
Cdd:PTZ00121 1233 eeAKKDAEEAKKAEEERNNEEIRKFEEARMAHFArrqaaikaEEARKADElkkaEEKKKADEAKKAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2314 EAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQrLDQETEGFQ 2393
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA-AKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2394 KSLEAERKRQlEITAEAEKLKVKvtqlSDAQSKAEEEAKKF--KKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQ 2471
Cdd:PTZ00121 1392 KADEAKKKAE-EDKKKADELKKA----AAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2472 EadglHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQE--QLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFE 2549
Cdd:PTZ00121 1467 E----EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2550 DEVKKAEALKAEQERQRKlmeEERKKLQSAmdaaiKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLReklqql 2629
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKA---EEKKKAEEA-----KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK------ 1608
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1207141765 2630 qsSQKASYTKEIEIQTDKVPEEELVQMTMVETTKKVLNGSTEVDGVKKD 2678
Cdd:PTZ00121 1609 --AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1354-2144 |
3.73e-22 |
|
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: 106.29 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1354 QEYVTLRTRYSEL-MTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEkqkqlaeTHAKAIAKAEQEANE 1432
Cdd:TIGR02168 213 ERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE-------ELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1433 LKTKMKDEVSKRQDVavdsEKQKHNIQRELQELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAE 1512
Cdd:TIGR02168 286 LQKELYALANEISRL----EQQKQILRERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1513 TELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRkseaekdaakekkkaledlekfklqaeeAERHL 1592
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER----------------------------LEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1593 KQAELEKQRQIQVVEEVAKKTAATQLESKQVALtARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWR 1672
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAELKELQAEL-EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1673 QKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKR----------------------------EAKKRAKAEEAALKQK 1724
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVlselisvdegyeaaieaalggrlqavvvENLNAAKKAIAFLKQN 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1725 E---AAEMELGNQRKMAEETAKQKLAAEQELIRLRAD--FEHAEQQRTVLDDELQRLK--NDVNSAVKQKKELEEELIKV 1797
Cdd:TIGR02168 569 ElgrVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKdlVKFDPKLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1798 RKEMEILLQQKS---KAEKETMSNTEKSKQLLESEaAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKE 1874
Cdd:TIGR02168 649 TLDGDLVRPGGVitgGSAKTNSSILERRREIEELE-EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1875 KLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEdQAAQHKQAIEEKIGQLKKssdtELDRQKKIVEETL 1954
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEA----QIEQLKEELKALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1955 KQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKlaleeekkrkeaeaKVKQIQAAE 2034
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA--------------EIEELEELI 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2035 EEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEF-EK 2113
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEE 948
|
810 820 830
....*....|....*....|....*....|.
gi 1207141765 2114 AKKLAQEAEKAKDNAEKEAALLHKKAEEAER 2144
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
47-161 |
5.99e-22 |
|
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: 93.15 E-value: 5.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 47 KTFTKWVNKHLVKhwkaEAQRHITDLYEDLRDGHNLISLLEVLSgetlPRERDVVRNSRlprekGRMRFHKLQNVQIALD 126
Cdd:smart00033 1 KTLLRWVNSLLAE----YDKPPVTNFSSDLKDGVALCALLNSLS----PGLVDKKKVAA-----SLSRFKKIENINLALS 67
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141765 127 FLKHRQVKLVNIRNDDIADGnPKLTLGLIWTIILH 161
Cdd:smart00033 68 FAEKLGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
44-164 |
6.33e-22 |
|
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: 93.51 E-value: 6.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 44 VQKKTFTKWVNKHLVKhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerdvvrnsrlPREKGRMRFHKLQNVQI 123
Cdd:pfam00307 2 ELEKELLRWINSHLAE---YGPGVRVTNFTTDLRDGLALCALLNKLAPGLVD-----------KKKLNKSEFDKLENINL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207141765 124 ALDFLKHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 164
Cdd:pfam00307 68 ALDVAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
177-275 |
7.70e-22 |
|
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: 93.07 E-value: 7.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGYqglRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVY-RQTNLENLEQAFSIAERDLGVTRLLD 255
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1207141765 256 PEDVDVPHPDEKSIITYVSS 275
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1580-2470 |
1.38e-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: 104.37 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1580 KFKLQAEEAERHLKQAELEKQRQIQVVEEVAKktaatQLES--KQVALTARLEEslkneqvmviqLQEEAEHLKKQQAEA 1657
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELER-----QLKSleRQAEKAERYKE-----------LKAELRELELALLVL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1658 DKarEQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELgnqrkm 1737
Cdd:TIGR02168 233 RL--EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK------ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1738 aEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtms 1817
Cdd:TIGR02168 305 -QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ--- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1818 ntekskqlLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLK-TEAEIALKEK 1896
Cdd:TIGR02168 381 --------LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1897 EAENDRLKRKAEEegyqrkvLEDQAAQHKQAIEEKIGQLkkssdteldrqkkiveETLKQRKVVEEEihiLKLNFEKASS 1976
Cdd:TIGR02168 453 QEELERLEEALEE-------LREELEEAEQALDAAEREL----------------AQLQARLDSLER---LQENLEGFSE 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1977 GKQELELELKKLKGIADETQKSKAKAEEEaekfrKLALEEEKKRKEAEAKVKQIQAAEEEAARQhkaAQEEVGRLMKLAE 2056
Cdd:TIGR02168 507 GVKALLKNQSGLSGILGVLSELISVDEGY-----EAAIEAALGGRLQAVVVENLNAAKKAIAFL---KQNELGRVTFLPL 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2057 EAKKQKEIAEKEAE--KQVILVQEAAQKCSAAEQKAQ--------NVLVQQNKDSmAQDKLKEEFEKAKKLAQEAEK--- 2123
Cdd:TIGR02168 579 DSIKGTEIQGNDREilKNIEGFLGVAKDLVKFDPKLRkalsyllgGVLVVDDLDN-ALELAKKLRPGYRIVTLDGDLvrp 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2124 ----AKDNAEKEAALLHKKAEeaerqkkaaeaeaakqakaqedaeklRKEAEKeasrraeaeaaalKLKQEADSEMAKYK 2199
Cdd:TIGR02168 658 ggviTGGSAKTNSSILERRRE--------------------------IEELEE-------------KIEELEEKIAELEK 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2200 KLAEkTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQME------DLLKLKL 2273
Cdd:TIGR02168 699 ALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEeleerlEEAEEEL 777
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2274 KIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKL 2353
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2354 KAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ---ETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEE 2430
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALlrsELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 1207141765 2431 AKKFKKQ-ADEIKIRLQETEKHTSEKHTVVEKLE--VQRLQSK 2470
Cdd:TIGR02168 938 IDNLQERlSEEYSLTLEEAEALENKIEDDEEEARrrLKRLENK 980
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1421-2299 |
3.38e-21 |
|
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: 103.13 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1421 KAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEAllsrtRIEEEIHIIRLQ 1500
Cdd:pfam02463 200 LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEK-----EEEKLAQVLKEN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1501 LETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEEtQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEK 1580
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE-KEKKKAEKELKKEKEEIEELEKELKELEIKREA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1581 FKLQAEEAErhlKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKqqaEADKA 1660
Cdd:pfam02463 354 EEEEEEELE---KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLK---EEKKE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1661 REQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEE 1740
Cdd:pfam02463 428 ELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1741 TAKQKLAAEQELIRLRADFEHAEQQR---TVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILL-QQKSKAEKETM 1816
Cdd:pfam02463 508 GLKVLLALIKDGVGGRIISAHGRLGDlgvAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLgARKLRLLIPKL 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1817 SNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKlTAINEATRLKTEAEIALKEK 1896
Cdd:pfam02463 588 KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKES-GLRKGVSLEEGLAEKSEVKA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1897 EAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIgqlKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKass 1976
Cdd:pfam02463 667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIK---KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKL--- 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1977 gkqelelelkKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEvgrlmKLAE 2056
Cdd:pfam02463 741 ----------LKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEE-----ELRA 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2057 EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKA-KDNAEKEAALL 2135
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKEEELEEQKLK 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2136 HKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKssVEEE 2215
Cdd:pfam02463 886 DELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEE--ERNK 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2216 LVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLE 2295
Cdd:pfam02463 964 RLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELG 1043
|
....
gi 1207141765 2296 EEAE 2299
Cdd:pfam02463 1044 GSAE 1047
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
181-279 |
4.43e-21 |
|
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: 91.26 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 181 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD-PEDV 259
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1207141765 260 DVPHPDEKSIITYVSSMYDV 279
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYEL 107
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1354-2191 |
6.21e-21 |
|
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: 102.36 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1354 QEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANEL 1433
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1434 KTKMKDEVSK---RQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNT 1510
Cdd:pfam02463 246 LRDEQEEIESskqEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1511 AETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAER 1590
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1591 HlKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQ------LQEEAEHLKKQQAEADKAREQA 1664
Cdd:pfam02463 406 E-AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQelkllkDELELKKSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1665 EKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKR-AKAEEAALKQKEAAEMELGNQRKMAEETAK 1743
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDlGVAVENYKVAISTAVIVEVSATADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1744 QKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKND--VNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEK 1821
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDpiLNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1822 SKQLLESEAAkMRELAEEATKLRSVAEEAKKQRQIAEE-EAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEK-EAE 1899
Cdd:pfam02463 645 ESGLRKGVSL-EEGLAEKSEVKASLSELTKELLEIQELqEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAeELL 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1900 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQ---LKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASS 1976
Cdd:pfam02463 724 ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKkeeKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1977 GKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAE 2056
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2057 EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKaqNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLH 2136
Cdd:pfam02463 884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKE--NEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141765 2137 KKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEA 2191
Cdd:pfam02463 962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1578-2511 |
7.70e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 101.83 E-value: 7.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1578 LEKFKLQAEE----AERHLKQAELEKQRQIQvveEVAKKTAATQLESKQVALTARLE------------ESLKNEQVM-V 1640
Cdd:NF041483 78 LRNAQIQADQlradAERELRDARAQTQRILQ---EHAEHQARLQAELHTEAVQRRQQldqelaerrqtvESHVNENVAwA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1641 IQLQEEAEH-----LKKQQAEADK----AREQAEKELETWRQK-ANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREA 1710
Cdd:NF041483 155 EQLRARTESqarrlLDESRAEAEQalaaARAEAERLAEEARQRlGSEAESARAEAEAILRRARKDAERLLNAASTQAQEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1711 KKRAK------AEEAALKQKEAAEMELGNQRKMAE-ETAKQKLAAEQELIRLRAD---------FEHAEQQRT-VLDDEL 1773
Cdd:NF041483 235 TDHAEqlrsstAAESDQARRQAAELSRAAEQRMQEaEEALREARAEAEKVVAEAKeaaakqlasAESANEQRTrTAKEEI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1774 QRLkndVNSAVKQ----KKELEEELIKVRKEMEILLQQ-----KSKAEKETMSNTEKSKQLLESEAAKMRELAEEATklR 1844
Cdd:NF041483 315 ARL---VGEATKEaealKAEAEQALADARAEAEKLVAEaaekaRTVAAEDTAAQLAKAARTAEEVLTKASEDAKATT--R 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1845 SVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAI---------------NEATRLKTEAEIALKEKEAENDRLKRKAEE 1909
Cdd:NF041483 390 AAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvelqEEARRLRGEAEQLRAEAVAEGERIRGEARR 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1910 EGYQR---------------KVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQkkiVEETLkQRKVVEEEihilKLNFEKA 1974
Cdd:NF041483 470 EAVQQieeaartaeelltkaKADADELRSTATAESERVRTEAIERATTLRRQ---AEETL-ERTRAEAE----RLRAEAE 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1975 SSGKQELELELKKLKGIADETQKSKAKAEEEAEkfRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRL-MK 2053
Cdd:NF041483 542 EQAEEVRAAAERAARELREETERAIAARQAEAA--EELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLrTE 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2054 LAEEAKKQKEIAEKEAEKqviLVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ-DKLKEEF-EKAKKLAQEAEKAKDNAEKE 2131
Cdd:NF041483 620 AAERIRTLQAQAEQEAER---LRTEAAADASAARAEGENVAVRLRSEAAAEaERLKSEAqESADRVRAEAAAAAERVGTE 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2132 AA-LLHKKAEEAERQkkaaeaeaakqakaqedaeklRKEAEKEASRRaeaeaaalklKQEADSEMAKYKKLAEKTLKQ-K 2209
Cdd:NF041483 697 AAeALAAAQEEAARR---------------------RREAEETLGSA----------RAEADQERERAREQSEELLASaR 745
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2210 SSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQ-KAQVEDELS-----------KVKIQMEDLLKLKLKIEK 2277
Cdd:NF041483 746 KRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGlQEQAEEEIAglrsaaehaaeRTRTEAQEEADRVRSDAY 825
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2278 ENQELMKKDKDNTKKLLEEEAENMKKLAE--------EAARLNIEAQE-AARLRQIAESDLAKQRELAEKMLEEkkqAIQ 2348
Cdd:NF041483 826 AERERASEDANRLRREAQEETEAAKALAErtvseaiaEAERLRSDASEyAQRVRTEASDTLASAEQDAARTRAD---ARE 902
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2349 EAAKLKAE-AEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLE-----ITAEAEKLKVKVTQ-LS 2421
Cdd:NF041483 903 DANRIRSDaAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEqliaeATGEAERLRAEAAEtVG 982
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2422 DAQSKAE---EEAKKFKKQADEikirlqETEKHTSEKHTVVEKL--EVQRLQSKQEADGLHKAIADLEKEKEKLKKEAAD 2496
Cdd:NF041483 983 SAQQHAErirTEAERVKAEAAA------EAERLRTEAREEADRTldEARKDANKRRSEAAEQADTLITEAAAEADQLTAK 1056
|
1050
....*....|....*
gi 1207141765 2497 LQKQSKEMANVQQEQ 2511
Cdd:NF041483 1057 AQEEALRTTTEAEAQ 1071
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1379-2461 |
8.81e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 101.83 E-value: 8.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1379 ETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLA-ETHAKAIAKAEQeANELKTKMKdevskrqdvavdsekqKHN 1457
Cdd:NF041483 251 QARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAkEAAAKQLASAES-ANEQRTRTA----------------KEE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1458 IQRELQELKTLSEQeIKAKSQQVeealLSRTRIEEEihiiRLQLETTMKQKN-TAETELLQLRAKAVDADKLRNAAQEEA 1536
Cdd:NF041483 314 IARLVGEATKEAEA-LKAEAEQA----LADARAEAE----KLVAEAAEKARTvAAEDTAAQLAKAARTAEEVLTKASEDA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1537 EKLRKQVAEETQK-KRKAEEELKRKSEAEKDAAKEKKKALEDLEKfklqaeeaERHLKQAEL-EKQRQIqvveevakKTA 1614
Cdd:NF041483 385 KATTRAAAEEAERiRREAEAEADRLRGEAADQAEQLKGAAKDDTK--------EYRAKTVELqEEARRL--------RGE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1615 ATQLESKQVALTARLEESLKNEQVMviQLQEEA----EHLKKQQAEADKAREQAEKELETWRQKANE-ALRLRLQAEEEA 1689
Cdd:NF041483 449 AEQLRAEAVAEGERIRGEARREAVQ--QIEEAArtaeELLTKAKADADELRSTATAESERVRTEAIErATTLRRQAEETL 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1690 NkktaaqeeaekqkeeakreaKKRAKAEEaalkqkeaaemelgnQRKMAEETA-KQKLAAEQELIRLRADFEHA-EQQRT 1767
Cdd:NF041483 527 E--------------------RTRAEAER---------------LRAEAEEQAeEVRAAAERAARELREETERAiAARQA 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1768 VLDDELQRLKNDVNSAVKQKkelEEELIKVRKEMEILlqqkskaEKETMSNTEKskqlLESEAA-KMRELAEEATklrsv 1846
Cdd:NF041483 572 EAAEELTRLHTEAEERLTAA---EEALADARAEAERI-------RREAAEETER----LRTEAAeRIRTLQAQAE----- 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1847 aEEAKKQRQIAEEEAARQRAEAEkilkekltaiNEATRLKTEAeialkekEAENDRLKRKAEEEGyQRKVLEDQAAQHKQ 1926
Cdd:NF041483 633 -QEAERLRTEAAADASAARAEGE----------NVAVRLRSEA-------AAEAERLKSEAQESA-DRVRAEAAAAAERV 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1927 AIEEkiGQLKKSSDTELDRQKKIVEETLkqrkvveeeihilklnfekassgkqelelelkklkgiadetqkskakaeeea 2006
Cdd:NF041483 694 GTEA--AEALAAAQEEAARRRREAEETL---------------------------------------------------- 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2007 ekfrklaleeekkrkeaeakvkqiQAAEEEAARQHKAAQEEVGRLMklaeeAKKQKEIAEKEAEKQViLVQEAAQKC--- 2083
Cdd:NF041483 720 ------------------------GSARAEADQERERAREQSEELL-----ASARKRVEEAQAEAQR-LVEEADRRAtel 769
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2084 -SAAEQKAQNVlvqqnKDSMA--QDKLKEEFekaKKLAQEAEKAKDNAEKEAallhkkAEEAERqkkaaeaeaakqakAQ 2160
Cdd:NF041483 770 vSAAEQTAQQV-----RDSVAglQEQAEEEI---AGLRSAAEHAAERTRTEA------QEEADR--------------VR 821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2161 EDAEKLRKEAEKEASrraeaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELvkvkvQLDETDKQKSVLDVELKRL 2240
Cdd:NF041483 822 SDAYAERERASEDAN----------RLRREAQEETEAAKALAERTVSEAIAEAERL-----RSDASEYAQRVRTEASDTL 886
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2241 KQEVSDAIKQKAQVEDELSKVK----IQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMK-KLAEEAARLNIEA 2315
Cdd:NF041483 887 ASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRaDAAAQAEQLIAEA 966
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2316 Q-EAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAklkAEAEKLqkqKDQAQVEAQKLL-EAKKEMQQRLDQETEGFQ 2393
Cdd:NF041483 967 TgEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAA---AEAERL---RTEAREEADRTLdEARKDANKRRSEAAEQAD 1040
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 2394 KSLEAERKRQLEITAEAEKLKVKVTqlSDAQSKAEEEAKKFKKQADEIkirlqeTEKHTSEKHTVVEK 2461
Cdd:NF041483 1041 TLITEAAAEADQLTAKAQEEALRTT--TEAEAQADTMVGAARKEAERI------VAEATVEGNSLVEK 1100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1176-1889 |
2.15e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.40 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1176 RSEAEGK-QATFDRLEEELQRATEVNKRMSQLHSERDVeLEHYRQLVGNLRERwqavfaQIELRQRELDLLNRQMQAyre 1254
Cdd:COG1196 174 KEEAERKlEATEENLERLEDILGELERQLEPLERQAEK-AERYRELKEELKEL------EAELLLLKLRELEAELEE--- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1255 sydwlirwiadakqrqdklhavpiggskgLQEQLTQEKKLLEEIEKNKDKVEDcqkfakgyidaikdyelqlvtykalve 1334
Cdd:COG1196 244 -----------------------------LEAELEELEAELEELEAELAELEA--------------------------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1335 piasplKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEErkkmAEMQAELEKQKQ 1414
Cdd:COG1196 268 ------ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL----AELEEELEELEE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1415 LAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEI 1494
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLERL 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1495 HIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKA 1574
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1575 LEDLEKFKLQAEEA-ERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKneqvmviQLQEEAEHLKKQ 1653
Cdd:COG1196 497 LEAEADYEGFLEGVkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE-------VAAAAIEYLKAA 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1654 QA--------EADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKE 1725
Cdd:COG1196 570 KAgratflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1726 AAEMELGNQRKMAEETAKQKLAAEQELIRLRAdfEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILL 1805
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL--EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1806 QQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQI-------AEEEAARQRAEAEKILKEK--- 1875
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQRedl 807
|
730 740
....*....|....*....|.
gi 1207141765 1876 -------LTAINEATRLKTEA 1889
Cdd:COG1196 808 eearetlEEAIEEIDRETRER 828
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
177-274 |
6.03e-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: 87.92 E-value: 6.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 256
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90
....*....|....*....
gi 1207141765 257 ED-VDVPHPDEKSIITYVS 274
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLC 98
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2105-2653 |
1.10e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.09 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2105 DKLKEEFEKAKK---LAQEAEKAK--------DNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKE 2173
Cdd:COG1196 203 EPLERQAEKAERyreLKEELKELEaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2174 ASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQ 2253
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2254 VEDELSKVKIQMEDLLKLKLKIEKENQELMkKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQR 2333
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEAL-RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2334 ELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDqetegfqksLEAERKRQLEITAEAEKL 2413
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL---------LLLEAEADYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2414 KVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEAdglhKAIADLEKEKEKLKKE 2493
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG----RATFLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2494 AADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEER 2573
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2574 KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEEL 2653
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
177-277 |
2.59e-19 |
|
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: 85.86 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 256
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1207141765 257 EDVDV--PHPDEKSIITYVSSMY 277
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1161-1975 |
2.63e-19 |
|
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: 96.96 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1161 NEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQavfAQIELRQR 1240
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ---ELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1241 ELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIK 1320
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1321 dyELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQ-----DEEKAAEKLK 1395
Cdd:pfam02463 332 --KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEeelelKSEEEKEAQL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1396 EEERKKMAEMQAELEKQKQLAETHA--KAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEI 1473
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEEeeESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1474 KAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKA 1553
Cdd:pfam02463 490 LSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRA 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1554 EEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESL 1633
Cdd:pfam02463 570 LTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLR 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1634 KNEQVMV---------IQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKktaaqEEAEKQKE 1704
Cdd:pfam02463 650 KGVSLEEglaeksevkASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLK-----LEAEELLA 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1705 EAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAV 1784
Cdd:pfam02463 725 DRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELR 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1785 KQKKELEEELIKVRKEMEILLQQKSKAEKETMSN-------------TEKSKQLLESEAAKMRELAEEATKLRSVAEEAK 1851
Cdd:pfam02463 805 ALEEELKEEAELLEEEQLLIEQEEKIKEEELEELalelkeeqkleklAEEELERLEEEITKEELLQELLLKEEELEEQKL 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1852 KQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRkaEEEGYQRKVLEDQAAQHKQAIEEK 1931
Cdd:pfam02463 885 KDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE--ELLLEEADEKEKEENNKEEEEERN 962
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1207141765 1932 IGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKAS 1975
Cdd:pfam02463 963 KRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKK 1006
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1379-2266 |
2.72e-19 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 96.82 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1379 ETQRRLQDEEKAAEKLKEEERKKMAEMQAELEK---------QKQLAETHAKAIAKAEQEANELKTKMKDEVSK------ 1443
Cdd:NF041483 313 EIARLVGEATKEAEALKAEAEQALADARAEAEKlvaeaaekaRTVAAEDTAAQLAKAARTAEEVLTKASEDAKAttraaa 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1444 ------RQDVAVDSEK---QKHNIQRELQELKTLSEQEIKAKSQQV-EEALLSRTRIEE-------EIHIIRLQLETTMK 1506
Cdd:NF041483 393 eeaeriRREAEAEADRlrgEAADQAEQLKGAAKDDTKEYRAKTVELqEEARRLRGEAEQlraeavaEGERIRGEARREAV 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1507 QK-----NTAEtELLQlRAKAvDADKLRNAAQEEAEKLRKQVAEE-TQKKRKAEEELKRKSEAEKDAAKEKKKALedlEK 1580
Cdd:NF041483 473 QQieeaaRTAE-ELLT-KAKA-DADELRSTATAESERVRTEAIERaTTLRRQAEETLERTRAEAERLRAEAEEQA---EE 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1581 FKLQAEEAERHLKQaELEK---QRQIQVVEEVAKK--TAATQLESKQVALT-ARLE-ESLKNEQVmviqlqEEAEHLKKQ 1653
Cdd:NF041483 547 VRAAAERAARELRE-ETERaiaARQAEAAEELTRLhtEAEERLTAAEEALAdARAEaERIRREAA------EETERLRTE 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1654 QAEADKA-REQAEKELETWRQKA------------NEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKR------- 1713
Cdd:NF041483 620 AAERIRTlQAQAEQEAERLRTEAaadasaaraegeNVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERvgteaae 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1714 --AKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELI---RLRADFEHAEQQRTVldDELQRLKNDVNSAVKQ-- 1786
Cdd:NF041483 700 alAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasaRKRVEEAQAEAQRLV--EEADRRATELVSAAEQta 777
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1787 ----------KKELEEELIKVRKEMEillqqksKAEKETMSNTEKSKQLLESEAAKMRELA-EEATKLRSVA-EEAKKQR 1854
Cdd:NF041483 778 qqvrdsvaglQEQAEEEIAGLRSAAE-------HAAERTRTEAQEEADRVRSDAYAERERAsEDANRLRREAqEETEAAK 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1855 QIAEEEAARQRAEAEKILKEkltAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGyqRKVLEDQAAQHKQAIEEKIGQ 1934
Cdd:NF041483 851 ALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADAREDA--NRIRSDAAAQADRLIGEATSE 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1935 LKKSSDTELDRQKKIVEETLKQRKvveeeihilKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLAl 2014
Cdd:NF041483 926 AERLTAEARAEAERLRDEARAEAE---------RVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEA- 995
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2015 eeekkrkeaeakvKQIQA-AEEEAARQHKAAQEEVGRLMKLAEE--AKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQ 2091
Cdd:NF041483 996 -------------ERVKAeAAAEAERLRTEAREEADRTLDEARKdaNKRRSEAAEQADTLITEAAAEADQLTAKAQEEAL 1062
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2092 NVLV--QQNKDSMAQDKLKEefekAKKLAQEA--------EKAKDNAE-------KEAALLHKKAEEAeRQKKAAEAEAA 2154
Cdd:NF041483 1063 RTTTeaEAQADTMVGAARKE----AERIVAEAtvegnslvEKARTDADellvgarRDATAIRERAEEL-RDRITGEIEEL 1137
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2155 KQAKAQEDAEKLRKEAEK-------EASRRAEAEAAALKLKQEADSEMAKYK----KLAEKTLKQKSSVEEELVKvkvql 2223
Cdd:NF041483 1138 HERARRESAEQMKSAGERcdalvkaAEEQLAEAEAKAKELVSDANSEASKVRiaavKKAEGLLKEAEQKKAELVR----- 1212
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*..
gi 1207141765 2224 dETDKQKSVLDVELKRL----KQEVSDAIKQKAQVEDELSKVKIQME 2266
Cdd:NF041483 1213 -EAEKIKAEAEAEAKRTveegKRELDVLVRRREDINAEISRVQDVLE 1258
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
43-165 |
3.22e-19 |
|
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: 86.67 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 43 RVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERdvvrnsrlpREKGRMRFHKLQNVQ 122
Cdd:cd21309 16 KIQQNTFTRWCNEHL-----KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKY---------HQRPTFRQMQLENVS 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141765 123 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 165
Cdd:cd21309 82 VALEFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
43-165 |
3.47e-19 |
|
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: 86.68 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 43 RVQKKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDvvrnsrlprEKGRMRFHKLQNVQ 122
Cdd:cd21308 19 KIQQNTFTRWCNEHL-----KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHN---------QRPTFRQMQLENVS 84
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141765 123 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 165
Cdd:cd21308 85 VALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
177-273 |
4.00e-19 |
|
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: 85.67 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 256
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90
....*....|....*...
gi 1207141765 257 ED-VDVPHPDEKSIITYV 273
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYL 97
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
173-280 |
5.01e-19 |
|
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: 85.38 E-value: 5.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 173 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTR 252
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*....
gi 1207141765 253 LLDPEDV-DVPHPDEKSIITYVSSMYDVM 280
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYEMF 109
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
180-276 |
5.62e-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: 5.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 180 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN----LENLEQAFSIAERDLGVTRLLD 255
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1207141765 256 PEDVDVPHPDEKSIITYVSSM 276
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1162-1807 |
2.16e-18 |
|
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: 93.97 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1162 EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRE 1241
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1242 LDLLNRQMQAYRE----SYDWLIRWIADAKQRQDKLHAVPIggsKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGYID 1317
Cdd:TIGR02168 395 IASLNNEIERLEArlerLEDRRERLQQEIEELLKKLEEAEL---KELQAELEELEEELEELQEELERLEEALEELREELE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1318 ----AIKDYELQLVTYKALV--------------EPIASPLKKAKMESASDDIIQEYVTLRTRYS------------ELM 1367
Cdd:TIGR02168 472 eaeqALDAAERELAQLQARLdslerlqenlegfsEGVKALLKNQSGLSGILGVLSELISVDEGYEaaieaalggrlqAVV 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1368 TLSSQYIKFIIETQRRlQDEEKAA-----EKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAE--------------- 1427
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQ-NELGRVTflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvdd 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1428 -QEANELKTKMK----------DEVSKRQDVAVDSEKQKHNIQ------RELQELKTLSEQEIKAKSQQVEEALLSRTRI 1490
Cdd:TIGR02168 631 lDNALELAKKLRpgyrivtldgDLVRPGGVITGGSAKTNSSILerrreiEELEEKIEELEEKIAELEKALAELRKELEEL 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1491 EEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKE 1570
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1571 KKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALT--------ARLEESLKNEQVMVIQ 1642
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieelsediESLAAEIEELEELIEE 870
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1643 LQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTaaqeeaekQKEEAKREAKKRAKAEEAALK 1722
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR--------EKLAQLELRLEGLEVRIDNLQ 942
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1723 QK--EAAEMELGNQRKMAEETAKQKLAAEQELIRLR--------------ADFEHAEQQRtvldDELQRLKNDVNSAVKQ 1786
Cdd:TIGR02168 943 ERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLEnkikelgpvnlaaiEEYEELKERY----DFLTAQKEDLTEAKET 1018
|
730 740
....*....|....*....|.
gi 1207141765 1787 kkeLEEELIKVRKEMEILLQQ 1807
Cdd:TIGR02168 1019 ---LEEAIEEIDREARERFKD 1036
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1543-2417 |
3.01e-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: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1543 VAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLK-QAELEKQRQIQVVEEvaKKTAATQLESK 1621
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQAlLKEKREYEGYELLKE--KEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1622 QVALtARLEESLKneqvmviQLQEEAEHLKKQQAEADKAREQAEKELEtwRQKANEALRLRLQAEEEANKKTAAQEEAEK 1701
Cdd:TIGR02169 243 ERQL-ASLEEELE-------KLTEEISELEKRLEEIEQLLEELNKKIK--DLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1702 QKEEAKREAKKRAKAEEAALKQKEAAEmelgNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVN 1781
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIE----ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1782 SAVKQKKELEEELIKVRKEMEILLQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEATklrSVAEEAKKQRQIAEEEA 1861
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEEL----ADLNAAIAGIEAKINELEEEKE---DKALEIKKQEWKLEQLA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1862 ArQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQ--------------AAQHKQA 1927
Cdd:TIGR02169 462 A-DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiqgvhgtvaqlgsvGERYATA 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1928 IEEKIGQLKKS--SDTELDRQKKIveETLKQRKVveEEIHILKLNfEKASSGKQELELELKKLKGIA-------DETQKS 1998
Cdd:TIGR02169 541 IEVAAGNRLNNvvVEDDAVAKEAI--ELLKRRKA--GRATFLPLN-KMRDERRDLSILSEDGVIGFAvdlvefdPKYEPA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1999 KAKAEEEAEKFRKLALEEEKKRK-----------EAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEK 2067
Cdd:TIGR02169 616 FKYVFGDTLVVEDIEAARRLMGKyrmvtlegelfEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQS 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2068 EAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkk 2147
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE--- 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2148 aaeaeaakqakaqeDAEKLRKEAEKEASRraeaeaaalklkqEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETD 2227
Cdd:TIGR02169 773 --------------DLHKLEEALNDLEAR-------------LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2228 KQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAEnMKKLAEE 2307
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ-LRELERK 904
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2308 AARLNIEAQEA-ARLRQIAESDLAKQRELAEkmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL-------LEAKK 2379
Cdd:TIGR02169 905 IEELEAQIEKKrKRLSELKAKLEALEEELSE--IEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALepvnmlaIQEYE 982
|
890 900 910
....*....|....*....|....*....|....*...
gi 1207141765 2380 EMQQRLDqETEGFQKSLEAERKRQLEITAEAEKLKVKV 2417
Cdd:TIGR02169 983 EVLKRLD-ELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
45-162 |
3.88e-17 |
|
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: 79.55 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 45 QKKTFTKWVNKHLVKHwkaEAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerDVVRNsrlPRekgrMRFHKLQNVQIA 124
Cdd:cd21212 1 EIEIYTDWANHYLEKG---GHKRIITDLQKDLGDGLTLVNLIEAVAGEKVP---GIHSR---PK----TRAQKLENIQAC 67
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141765 125 LDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 162
Cdd:cd21212 68 LQFLAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
181-279 |
4.12e-17 |
|
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: 79.92 E-value: 4.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 181 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD-PEDV 259
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1207141765 260 DVPHPDEKSIITYVSSMYDV 279
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYEL 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1819-2482 |
5.01e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1819 TEKSKQL--LESEAAKmrelAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLtainEATRLKTEAEIALKEK 1896
Cdd:COG1196 196 GELERQLepLERQAEK----AERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL----EAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1897 EAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKigqlkkssdtELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASS 1976
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQ----------DIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1977 GKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAE 2056
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2057 EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLH 2136
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2137 KKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEEL 2216
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2217 vkvkvQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVkIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEE 2296
Cdd:COG1196 578 -----PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV-LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2297 EAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLE 2376
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2377 AKKEMQQRLDQETEGFqksLEAERKRQLEITAEAEKLKVKVTQLSDAQSK-------AEEEAkkfkkqaDEIKIRLQEte 2449
Cdd:COG1196 732 AEREELLEELLEEEEL---LEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEY-------EELEERYDF-- 799
|
650 660 670
....*....|....*....|....*....|...
gi 1207141765 2450 khtsekhtvvekLEVQRLQSKQEADGLHKAIAD 2482
Cdd:COG1196 800 ------------LSEQREDLEEARETLEEAIEE 820
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1708-2628 |
6.01e-17 |
|
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: 88.96 E-value: 6.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1708 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKlaaeQELIRLRADFEHAE-----QQRTVLDDELQRLKNDVNS 1782
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKA----ERYKELKAELRELElallvLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1783 AVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsntekskqlLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAA 1862
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1863 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEgyqrkvleDQAAQHKQAIEEKIGQLKKssdtE 1942
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL--------EELESRLEELEEQLETLRS----K 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1943 LDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELElelkklkgiadetqkskakaeeeaekfRKLALEEEKKRKE 2022
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL---------------------------KKLEEAELKELQA 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2023 AEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSM 2102
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2103 AQDKLKEEFEKAKKLAQEAEKA-----------KDNAEKEAALLHKKAEE-----------AERQKKAAEAEAAKQAKAQ 2160
Cdd:TIGR02168 521 ILGVLSELISVDEGYEAAIEAAlggrlqavvveNLNAAKKAIAFLKQNELgrvtflpldsiKGTEIQGNDREILKNIEGF 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2161 EDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKqkSSVEEELVKVK-VQLDETDKQKSVL---DVE 2236
Cdd:TIGR02168 601 LGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRI--VTLDGDLVRPGgVITGGSAKTNSSIlerRRE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2237 LKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQElMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQ 2316
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-LSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2317 EAARLRQIAESDLAKQRElaekmleEKKQAIQEAAKLKAEAEKLQKQKDQ---AQVEAQKLLEAKKEMQQRLDQETEGFQ 2393
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEE-------ELAEAEAEIEELEAQIEQLKEELKAlreALDELRAELTLLNEEAANLRERLESLE 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2394 KSLEAERKRQLEITAEAEKLKVKVTQLSDAQS-------KAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQR 2466
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEeleelieELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2467 LQSKQEADGLHKAIADlekekeklkkeaadlqkqskemANVQQEQLQQEKTILQQSFFAEKETLLKKekaieeekkklek 2546
Cdd:TIGR02168 911 SELRRELEELREKLAQ----------------------LELRLEGLEVRIDNLQERLSEEYSLTLEE------------- 955
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2547 qFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKL 2626
Cdd:TIGR02168 956 -AEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERF 1034
|
..
gi 1207141765 2627 QQ 2628
Cdd:TIGR02168 1035 KD 1036
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1382-2130 |
7.67e-17 |
|
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: 88.58 E-value: 7.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1382 RRLQDEEKAAE-----KLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKdEVSKRQDVavdsekqkh 1456
Cdd:TIGR02168 216 KELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS-ELEEEIEE--------- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1457 nIQRELQELKtlseQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEA 1536
Cdd:TIGR02168 286 -LQKELYALA----NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1537 EKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKekkkaleDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAT 1616
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLEL-------QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1617 QLESKQVALtARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQ 1696
Cdd:TIGR02168 434 ELKELQAEL-EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1697 EEAEKQKEEAKR----------------------------EAKKRAKAEEAALKQKE---AAEMELGNQRKMAEETAKQK 1745
Cdd:TIGR02168 513 KNQSGLSGILGVlselisvdegyeaaieaalggrlqavvvENLNAAKKAIAFLKQNElgrVTFLPLDSIKGTEIQGNDRE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1746 LAAEQELIRLRADF--EHAEQQRTVLDDELQRLK--NDVNSAVKQKKELEEE---------------------------L 1794
Cdd:TIGR02168 593 ILKNIEGFLGVAKDlvKFDPKLRKALSYLLGGVLvvDDLDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssI 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1795 IKVRKEMEILLQQKSKAEketmSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKE 1874
Cdd:TIGR02168 673 LERRREIEELEEKIEELE----EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1875 KLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE----------------KIGQLKKS 1938
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldelraeltllneeaaNLRERLES 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1939 SDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEK 2018
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2019 KRKEAEAKVKQIQAAEEEA-ARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNvLVQQ 2097
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLeLRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE-LGPV 987
|
810 820 830
....*....|....*....|....*....|....
gi 1207141765 2098 NKDSMAQ-DKLKEEFEKAKKLAQEAEKAKDNAEK 2130
Cdd:TIGR02168 988 NLAAIEEyEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1147-1962 |
8.85e-17 |
|
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: 88.58 E-value: 8.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1147 KYENQLREVnKVPVNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRE 1226
Cdd:TIGR02168 217 ELKAELREL-ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1227 RWQAVFAQIELRQRELDLLNRQMQAYRESydwlirwIADAKQRQDKLhavpiggskglQEQLTQEKKLLEEIEKNkdkVE 1306
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQ-------LEELESKLDEL-----------AEELAELEEKLEELKEE---LE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1307 DCQKFAKGYIDAIKDYELQLVTykalvepiasplKKAKMESASDDIIQEYVTLRTRYSELMTLSSQyIKFIIETQRRLQD 1386
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEE------------LEEQLETLRSKVAQLELQIASLNNEIERLEAR-LERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1387 EEKAAEKLKEEERkkMAEMQAELEKQKQLAETHAKAIAKAEQEANELKtkmkDEVSKRQDVAVDSEKQKHNIQRELQELK 1466
Cdd:TIGR02168 422 EIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELR----EELEEAEQALDAAERELAQLQARLDSLE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1467 TLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETeLLQLRAKAV-----DADKLRNAAQEEAEKLRK 1541
Cdd:TIGR02168 496 RL-QENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEA-ALGGRLQAVvvenlNAAKKAIAFLKQNELGRV 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1542 QVAEETQKKrkaEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEA--------------ERHLKQAELEKQRQIQVVE 1607
Cdd:TIGR02168 574 TFLPLDSIK---GTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvddlDNALELAKKLRPGYRIVTL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1608 E---VAKKTAATQLESKQVALT-------ARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANE 1677
Cdd:TIGR02168 651 DgdlVRPGGVITGGSAKTNSSIlerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1678 A----LRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEE---AALKQKEAAEMELGNQRKMAEETAKQKLAAEQ 1750
Cdd:TIGR02168 731 LrkdlARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1751 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEA 1830
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1831 AKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALkeKEAENDRLKRKAEEE 1910
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL--EEAEALENKIEDDEE 968
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 1911 GYQRKVledqaAQHKQAIEEkIGQLKKSSDTELDRQKKIVEETLKQRKVVEE 1962
Cdd:TIGR02168 969 EARRRL-----KRLENKIKE-LGPVNLAAIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
179-277 |
3.71e-16 |
|
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: 77.34 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 179 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 258
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 1207141765 259 -VDVPHPDEKSIITYVSSMY 277
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1715-2652 |
3.81e-16 |
|
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: 86.38 E-value: 3.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1715 KAEEAALK-QKEAAEMELGNQRKMAEETAKQ-KLAAEQELirlradFEHAEQQRTVL---DDELQRLKNDVNSAVKQKKE 1789
Cdd:pfam01576 16 KVKERQQKaESELKELEKKHQQLCEEKNALQeQLQAETEL------CAEAEEMRARLaarKQELEEILHELESRLEEEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1790 LEEELIKVRKEMeillQQKSKAEKETMSNTEKSKQLLESEA----AKMRELAEEATKLRSVAEEAKKQRQIAEE---EAA 1862
Cdd:pfam01576 90 RSQQLQNEKKKM----QQHIQDLEEQLDEEEAARQKLQLEKvtteAKIKKLEEDILLLEDQNSKLSKERKLLEErisEFT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1863 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEA---ENDRLKRKAEEEGYQrkvLEDQAAQHKQAIEEKIGQLKKSS 1939
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKgrqELEKAKRKLEGESTD---LQEQIAELQAQIAELRAQLAKKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1940 DTELDRQKKIVEETLK----QRKVVEEEIHILKLNfEKASSGKQELELELKKLKGIADETQkskakaeeeaekfrklALE 2015
Cdd:pfam01576 243 EELQAALARLEEETAQknnaLKKIRELEAQISELQ-EDLESERAARNKAEKQRRDLGEELE----------------ALK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2016 eekkrkeaeakvkqiqaAEEEAARQHKAAQEEVgrlmklaeEAKKQKEIAEkeaekqvilvqeaAQKCSAAEQKAQNVLV 2095
Cdd:pfam01576 306 -----------------TELEDTLDTTAAQQEL--------RSKREQEVTE-------------LKKALEEETRSHEAQL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2096 QQ--NKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKK-------AEEAERQKKAAEAEAAKQAKAQEDAEKL 2166
Cdd:pfam01576 348 QEmrQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAElrtlqqaKQDSEHKRKKLEGQLQELQARLSESERQ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2167 RKEAEKEASRRAEAEAAALKLKQEADSEmakykklAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSD 2246
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNEAEGK-------NIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNS 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2247 AIKQ-------KAQVEDELSKVKIQMEDLLKLKLKIEKENQEL------MKKDKDNTKKLLEEEAENMKKLAEEAARLNI 2313
Cdd:pfam01576 501 LQEQleeeeeaKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALeegkkrLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2314 EAQEAA----RLRQIAeSDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQV----EAQKLLEAKKEM---- 2381
Cdd:pfam01576 581 ELDDLLvdldHQRQLV-SNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALslarALEEALEAKEELertn 659
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2382 -QQRLD---------------QETEGFQKSLEA---ERKRQLE------ITAEAEKLKVKVT----------QLSDAQSK 2426
Cdd:pfam01576 660 kQLRAEmedlvsskddvgknvHELERSKRALEQqveEMKTQLEeledelQATEDAKLRLEVNmqalkaqferDLQARDEQ 739
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2427 AEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMAN 2506
Cdd:pfam01576 740 GEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARA 819
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2507 VQQEQLQQEKTILQQSFFAEKETL-----LKKEKAIEEEKKKLEKQFEDEVKKAEALK-AEQERQRKL------MEEERK 2574
Cdd:pfam01576 820 SRDEILAQSKESEKKLKNLEAELLqlqedLAASERARRQAQQERDELADEIASGASGKsALQDEKRRLeariaqLEEELE 899
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2575 KLQSAMDAAIKKQKEAEE-------EMNGKQKEMQDLEKKRIEQEKllaeENKNLREKLQQLQSSQKASYTKEIEIQTDK 2647
Cdd:pfam01576 900 EEQSNTELLNDRLRKSTLqveqlttELAAERSTSQKSESARQQLER----QNKELKAKLQEMEGTVKSKFKSSIAALEAK 975
|
....*
gi 1207141765 2648 VPEEE 2652
Cdd:pfam01576 976 IAQLE 980
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
46-160 |
4.59e-16 |
|
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: 76.61 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 46 KKTFTKWVNKHLVKhwkaEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdvvrnsrlpREKGRMRFHKLQNVQIAL 125
Cdd:cd00014 1 EEELLKWINEVLGE----ELPVSITDLFESLRDGVLLCKLINKLSPGSIPKI----------NKKPKSPFKKRENINLFL 66
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141765 126 DFLKHRQV-KLVNIRNDDI-ADGNPKLTLGLIWTIIL 160
Cdd:cd00014 67 NACKKLGLpELDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
179-278 |
9.89e-16 |
|
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: 75.77 E-value: 9.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 179 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 258
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1207141765 259 VDV--PHPDEKSIITYVSSMYD 278
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
646-836 |
1.84e-15 |
|
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: 78.26 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 646 QLHAFVVAATKELMWLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNVQMTGDKLLKDGHPARKTIEAF 725
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 726 TAALQTQWSWILQLCCCIETHLKENTAYFQFFSDVKEAEDRMKKMEDTMKKKYVCDrsiTVTRLEDLLQDAVEEKEQLNE 805
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|.
gi 1207141765 806 FKTHLEGLNRRAKTIIQLKPRNPAQPIKGKL 836
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
177-274 |
3.14e-15 |
|
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: 74.34 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN-LENLEQAFSIAERDLGVTRLLD 255
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1207141765 256 PEDVDVPHPDEKSIITYVS 274
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1644-2617 |
4.13e-15 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 82.95 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1644 QEEAEHLKKQQAEADKAREQAEK----------ELETWRQKANEALR------------LRLQAEEEANKKTAAQEEAEK 1701
Cdd:NF041483 11 RADDDHLSRFEAEMDRLKTEREKavqhaedlgyQVEVLRAKLHEARRslasrpaydgadIGYQAEQLLRNAQIQADQLRA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1702 QKEEAKREAKKRAK------AEEAALKQKE----------AAEMELGNQRKMAEETAKQKLA--------AEQELIRL-- 1755
Cdd:NF041483 91 DAERELRDARAQTQrilqehAEHQARLQAElhteavqrrqQLDQELAERRQTVESHVNENVAwaeqlrarTESQARRLld 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1756 --RADFEH------AEQQRtVLDDELQRLKNDVNSAvkqKKELEEELIKVRKEMEILLQQKSKAEKETMSNTE--KSKQL 1825
Cdd:NF041483 171 esRAEAEQalaaarAEAER-LAEEARQRLGSEAESA---RAEAEAILRRARKDAERLLNAASTQAQEATDHAEqlRSSTA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1826 LESEAAKMR----------ELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAE-------KILKEKLT-----AINEAT 1883
Cdd:NF041483 247 AESDQARRQaaelsraaeqRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAEsaneqrtRTAKEEIArlvgeATKEAE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1884 RLKTEAEIALKEKEAENDRLKRKAEEEGyQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEE 1963
Cdd:NF041483 327 ALKAEAEQALADARAEAEKLVAEAAEKA-RTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1964 IHilKLNFEKASSGKQelelelkkLKGIA-DETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQA-AEEEAARQ- 2040
Cdd:NF041483 406 AD--RLRGEAADQAEQ--------LKGAAkDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGeARREAVQQi 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2041 HKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKqviLVQEAAQKCSAAEQKAQNVLvqqnkdsmaqDKLKEEFEKAKKLAQE 2120
Cdd:NF041483 476 EEAARTAEELLTKAKADADELRSTATAESER---VRTEAIERATTLRRQAEETL----------ERTRAEAERLRAEAEE 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2121 -AEKAKDNAEKEAALLHkkaEEAERqkkaaeAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAaalklkqEADSEMAKYK 2199
Cdd:NF041483 543 qAEEVRAAAERAARELR---EETER------AIAARQAEAAEELTRLHTEAEERLTAAEEALA-------DARAEAERIR 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2200 K-LAEKTLKQKSSVEEELVKVKVQLDEtdkqksvldvELKRLKQEVSdAIKQKAQVEDELSKVKIQMEdllklklkIEKE 2278
Cdd:NF041483 607 ReAAEETERLRTEAAERIRTLQAQAEQ----------EAERLRTEAA-ADASAARAEGENVAVRLRSE--------AAAE 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2279 NQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQ-EAARLRQIAESDLAKQRELAEkmlEEKKQAIQEAAKLKAEA 2357
Cdd:NF041483 668 AERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQeEAARRRREAEETLGSARAEAD---QERERAREQSEELLASA 744
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2358 eklQKQKDQAQVEAQKLLE------------AKKEMQQRLD----------QETEGFQKSLE--AERKRQlEITAEAEKL 2413
Cdd:NF041483 745 ---RKRVEEAQAEAQRLVEeadrratelvsaAEQTAQQVRDsvaglqeqaeEEIAGLRSAAEhaAERTRT-EAQEEADRV 820
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2414 KvkvtqlSDAQS---KAEEEAKKFKKQADEikirlqETE--KHTSEKhTVVEKL-EVQRLQSkQEADGLHKAIADLEKEK 2487
Cdd:NF041483 821 R------SDAYAereRASEDANRLRREAQE------ETEaaKALAER-TVSEAIaEAERLRS-DASEYAQRVRTEASDTL 886
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2488 EKLKKEAADLQKQSKEMANvqqeqlqqektiLQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRK 2567
Cdd:NF041483 887 ASAEQDAARTRADAREDAN------------RIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRAD 954
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2568 LMEEERKKLQSAMDAAIKKQKEAEEEMNGKQkemQDLEKKRIEQEKLLAE 2617
Cdd:NF041483 955 AAAQAEQLIAEATGEAERLRAEAAETVGSAQ---QHAERIRTEAERVKAE 1001
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2021-2581 |
4.42e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 4.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2021 KEAEAKVKQIQAAEEEAARQHKAAQEEVGRLmkLAEEAKKQKEIAEKEAEKQVilvqeaaqkcsaAEQKAQNVLVQQNKD 2100
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEA--QAEEYELLAELARLEQDIAR------------LEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2101 SMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEA 2180
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2181 EAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSK 2260
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2261 VKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKL------AEEAARLNIEAQEAARLRQIAESDLAKQRE 2334
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvavligVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2335 LAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL-----LEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAE 2409
Cdd:COG1196 562 AIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVdlvasDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2410 AEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETekhtsekhtvvEKLEVQRLQSKQEADGLHKAIADLEKEKEK 2489
Cdd:COG1196 642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE-----------LEELAERLAEEELELEEALLAEEEEERELA 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2490 LKKEAADLQKQSKEMANVQQEQLQQEKTILQQsffaEKETLLKKEKAIEEEKKKLEKQFEDEVKKA-------------- 2555
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELL----EEEELLEEEALEELPEPPDLEELERELERLereiealgpvnlla 786
|
570 580 590
....*....|....*....|....*....|...
gi 1207141765 2556 -EALKAEQER------QRKLMEEERKKLQSAMD 2581
Cdd:COG1196 787 iEEYEELEERydflseQREDLEEARETLEEAIE 819
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1141-1807 |
5.37e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1141 AEDILNKYENQLREVnkvpvnEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEvnkrmsqlhserdvELEHYRQL 1220
Cdd:COG1196 251 LEAELEELEAELAEL------EAELEELRLELEELELELEEAQAEEYELLAELARLEQ--------------DIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1221 VGNLRERwqavfaQIELRQRELDLLNRQMQAYREsydwLIRWIADAKQRQDKLHAvpiggskgLQEQLTQEKKLLEEIEK 1300
Cdd:COG1196 311 RRELEER------LEELEEELAELEEELEELEEE----LEELEEELEEAEEELEE--------AEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1301 NKDKVEdcqkfakgyidaikdyELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRyselmtlssqyikfIIET 1380
Cdd:COG1196 373 ELAEAE----------------EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER--------------LEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1381 QRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDvavdsEKQKHNIQR 1460
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-----AAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1461 ELQELKTLSEQEIKAKSQQVEEALLSRTrieeeihiIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLR 1540
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGA--------VAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1541 KQVAEEtqkkRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLES 1620
Cdd:COG1196 570 KAGRAT----FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1621 KQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAE 1700
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1701 KQKEEAKREAKKRAKAEEAALKQKEAAEMELgnQRKMAEETAKQKLA-AEQELIRL-----RADFEHAEQQRTVldDELQ 1774
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEEL--PEPPDLEELERELErLEREIEALgpvnlLAIEEYEELEERY--DFLS 801
|
650 660 670
....*....|....*....|....*....|...
gi 1207141765 1775 RLKNDVNSAvkqKKELEEELIKVRKEMEILLQQ 1807
Cdd:COG1196 802 EQREDLEEA---RETLEEAIEEIDRETRERFLE 831
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
179-282 |
6.57e-15 |
|
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: 73.54 E-value: 6.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 179 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 258
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1207141765 259 VDV--PHPDEKSIITYVSSMYDVMPR 282
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4071-4109 |
7.78e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.82 E-value: 7.78e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1207141765 4071 LLEAQIATGGIIDPEESHRLPVEMAYKRGLFDEEMNGIL 4109
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
179-277 |
8.79e-15 |
|
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: 73.58 E-value: 8.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 179 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 258
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|
gi 1207141765 259 -VDVPHPDEKSIITYVSSMY 277
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELY 102
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
182-277 |
1.06e-14 |
|
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: 73.16 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 182 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAErDLGVTRLLDPED-VD 260
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1207141765 261 VPHPDEKSIITYVSSMY 277
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
45-162 |
1.36e-14 |
|
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: 72.72 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 45 QKKTFTKWVNKHLVKHwkaEAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerDVVRNsrlPREKGRMRfhklQNVQIA 124
Cdd:cd21213 1 QLQAYVAWVNSQLKKR---PGIRPVQDLRRDLRDGVALAQLIEILAGEKLP---GIDWN---PTTDAERK----ENVEKV 67
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141765 125 LDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 162
Cdd:cd21213 68 LQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1409-2344 |
1.54e-14 |
|
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: 81.25 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1409 LEKQKQLAETHAKAIAKAEQEANELKT------KMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSE--QEIKAKSQQV 1480
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQykekacEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKeiEHNLSKIMKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1481 EEALLSRTRIEEEIHIIRLQLETTMKQ--KNTAE--TELLQLRAKAV-DADKLRNAAQEEAEKLRKQVAEETQKKRKAEE 1555
Cdd:TIGR00606 268 DNEIKALKSRKKQMEKDNSELELKMEKvfQGTDEqlNDLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQEKTELLV 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1556 ELKRKSEAEKDAAKEKKKALEDLEKFKLQAE--------EAERHLKQA-ELEKQRQIQVVEEVAKKTA--ATQLESKQVA 1624
Cdd:TIGR00606 348 EQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfergpFSERQIKNFhTLVIERQEDEAKTAAQLCAdlQSKERLKQEQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1625 LT------ARLEESLKNEQVMVIQLQEEAEHLKKQQAEAdkarEQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEE 1698
Cdd:TIGR00606 428 ADeirdekKGLGRTIELKKEILEKKQEELKFVIKELQQL----EGSSDRILELDQELRKAERELSKAEKNSLTETLKKEV 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1699 AEKQKEEAKREAKKRAKAEEAALKQKEA---AEMELGNQRKMA--EETAKQKLAAEQELIRLRADFEHAEQqrtvLDDEL 1773
Cdd:TIGR00606 504 KSLQNEKADLDRKLRKLDQEMEQLNHHTttrTQMEMLTKDKMDkdEQIRKIKSRHSDELTSLLGYFPNKKQ----LEDWL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1774 QRLKNDvnsavkqKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLES--EAAKMRELAEEATKLRSVAEEAK 1851
Cdd:TIGR00606 580 HSKSKE-------INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIEKSS 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1852 KQRQIAEEEAARQRAEAEKILKEKLTAINEATR-LKTEAEIALKEKEAENDRLKRKAEEEGyqrkvLEDQAAQHKQAIEE 1930
Cdd:TIGR00606 653 KQRAMLAGATAVYSQFITQLTDENQSCCPVCQRvFQTEAELQEFISDLQSKLRLAPDKLKS-----TESELKKKEKRRDE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1931 KIGqLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFR 2010
Cdd:TIGR00606 728 MLG-LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVER 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2011 KLA-LEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKqviLVQEAAQKCSAAEQK 2089
Cdd:TIGR00606 807 KIAqQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE---LKSEKLQIGTNLQRR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2090 AQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEaerqkkaaeaeaakqakaqedaeklRKE 2169
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETS-------------------------NKK 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2170 AEKEASRRAEaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIK 2249
Cdd:TIGR00606 939 AQDKVNDIKE------KVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI 1012
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2250 QKAQVEDELSKVKIQMEdllklklkIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAArlNIEAQEAARLRQIAESDl 2329
Cdd:TIGR00606 1013 QERWLQDNLTLRKRENE--------LKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENID--LIKRNHVLALGRQKGYE- 1081
|
970
....*....|....*
gi 1207141765 2330 aKQRELAEKMLEEKK 2344
Cdd:TIGR00606 1082 -KEIKHFKKELREPQ 1095
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2106-2641 |
2.95e-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: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2106 KLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKaaeaeaakqakaqeDAEKLRKEAEKEASrraeaeaaal 2185
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMK--------------DLTFLLEESRDKAN---------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2186 KLKQEADSEMAKYKKLAEKtlkqKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQM 2265
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEK----KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAH 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2266 EDLLKLKLKIEKENQELMKKDKDNtkklLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQREL---AEKMLEE 2342
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQR----LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIlaeDEKLLDE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2343 KKQAIQEAAKLKAEAEKL-----QKQKDQAQVEAQklLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKV 2417
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELifllqAREKEIHDLEIQ--LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2418 TQLSDAQS-------KAEEEAKKFKKQADEIKIR---LQETEKH-TSEKHTVVEKLEVQRLQ-------SKQEADGLHKA 2479
Cdd:pfam05483 502 KELTQEASdmtlelkKHQEDIINCKKQEERMLKQienLEEKEMNlRDELESVREEFIQKGDEvkckldkSEENARSIEYE 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2480 IADLEKEKEKLKKEAADLQKQSkEMANVQQEQLQQEKTILQQSFFAEKETLLK---KEKAIEEEKKKLEKQFEDEVKKAE 2556
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQI-ENKNKNIEELHQENKALKKKGSAENKQLNAyeiKVNKLELELASAKQKFEEIIDNYQ 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2557 ALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKN---LREKLQQLQSSQ 2633
Cdd:pfam05483 661 KEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSelgLYKNKEQEQSSA 740
|
....*...
gi 1207141765 2634 KASYTKEI 2641
Cdd:pfam05483 741 KAALEIEL 748
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2296-2656 |
3.54e-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: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2296 EEAEnmKKLaeEAARLNIEaqeaaRLRQIAE------SDLAKQRELAEKMLE---EKKQAIQEAAKLKAEAEKLQKQKDQ 2366
Cdd:COG1196 175 EEAE--RKL--EATEENLE-----RLEDILGelerqlEPLERQAEKAERYRElkeELKELEAELLLLKLRELEAELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2367 AQVEAQKLLEAKKEMQQRLDQETegfqksLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQ 2446
Cdd:COG1196 246 AELEELEAELEELEAELAELEAE------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2447 ETEKhtsekhtVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAE 2526
Cdd:COG1196 320 ELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2527 KETLlkkekaieeekkklekqfedevkKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEK 2606
Cdd:COG1196 393 RAAA-----------------------ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2607 KRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQM 2656
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
39-161 |
4.19e-14 |
|
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: 71.54 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 39 DERDrvqKKTFTKWVNKHLVKHwkaeaqrHITDLYEDLRDGhnlISLLEVLsgETLprERDVVRNSRLPREKGRMRFHKL 118
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLDP-------LINNLYEDLRDG---LVLLQVL--DKI--QPGCVNWKKVNKPKPLNKFKKV 64
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141765 119 QNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 161
Cdd:cd21219 65 ENCNYAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1379-2474 |
5.98e-14 |
|
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: 79.06 E-value: 5.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1379 ETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKaEQEANELKTKMKDEVSKRQDVAVDSEKQKHNI 1458
Cdd:pfam01576 23 KAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAAR-KQELEEILHELESRLEEEEERSQQLQNEKKKM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1459 QRELQELKT-LSEQEIKAKSQQVEEALLSRT--RIEEEIHIIRLQLETTMKQKNTAE-------TELLQLRAKAVDADKL 1528
Cdd:pfam01576 102 QQHIQDLEEqLDEEEAARQKLQLEKVTTEAKikKLEEDILLLEDQNSKLSKERKLLEeriseftSNLAEEEEKAKSLSKL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1529 RNAAQEEAEKLRKQVAEEtQKKRKAEEELKRKSEAEKDAAKEKkkaledLEKFKLQAEEAERHLKQAELEKQR-QIQVVE 1607
Cdd:pfam01576 182 KNKHEAMISDLEERLKKE-EKGRQELEKAKRKLEGESTDLQEQ------IAELQAQIAELRAQLAKKEEELQAaLARLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1608 EVAKKTAATQLESKQVALTARLEESLKNEQVMVIQ-------LQEEAEHLKKQ----------QAEADKAREQAEKELEt 1670
Cdd:pfam01576 255 ETAQKNNALKKIRELEAQISELQEDLESERAARNKaekqrrdLGEELEALKTEledtldttaaQQELRSKREQEVTELK- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1671 wRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKE--AAEMELGNQRKMAEETAKQKLaa 1748
Cdd:pfam01576 334 -KALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAelQAELRTLQQAKQDSEHKRKKL-- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1749 EQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLles 1828
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNL--- 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1829 eAAKMRELAEEATKLRSVAEEAKKQRQIAEEE---AARQRAEAEKILKEKLTAINEATRLKTEAEialKEKEAENDRLKR 1905
Cdd:pfam01576 488 -STRLRQLEDERNSLQEQLEEEEEAKRNVERQlstLQAQLSDMKKKLEEDAGTLEALEEGKKRLQ---RELEALTQQLEE 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1906 KAEEegYQRkvLEDQAAQHKQAIEEKIgqlkkssdTELDRQKKIVEETLKQRKVVEEeihilKLNFEKASSGKqelelel 1985
Cdd:pfam01576 564 KAAA--YDK--LEKTKNRLQQELDDLL--------VDLDHQRQLVSNLEKKQKKFDQ-----MLAEEKAISAR------- 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1986 kklkgIADETQKSKAKAEEEAEKFRKLAleeekkrkeaeAKVKQIQAAEEEAARQHKAAQEEVGRLM-------KLAEEA 2058
Cdd:pfam01576 620 -----YAEERDRAEAEAREKETRALSLA-----------RALEEALEAKEELERTNKQLRAEMEDLVsskddvgKNVHEL 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2059 KKQKEIAEKEAEKQVILVQEAAQKCSAAEQ------------KAQNVLVQQNKDSMAQDKLKEEFEKAKKLaqEAEKAKD 2126
Cdd:pfam01576 684 ERSKRALEQQVEEMKTQLEELEDELQATEDaklrlevnmqalKAQFERDLQARDEQGEEKRRQLVKQVREL--EAELEDE 761
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2127 NAEKEAALLHKKAEEAErqkkaaeaeAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTL 2206
Cdd:pfam01576 762 RKQRAQAVAAKKKLELD---------LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESE 832
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2207 KQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekenqelmkkd 2286
Cdd:pfam01576 833 KKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQL------------------ 894
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2287 kdntKKLLEEEAENMKKLAEEAARLNIEAqEAARLRQIAESDLAKQRELAEKMLEEKKQAIQeaAKLkAEAEKLQKQKDQ 2366
Cdd:pfam01576 895 ----EEELEEEQSNTELLNDRLRKSTLQV-EQLTTELAAERSTSQKSESARQQLERQNKELK--AKL-QEMEGTVKSKFK 966
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2367 AQVEAqklLEAK-KEMQQRLDQETEGFQKSLEAERKRQleitaeaEKLKVKVTQLSDAQSKAEEeakkFKKQADEIKIRL 2445
Cdd:pfam01576 967 SSIAA---LEAKiAQLEEQLEQESRERQAANKLVRRTE-------KKLKEVLLQVEDERRHADQ----YKDQAEKGNSRM 1032
|
1130 1140
....*....|....*....|....*....
gi 1207141765 2446 QETEKHTSEKHTVVEKLEVQRLQSKQEAD 2474
Cdd:pfam01576 1033 KQLKRQLEEAEEEASRANAARRKLQRELD 1061
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
42-158 |
6.33e-14 |
|
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: 71.02 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 42 DRVQKKTFTKWVNKHLVKhwkaEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDVVRNSRLPRekgrmrfhkLQNV 121
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEK----RGIPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEPKNRIQM---------IQNL 68
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141765 122 QIALDFL-KHRQVKLVNIRNDDIADGNPKLTLGLIWTI 158
Cdd:cd21225 69 HLAMLFIeEDLKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
179-274 |
6.70e-14 |
|
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: 70.49 E-value: 6.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 179 KEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGVTRLLDPE 257
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1207141765 258 DVDVPHPDEKSIITYVS 274
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3092-3130 |
7.06e-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: 7.06e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1207141765 3092 LLEAQAGTGFIIDPVKNQKLTVDEAVKSGVVGPELHEKL 3130
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
177-277 |
2.54e-13 |
|
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: 69.33 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAErDLGVTRLLDP 256
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1207141765 257 ED-VDVPHPDEKSIITYVSSMY 277
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1162-1930 |
3.37e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 76.75 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1162 EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQR-ATEVNKRMSQLHSERDV--ELEHYRQLVGNLRERWQAVFAQIELR 1238
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQlCEEKNALQEQLQAETELcaEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1239 QRELDLLNRQMQAYRESydwLIRWIADAKQRQDKLHAvpigGSKGLQ-EQLTQE---KKLLEEIEKNKDKVEDCQKFAKG 1314
Cdd:pfam01576 84 LEEEEERSQQLQNEKKK---MQQHIQDLEEQLDEEEA----ARQKLQlEKVTTEakiKKLEEDILLLEDQNSKLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1315 YIDAIKDYELQLvtykalvepiASPLKKAKMesasddiiqeyvtlrtryseLMTLSSQYIKFIIETQRRLQDEEK----- 1389
Cdd:pfam01576 157 LEERISEFTSNL----------AEEEEKAKS--------------------LSKLKNKHEAMISDLEERLKKEEKgrqel 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1390 -----AAEKLKEEERKKMAEMQAELEKQK-QLA---ETHAKAIAKAEQEAN-----------------ELKTKMKDEVSK 1443
Cdd:pfam01576 207 ekakrKLEGESTDLQEQIAELQAQIAELRaQLAkkeEELQAALARLEEETAqknnalkkireleaqisELQEDLESERAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1444 RQdvavDSEKQKHNIQRELQELK---------TLSEQEIKAKSQQvEEALLSRTrIEEEIHIIRLQLEtTMKQKNTAETE 1514
Cdd:pfam01576 287 RN----KAEKQRRDLGEELEALKteledtldtTAAQQELRSKREQ-EVTELKKA-LEEETRSHEAQLQ-EMRQKHTQALE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1515 -----LLQLRAKAVDADKLRNAAQEEAEKLRKQV-------AEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFK 1582
Cdd:pfam01576 360 elteqLEQAKRNKANLEKAKQALESENAELQAELrtlqqakQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1583 LQAEEAERHLKQAElekQRQIQVVEEVAkkTAATQLESKQVALTARLEESLKNEQvMVIQLQEEAEHLKKQQAEADKARE 1662
Cdd:pfam01576 440 SELESVSSLLNEAE---GKNIKLSKDVS--SLESQLQDTQELLQEETRQKLNLST-RLRQLEDERNSLQEQLEEEEEAKR 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1663 QAEKELETWRQ------KANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQK-EAAEMELGNQR 1735
Cdd:pfam01576 514 NVERQLSTLQAqlsdmkKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQElDDLLVDLDHQR 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1736 KMAEETAKQ-----KLAAEQELIRLRA--DFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQK 1808
Cdd:pfam01576 594 QLVSNLEKKqkkfdQMLAEEKAISARYaeERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK 673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1809 SKAEKeTMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAK------------------KQRQIAEEEAARQRA---- 1866
Cdd:pfam01576 674 DDVGK-NVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKlrlevnmqalkaqferdlQARDEQGEEKRRQLVkqvr 752
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141765 1867 EAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE 1930
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEE 816
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3752-3790 |
3.75e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.20 E-value: 3.75e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1207141765 3752 LLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPEFHDKL 3790
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1120-1904 |
3.97e-13 |
|
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: 76.70 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1120 LSSVYLDKLKTIDLVIRSTQGAEDILNKYENQLREVNKVP-VNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATE 1198
Cdd:pfam15921 119 LQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKcLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1199 VNKRmsQLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYREsydwlirwiadakQRQDKLHAVpi 1278
Cdd:pfam15921 199 ASGK--KIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKS-------------ESQNKIELL-- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1279 ggskglqeqltqekklleeIEKNKDKVEDCqkfakgyidaIKDYELQLVtykALVEPIASPLKKAKMESASDDIIQEYVT 1358
Cdd:pfam15921 262 -------------------LQQHQDRIEQL----------ISEHEVEIT---GLTEKASSARSQANSIQSQLEIIQEQAR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1359 LRT-----RYSELMTLSSQYIKFIIETQRRLQDEEKaaeklkeeerkkmaemqaELEKQKQLAETHakaIAKAEQEANEL 1433
Cdd:pfam15921 310 NQNsmymrQLSDLESTVSQLRSELREAKRMYEDKIE------------------ELEKQLVLANSE---LTEARTERDQF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1434 KTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIkAKSQQVEEalLSRTRIEEEIHIIRLQ-LETTMKQKNTAE 1512
Cdd:pfam15921 369 SQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDT-GNSITIDH--LRRELDDRNMEVQRLEaLLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1513 TEllqlraKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaledlekfKLQAEEAER-- 1590
Cdd:pfam15921 446 ME------RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAK---------------------KMTLESSERtv 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1591 -HLKQAELEKQRQIQvveevAKKTAATQLESKqVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELE 1669
Cdd:pfam15921 499 sDLTASLQEKERAIE-----ATNAEITKLRSR-VDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIE 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1670 TWRQKANEALRL-------RLQAEEEANKKtaAQEEAEKQKEEAKREAKKRA-KAEEAALKQKEAAEMELGNQRKMAEET 1741
Cdd:pfam15921 573 NMTQLVGQHGRTagamqveKAQLEKEINDR--RLELQEFKILKDKKDAKIRElEARVSDLELEKVKLVNAGSERLRAVKD 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1742 AKQKL--------AAEQELIRLRADFE--------HAEQQRTVLD----------DELQRLKNDVNS-------AVKQKK 1788
Cdd:pfam15921 651 IKQERdqllnevkTSRNELNSLSEDYEvlkrnfrnKSEEMETTTNklkmqlksaqSELEQTRNTLKSmegsdghAMKVAM 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1789 ELEEELIKVRKEMEIlLQQKSKAEKETMSNTEKSKQLLESEAAKMRElaeeatKLRSVAEEakKQRQIAEEEAARQRaea 1868
Cdd:pfam15921 731 GMQKQITAKRGQIDA-LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ------ELSTVATE--KNKMAGELEVLRSQ--- 798
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1207141765 1869 EKILKEKLT----AINEATRLKTEAEIALKEKEAENDRLK 1904
Cdd:pfam15921 799 ERRLKEKVAnmevALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2765-2803 |
4.13e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.20 E-value: 4.13e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1207141765 2765 LLEAQAASGYIIDPIKNRRLSVSESVKDGLIGPELHTKL 2803
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1873-2671 |
5.78e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.86 E-value: 5.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1873 KEKLTAINEA---TRLKTEAEIALKEKEAENDRLKRkaeeegyqrkvLEDqaaqhkqAIEEKIGQLKKssdteLDRQKKI 1949
Cdd:TIGR02168 155 EERRAIFEEAagiSKYKERRKETERKLERTRENLDR-----------LED-------ILNELERQLKS-----LERQAEK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1950 VEETLKQRKVVEE-EIHILKLNFEKASSGKQELELELKKLKGIADETQKskakaeeeaekfrklaleeekkrkeaeaKVK 2028
Cdd:TIGR02168 212 AERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTA----------------------------ELQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2029 QIQAAEEEAARQHKAAQEEVGRLMKLAEEAKkqKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKdsmaqDKLK 2108
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALA--NEISRLEQQKQILRERLANLERQLEELEAQLEELESKL-----DELA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2109 EEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEK----LRKEAEKEASRRAEAEAAA 2184
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELqiasLNNEIERLEARLERLEDRR 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2185 LKLKQEADSEMAKYKKLAEKTLKQK-SSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKI 2263
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2264 QME--DLLKLKLKIEKENQELMKKDKDNTKKLLEEEA-----------ENMKKLA---EEAARLNIEAQEAARL--RQIA 2325
Cdd:TIGR02168 497 LQEnlEGFSEGVKALLKNQSGLSGILGVLSELISVDEgyeaaieaalgGRLQAVVvenLNAAKKAIAFLKQNELgrVTFL 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2326 ESDLAKQRELAEKMLEEKK-------------------------------------QAIQEAAKL--------------- 2353
Cdd:TIGR02168 577 PLDSIKGTEIQGNDREILKniegflgvakdlvkfdpklrkalsyllggvlvvddldNALELAKKLrpgyrivtldgdlvr 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2354 -------------------KAEAEKLQKQKDQAQV---EAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAE 2411
Cdd:TIGR02168 657 pggvitggsaktnssilerRREIEELEEKIEELEEkiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2412 KLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEkekeklk 2491
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR------- 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2492 keaADLQKQSKEMANVQQEQLQQEKTIlqqsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEE 2571
Cdd:TIGR02168 810 ---AELTLLNEEAANLRERLESLERRI------AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2572 ERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEenknLREKLQQLQSsqkasytkEIEIQTDKVPEE 2651
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ----LELRLEGLEV--------RIDNLQERLSEE 948
|
890 900
....*....|....*....|
gi 1207141765 2652 ELVQMTMVETTKKVLNGSTE 2671
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEE 968
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1213-1911 |
6.10e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 75.78 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1213 ELEHYRQLVGNLRERWQAVFAQIELRQREL----DLLNRQMQAYRESYDWLIRWIADAKQRQDKLhavpiggsKGLQEQL 1288
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQT--------QQSHAYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1289 TQEKKLLEEIEKNkdkvedcQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMESASDDIIQ-------EYVTLRT 1361
Cdd:TIGR00618 246 TQKREAQEEQLKK-------QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQieqqaqrIHTELQS 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1362 RYSELMTLSSQYIKFI-----IETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAEtHAKAIAKAEQEANELKTK 1436
Cdd:TIGR00618 319 KMRSRAKLLMKRAAHVkqqssIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1437 MKDEVSKRQDVAVDSEKQkHNIQRELQELKTLSEQEIKAksqQVEEALLSRTRIEEE--IHIIRLQLETTMKQKNTAETE 1514
Cdd:TIGR00618 398 LCKELDILQREQATIDTR-TSAFRDLQGQLAHAKKQQEL---QQRYAELCAAAITCTaqCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1515 LLQLRAKAVDADKlRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQ 1594
Cdd:TIGR00618 474 QLQTKEQIHLQET-RKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1595 AELEkqrQIQVVEEvaKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEhlKKQQAEADKAREQAEKELETWRQK 1674
Cdd:TIGR00618 553 SERK---QRASLKE--QMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE--KLSEAEDMLACEQHALLRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1675 ANEALRLRLQ--AEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQEL 1752
Cdd:TIGR00618 626 DLQDVRLHLQqcSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTL 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1753 IR-----LRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLE 1827
Cdd:TIGR00618 706 LRelethIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1828 SEAAKMRELAEEATKLRSVAEEAKKQ-------RQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAEN 1900
Cdd:TIGR00618 786 EIQFFNRLREEDTHLLKTLEAEIGQEipsdediLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLT 865
|
730
....*....|.
gi 1207141765 1901 DRLKRKAEEEG 1911
Cdd:TIGR00618 866 QEQAKIIQLSD 876
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
47-165 |
8.56e-13 |
|
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: 67.65 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 47 KTFTKWVNKHLVkhwkaeaQRHITDLYEDLRDGHNLISLLEVLSgetlPRERDVVRNSRLPREKGRMrFHKLQNVQIALD 126
Cdd:cd21298 9 KTYRNWMNSLGV-------NPFVNHLYSDLRDGLVLLQLYDKIK----PGVVDWSRVNKPFKKLGAN-MKKIENCNYAVE 76
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141765 127 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 165
Cdd:cd21298 77 LGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
177-277 |
1.38e-12 |
|
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: 66.98 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAErDLGVTRLLDP 256
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1207141765 257 ED-VDVPHPDEKSIITYVSSMY 277
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3168-3206 |
2.05e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.89 E-value: 2.05e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1207141765 3168 LLEAQLATGGIIDPEKSYRITPDIAYKRGHLNEEMNQNL 3206
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1655-2442 |
2.58e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.95 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1655 AEADKAREQAEKELETWRQKANealRLRLQAEEEANKktaaqeeaekqkeeAKREAKKRAKAEEAALKQKEAAEMELGNQ 1734
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIE---RLDLIIDEKRQQ--------------LERLRREREKAERYQALLKEKREYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1735 RKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKEL-EEELIKVRKEMEILLQQKSKAEK 1813
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1814 ETMSNTEKSKQLLESEA---AKMRELAEEATKL-RSVAEEAKKQRQIAEEEAARQ------RAEAEKILKEKLTAINEAT 1883
Cdd:TIGR02169 309 SIAEKERELEDAEERLAkleAEIDKLLAEIEELeREIEEERKRRDKLTEEYAELKeeledlRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1884 RLKTEAEIALKEKEAENDRLKRKAEEegyqRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKI------VEETLKQR 1957
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEE----LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIkkqewkLEQLAADL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1958 KVVEEEIHILKLNF---EKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRK-----------------LALEEE 2017
Cdd:TIGR02169 465 SKYEQELYDLKEEYdrvEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryaTAIEVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2018 KKRKEAEAKVKQIQAAEE--EAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAaqkcsaaEQKAQNVLV 2095
Cdd:TIGR02169 545 AGNRLNNVVVEDDAVAKEaiELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEF-------DPKYEPAFK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2096 QQNKDSMaqdkLKEEFEKAKKLAQEAEKAKDNAEkeaalLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEAS 2175
Cdd:TIGR02169 618 YVFGDTL----VVEDIEAARRLMGKYRMVTLEGE-----LFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2176 RRAEAEAAALKLKQEADSEMAKYKKLAEKT---LKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKA 2252
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIgeiEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2253 QVEDELSKVKIQMEDllklklKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQ 2332
Cdd:TIGR02169 769 ELEEDLHKLEEALND------LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2333 RELAEKMLEEKkqaiQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEmqqrLDQETEGFQKSLEAERKRQLEITAEAEK 2412
Cdd:TIGR02169 843 IDLKEQIKSIE----KEIENLNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIEELEAQIEK 914
|
810 820 830
....*....|....*....|....*....|
gi 1207141765 2413 LKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2442
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
551-740 |
3.30e-12 |
|
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: 69.01 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 551 LKYIQDLLSWVEENQRRIEGAEWGEDLPSVESQLGSHRGLHQSIEEFKYKIDRARADENQLT---PVSKGAYREYLGKLD 627
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIeegHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 628 LQYAKLLTSSKTRLRSLD---QLHAFVVAATKELMWLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNV 704
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207141765 705 QMTGDKLLKDGHP-ARKTIEAFTAALQTQWSWILQLC 740
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3419-3457 |
7.29e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 7.29e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1207141765 3419 LLEAQAATGYIIDPIRNEMFTVDDAVKAGIVGPEVHEKL 3457
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3995-4033 |
7.51e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 7.51e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1207141765 3995 LLEAQAATGYIIDPIKNLKMNVQEAVKMGVVGPEFKDKL 4033
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1708-2360 |
8.58e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1708 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRtvldDELQRLKNDVNSAVKQK 1787
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1788 KELEEELikvrKEMEILLQQKSKAEKETMSNTEKSKQLLEsEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAE 1867
Cdd:PRK03918 248 ESLEGSK----RKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1868 AEKIlKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEegYQR-KVLEDQAAQHKqaieekigqlKKSSDTELDRQ 1946
Cdd:PRK03918 323 INGI-EERIKELEEKEERLEELKKKLKELEKRLEELEERHEL--YEEaKAKKEELERLK----------KRLTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1947 KKIVEETLKQRKVVEEEIHILKlnfEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRK-LALEEEKKRKEAEA 2025
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKIT---ARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKeLLEEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2026 KVKQIQAAEEEAarqhKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQD 2105
Cdd:PRK03918 467 ELKEIEEKERKL----RKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2106 KLKEEFEKAKKLaqeaekakdnaEKEAALLHKKAEEAERQKkaaeaeaakqakaqedaEKLRKEAEKEASRRAEAEAAAL 2185
Cdd:PRK03918 543 SLKKELEKLEEL-----------KKKLAELEKKLDELEEEL-----------------AELLKELEELGFESVEELEERL 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2186 KLKQEADSEMAKYKKlAEKTLKQKssvEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVE-DELSKVKIQ 2264
Cdd:PRK03918 595 KELEPFYNEYLELKD-AEKELERE---EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLE 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2265 MEDLLKLKLKIEKENQELMKKDKDNTKKlLEEEAENMKKLAEEAARLNIEAQEAARLRQ--------IAESDLAKQRELA 2336
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEK-LKEELEEREKAKKELEKLEKALERVEELREkvkkykalLKERALSKVGEIA 749
|
650 660
....*....|....*....|....
gi 1207141765 2337 EKMLEEKKQAIQEAAKLKAEAEKL 2360
Cdd:PRK03918 750 SEIFEELTEGKYSGVRVKAEENKV 773
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1403-1919 |
9.99e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.61 E-value: 9.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1403 AEMQAELEKQKQLAETHAKAIAKAEQEANELKtkmkDEVSKRQDVAVDSEKQKHNIQRELQelktLSEQEIKAKSQQVEE 1482
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELA----EEVRDLRERLEELEEERDDLLAEAG----LDDADAEAVEARREE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1483 ALLSRTRIEEEIHIIRLQLETTmkqKNTAETellqLRAKAVDADKLRNAAQEEAEKLRKQV--AEETQKKRKAE-EELKR 1559
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAH---NEEAES----LREDADDLEERAEELREEAAELESELeeAREAVEDRREEiEELEE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1560 KSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEES-----LK 1634
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSphvetIE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1635 NEQVMVIQLQEEAEHLKKQQAEADKAREQA------EKELETWRQKANEALRLRLQAEEEANkktaaqeeaekqkeeakr 1708
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAedlveaEDRIERLEERREDLEELIAERRETIE------------------ 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1709 eakkrAKAEEAALKQKEAAEMELGNQRKmAEETAKQKLAAEQELIRLRAdfehAEQQRTVLDDELQRLkNDVNSAVKQKK 1788
Cdd:PRK02224 534 -----EKRERAEELRERAAELEAEAEEK-REAAAEAEEEAEEAREEVAE----LNSKLAELKERIESL-ERIRTLLAAIA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1789 ELEEELIKVRKemeillQQKSKAEKEtmsntEKSKQLLESEAAKMRELAEEATKLRsvAEEAKKQRQIAEEEAARqraea 1868
Cdd:PRK02224 603 DAEDEIERLRE------KREALAELN-----DERRERLAEKRERKRELEAEFDEAR--IEEAREDKERAEEYLEQ----- 664
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141765 1869 ekiLKEKLTAINEA-TRLKTE---AEIALKEKEAENDRLKRKAEEEGYQRKVLED 1919
Cdd:PRK02224 665 ---VEEKLDELREErDDLQAEigaVENELEELEELRERREALENRVEALEALYDE 716
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2062-2642 |
1.01e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.63 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2062 KEIAEKEAEKQVILVQEA--AQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKD---NAEKEAALLH 2136
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEeieELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2137 KKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAeaaaLKLKQEadseMAKYKKLAEKTLKQKSSVEEEL 2216
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY----IKLSEF----YEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2217 VKVKVQLDETDKQKSVLDvELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEE 2296
Cdd:PRK03918 324 NGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2297 EAENMKKLAEEAARLNIEAQEaaRLRQIAESDLAKQ------RELAE----KMLEEKKQAIQEAAKLKAEAEKLQKQKDQ 2366
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKE--LKKAIEELKKAKGkcpvcgRELTEehrkELLEEYTAELKRIEKELKEIEEKERKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2367 AQVEAQKLLEAKKEM--QQRLDQETEGFQKSLEAERKRQLEITA-EAEKLKVKVTQLSDAQSKAEEEAKK---FKKQADE 2440
Cdd:PRK03918 481 ELRELEKVLKKESELikLKELAEQLKELEEKLKKYNLEELEKKAeEYEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2441 IKIRLQETEKHTSEKHTvveKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIlq 2520
Cdd:PRK03918 561 LEKKLDELEEELAELLK---ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEEL-- 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2521 qsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLME-EERKKLQSAMDAAIKKQKEAEEEMNGKQK 2599
Cdd:PRK03918 636 ----AETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAElEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1207141765 2600 EMQDLEKKRieqekllaEENKNLREKLQQLQSSQKASYTKEIE 2642
Cdd:PRK03918 712 ELEKLEKAL--------ERVEELREKVKKYKALLKERALSKVG 746
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4341-4379 |
1.07e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 1.07e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1207141765 4341 LLEAQACTGGIIDPNTGEKFSVADAQNKGLVDKIMVDRI 4379
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1387-2144 |
1.11e-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: 71.64 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1387 EEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQ--------DVAVDSEKQKHNI 1458
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkekigELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1459 QRELQELKTLSEQEIKAKSQqveeallsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAvdaDKLRNAAQEEAEK 1538
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAE--------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL---EDLRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1539 LRKQVaEETQKKRKAEEELKRKSEAEKDaakekkkaledlEKFKLQAEEAERHLKQAELEKQrqIQVVEEvAKKTAATQL 1618
Cdd:TIGR02169 380 FAETR-DELKDYREKLEKLKREINELKR------------ELDRLQEELQRLSEELADLNAA--IAGIEA-KINELEEEK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1619 ESKQVALTArLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKEL---ETWRQKANEALRLRLQAEEEANKKTAA 1695
Cdd:TIGR02169 444 EDKALEIKK-QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELaeaEAQARASEERVRGGRAVEEVLKASIQG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1696 QEEAEKQKEEAKREakkRAKAEEAA----------------------LKQKEAAEMELGNQRKMAEETAKQKLAAEQELI 1753
Cdd:TIGR02169 523 VHGTVAQLGSVGER---YATAIEVAagnrlnnvvveddavakeaielLKRRKAGRATFLPLNKMRDERRDLSILSEDGVI 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1754 RLRADFEHAEQQ-----RTVLDDELqrLKNDVNSAVKQKKE-----LEEELIK---------VRKEMEILLQQKSKAEKE 1814
Cdd:TIGR02169 600 GFAVDLVEFDPKyepafKYVFGDTL--VVEDIEAARRLMGKyrmvtLEGELFEksgamtggsRAPRGGILFSRSEPAELQ 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1815 TMSNT----EKSKQLLESEAAKMRELAEEATKLRSVAE----EAKKQRQIAEEEAARQRAEAEKiLKEKLTAINEAtrlK 1886
Cdd:TIGR02169 678 RLRERleglKRELSSLQSELRRIENRLDELSQELSDASrkigEIEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQE---I 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1887 TEAEIALKEKEAENDRLKRKAEEEgyqRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETlkqrKVVEEEIHI 1966
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKL---EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI----EQKLNRLTL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1967 LKLNFEKASSGKQELElelkklkgIADETQKSKAKAEEEAEKFRKLALEEEkkrkeaeakVKQIQAAEEEAARQHKAAQE 2046
Cdd:TIGR02169 827 EKEYLEKEIQELQEQR--------IDLKEQIKSIEKEIENLNGKKEELEEE---------LEELEAALRDLESRLGDLKK 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2047 EVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVL------------------VQQNKDSMAQD--- 2105
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEdpkgedeeipeeelsledVQAELQRVEEEira 969
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1207141765 2106 ------KLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER 2144
Cdd:TIGR02169 970 lepvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
64-159 |
1.17e-11 |
|
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: 64.54 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 64 EAQRHITDLYEDLRDGHNLISLLEVLSGEtlpreRDVVRNSRLPrEKGRMRfhKLQNVQIALDFLKHRQV----KLVNIR 139
Cdd:cd21223 21 EFDFAVTNLAVDLRDGVRLCRLVELLTGD-----WSLLSKLRVP-AISRLQ--KLHNVEVALKALKEAGVlrggDGGGIT 92
|
90 100
....*....|....*....|
gi 1207141765 140 NDDIADGNPKLTLGLIWTII 159
Cdd:cd21223 93 AKDIVDGHREKTLALLWRII 112
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
179-278 |
1.34e-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: 63.90 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 179 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN---LENLEQAFSIAER-DLGVTRLL 254
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1207141765 255 DPEDVdVPHPDEKSIITYVSSMYD 278
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
40-156 |
1.39e-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: 64.37 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 40 ERDRvQKKTFTKWVNKHLVkhwkaeaQRHITDLYEDLRDGhnLIsLLEVLSGeTLPRERDVVRNSRLPREKGRMRFHKLQ 119
Cdd:cd21300 4 EGER-EARVFTLWLNSLDV-------EPAVNDLFEDLRDG--LI-LLQAYDK-VIPGSVNWKKVNKAPASAEISRFKAVE 71
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141765 120 NVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIW 156
Cdd:cd21300 72 NTNYAVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2046-2660 |
1.61e-11 |
|
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: 71.15 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2046 EEVGRLMKLAEEAKKQKEIAEKEAEKQV----ILVQEAAQKCSAAEQKAQnvlVQQNKDSMAQDKLKEEFEKAKKLAQEA 2121
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTlrsqLLTLCTPCMPDTYHERKQ---VLEKELKHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2122 EKAKDNAEKEAALLHKKAEEAE-RQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLkQEADSEMAKYKK 2200
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEElRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTEL-QSKMRSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2201 LAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQevsdaikqKAQVEDELSKVKIQMEDLLKLKLKIEKENQ 2280
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI--------SCQQHTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2281 ELMKKDKDNTKKLLEEEAENmkklAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQaIQEAAKLKAEAEKL 2360
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFR----DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL-QESAQSLKEREQQL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2361 QKQKDQAQVEAQK--LLEAKKEMQQRLDQETEGFQKSLEAERKRQLEitaeAEKLKVKVTQLSDAQSKAEEEAKKFKKQA 2438
Cdd:TIGR00618 476 QTKEQIHLQETRKkaVVLARLLELQEEPCPLCGSCIHPNPARQDIDN----PGPLTRRMQRGEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2439 DEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTI 2518
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2519 LQQSFFAEKETLLKKEKAIEEEKKKLEKQFED--EVKKAEALKAEQeRQRKLMEEERKKLQSAMDAAIKKQK-----EAE 2591
Cdd:TIGR00618 632 LHLQQCSQELALKLTALHALQLTLTQERVREHalSIRVLPKELLAS-RQLALQKMQSEKEQLTYWKEMLAQCqtllrELE 710
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141765 2592 EEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMTMVE 2660
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1941-2655 |
1.80e-11 |
|
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: 71.15 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1941 TELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASS-GKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLA--LEEE 2017
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTqkREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2018 KKRKEAEAKVKQIQAAEEEAARQ---HKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVIL--VQEAAQKCSAAEQKAQN 2092
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIEELRAQeavLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHteLQSKMRSRAKLLMKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2093 VLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKA---KDNAEKEAALLHK-KAEEAERQKKAAEAEAAKQAKAQEDAEKLRK 2168
Cdd:TIGR00618 333 HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAtsiREISCQQHTLTQHiHTLQQQKTTLTQKLQSLCKELDILQREQATI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2169 EAEKEASRRAEAEAAALKLKQEADSEMAKYKKLA-EKTLKQKSSVEEELVKVKVQLDETD---KQKSVLDVELKRLKQEV 2244
Cdd:TIGR00618 413 DTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAiTCTAQCEKLEKIHLQESAQSLKEREqqlQTKEQIHLQETRKKAVV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2245 SDAIKQKAQVEDELSKVKIQMEdLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQi 2324
Cdd:TIGR00618 493 LARLLELQEEPCPLCGSCIHPN-PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ- 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2325 AESDLAKQRElaekmleekkqaiqeaaKLKAEAEKLQKQKDQAQVEAQKLLEAKKemqqrldqetegfqKSLEAERKRQL 2404
Cdd:TIGR00618 571 SFSILTQCDN-----------------RSKEDIPNLQNITVRLQDLTEKLSEAED--------------MLACEQHALLR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2405 EITAEAEKLKVKVTQlsdaQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLE 2484
Cdd:TIGR00618 620 KLQPEQDLQDVRLHL----QQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYW 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2485 KEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLlkkekaieEEKKKLEKQFEDEVKKAEALKAEQER 2564
Cdd:TIGR00618 696 KEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAL--------NQSLKELMHQARTVLKARTEAHFNNN 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2565 QRKLMEEER-KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEI 2643
Cdd:TIGR00618 768 EEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
730
....*....|..
gi 1207141765 2644 QTDKVPEEELVQ 2655
Cdd:TIGR00618 848 THQLLKYEECSK 859
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1718-2624 |
1.88e-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: 70.87 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1718 EAALKQKEAAEMELGNQRKMAEETAKQklaaeqeLIRLRADFEHAEQQRTVLDD----ELQRLKNDVNSAVKQKKELEEE 1793
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQ-------LERLRREREKAERYQALLKEkreyEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1794 LIKVRKEMEILLQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEatklrsvaEEAKKQRQIAEEEAarQRAEAEKILK 1873
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRL----EEIEQLLEELNKKIKDLGEE--------EQLRVKEKIGELEA--EIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1874 EKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQ---AIEEKIGQLKKSSDTELDRQKKIV 1950
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEeleDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1951 EETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLaleeekkrkeaEAKVKQI 2030
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ-----------EWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2031 QAAEEEAARQHKAAQEEVGRLMKlaEEAKKQKEIAEKEAEKQVIlvqEAAQKCSAAEQKAQNVLVQQNKDSMAQ-DKLKE 2109
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEK--ELSKLQRELAEAEAQARAS---EERVRGGRAVEEVLKASIQGVHGTVAQlGSVGE 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2110 EFEKAKKLAQEAEKA----KDNAEKEAALLHKKAEEAERQKKAaeaeaakqakaqedaeKLRKEAEKEASRRAEAEAAAL 2185
Cdd:TIGR02169 536 RYATAIEVAAGNRLNnvvvEDDAVAKEAIELLKRRKAGRATFL----------------PLNKMRDERRDLSILSEDGVI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2186 KLKQEADSEMAKYKKlAEKTLKQKSSVEEELVKVKVQLDETdkQKSVLDVEL-----------KRLKQEVSDAIKQKAQV 2254
Cdd:TIGR02169 600 GFAVDLVEFDPKYEP-AFKYVFGDTLVVEDIEAARRLMGKY--RMVTLEGELfeksgamtggsRAPRGGILFSRSEPAEL 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2255 E---DELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAEnmkklaeeaarlnieaqeaarlRQIAESDLAK 2331
Cdd:TIGR02169 677 QrlrERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE----------------------IEQLEQEEEK 734
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2332 QRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLD----QETEGFQKSLEAERKRQLEIT 2407
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVSRIEARL 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2408 AEAEKlkvKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEvqrlqskQEADGLHKAIADLEKEK 2487
Cdd:TIGR02169 815 REIEQ---KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE-------EELEELEAALRDLESRL 884
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2488 EKLKKEAADLQKQSKEMANVQQEQ-LQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERqr 2566
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELeAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQR-- 962
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 2567 klMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLRE 2624
Cdd:TIGR02169 963 --VEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3495-3531 |
2.35e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.19 E-value: 2.35e-11
10 20 30
....*....|....*....|....*....|....*..
gi 1207141765 3495 LLDAQVATGGIIDPVNSHRLPNDVAIERGYFSKQLAK 3531
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQ 37
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1642-2626 |
3.31e-11 |
|
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: 70.20 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1642 QLQEEAEHLKKQQAEADKArEQAEKELETWRQKANE---ALRLRLQAEEE----ANKKTAAQEEAEKQKEEAKREAKKRA 1714
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKA-ESELKELEKKHQQLCEeknALQEQLQAETElcaeAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1715 KAEE------AALKQKEAAEMELGNQRKMAEETAKQKL-----AAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSA 1783
Cdd:pfam01576 85 EEEEersqqlQNEKKKMQQHIQDLEEQLDEEEAARQKLqlekvTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1784 VKQKKELEEE---LIKVRKEMEIL---LQQKSKAEKETMSNTEKSKQLLESEAAKMRElaeeatklrsvaEEAKKQRQIA 1857
Cdd:pfam01576 165 TSNLAEEEEKaksLSKLKNKHEAMisdLEERLKKEEKGRQELEKAKRKLEGESTDLQE------------QIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1858 EEEAARQRAEAEkiLKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRkvleDQAAQHKQAIEEKIGQLKK 1937
Cdd:pfam01576 233 ELRAQLAKKEEE--LQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAAR----NKAEKQRRDLGEELEALKT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1938 SSDTELDRQKkiVEETLKQRKvvEEEIHILKLNFEKASSGKQELELELKKLKGIA-DETQKSKAKAEEEAEKFRKLALEE 2016
Cdd:pfam01576 307 ELEDTLDTTA--AQQELRSKR--EQEVTELKKALEEETRSHEAQLQEMRQKHTQAlEELTEQLEQAKRNKANLEKAKQAL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2017 EKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQK-EIAEK----------------EAEKQVILVQEA 2079
Cdd:pfam01576 383 ESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRaELAEKlsklqselesvssllnEAEGKNIKLSKD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2080 AQKCSAAEQKAQNVLVQQNKDSMAQD----KLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEA----ERQKKAAEA 2151
Cdd:pfam01576 463 VSSLESQLQDTQELLQEETRQKLNLStrlrQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMkkklEEDAGTLEA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2152 EAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEAD-------------SEMAKYKKLAEKTLKQKSSVEEELVK 2218
Cdd:pfam01576 543 LEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDdllvdldhqrqlvSNLEKKQKKFDQMLAEEKAISARYAE 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2219 VKVQLDETDKQKSVLDVELKRlkqEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKkdkdnTKKLLEEEA 2298
Cdd:pfam01576 623 ERDRAEAEAREKETRALSLAR---ALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELER-----SKRALEQQV 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2299 ENMKKLAEEA---------ARL----NIEAQEAARLRQIAESD---------LAKQ-RELAEKMLEEKKQAIQEAA---- 2351
Cdd:pfam01576 695 EEMKTQLEELedelqatedAKLrlevNMQALKAQFERDLQARDeqgeekrrqLVKQvRELEAELEDERKQRAQAVAakkk 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2352 ------KLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ-------------ETEGFQKSLEAERKRQLEITAEAEK 2412
Cdd:pfam01576 775 leldlkELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEarasrdeilaqskESEKKLKNLEAELLQLQEDLAASER 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2413 LKVKVTQLSDA-QSKAEEEAKKFKKQADE---IKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKE 2488
Cdd:pfam01576 855 ARRQAQQERDElADEIASGASGKSALQDEkrrLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQ 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2489 KLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSF------FAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQ 2562
Cdd:pfam01576 935 KSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIaaleakIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDE 1014
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141765 2563 ERQRKLMEEERKKLQSAMDAAIKKQKEAEEE---MNGKQKEMQDLEKKRIEQEKLLAEENKNLREKL 2626
Cdd:pfam01576 1015 RRHADQYKDQAEKGNSRMKQLKRQLEEAEEEasrANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1462-1775 |
3.49e-11 |
|
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: 69.77 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1462 LQELKTLSEQEIKAKSQQVEEallSRTRIEEEIHIIRLQLETTMKQKNTAETELLQlRAKAVDADKLRNAAQEEAEKLRK 1541
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQ---ERLRQEKEEKAREVERRRKLEEAEKARQAEMD-RQAAIYAEQERMAMERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1542 QvaeetQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFK-----LQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAT 1616
Cdd:pfam17380 354 R-----QEERKRELERIRQEEIAMEISRMRELERLQMERQQknervRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1617 QLESKQVALTaRLEESLKNEQVMV----IQLQEEAEHLKKQQAEADKAREQAEKELETwRQKANEALRLRLQAEEEANK- 1691
Cdd:pfam17380 429 QEEARQREVR-RLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLELEKEKRD-RKRAEEQRRKILEKELEERKq 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1692 -------KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEmelgnQRKMAEETAKqklaAEQELIRLRADFEHAEQ 1764
Cdd:pfam17380 507 amieeerKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE-----RRRIQEQMRK----ATEERSRLEAMEREREM 577
|
330
....*....|.
gi 1207141765 1765 QRTVLDDELQR 1775
Cdd:pfam17380 578 MRQIVESEKAR 588
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1144-1935 |
4.56e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.71 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1144 ILNKYENQLREVNKVPVNEKEIEASQTQLQKLRSEAEgkqatfDRLEEELQRATEVNKRMSQLHSERDVElehyrqlvgn 1223
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELE------KRLEEIEQLLEELNKKIKDLGEEEQLR---------- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1224 LRERWQAVFAQIELRQRELDLLNRQMQAyresydwlirwiADAKQRQDKLhavpiggskglqeqltQEKKLLEEIEKNKD 1303
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELED------------AEERLAKLEA----------------EIDKLLAEIEELER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1304 KVEDCQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMESASddiiqeyvtLRTRYSELmtlsSQYIKFIIETQRR 1383
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------YREKLEKL----KREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1384 LQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEvskrqdvavdsEKQKHNIQRELQ 1463
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY-----------EQELYDLKEEYD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1464 ELktlsEQEIKAKSQQVEEALLSRTRIEEE-----------------IHIIRLQLETTMKQKNTAETELLQLRAKAVDAD 1526
Cdd:TIGR02169 480 RV----EKELSKLQRELAEAEAQARASEERvrggraveevlkasiqgVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1527 KLRNAAQEEAEKLRKQVAEET---QKKRKAEEELKRKSEAEKDAAKEKKKALEDLE-----KFKLQA-------EEAERH 1591
Cdd:TIGR02169 556 DDAVAKEAIELLKRRKAGRATflpLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafKYVFGDtlvvediEAARRL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1592 LKQAelekqRQIQVVEEVAKKT--------AATQLESKQVALTARLEESLKNEQVMVIQ---LQEEAEHLKKQQAEADKA 1660
Cdd:TIGR02169 636 MGKY-----RMVTLEGELFEKSgamtggsrAPRGGILFSRSEPAELQRLRERLEGLKRElssLQSELRRIENRLDELSQE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1661 REQAEKELETWRQKANealrlRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAE-EAALKQKEAAEMELgnqrKMAE 1739
Cdd:TIGR02169 711 LSDASRKIGEIEKEIE-----QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKElEARIEELEEDLHKL----EEAL 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1740 ETAKQKLaAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSaVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNT 1819
Cdd:TIGR02169 782 NDLEARL-SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1820 EKSKQLLESEAAK----MRELAEEATKLRSVAEEAKKQR---QIAEEEAARQRAEAEKILKEkltaineatrLKTEAEiA 1892
Cdd:TIGR02169 860 NGKKEELEEELEEleaaLRDLESRLGDLKKERDELEAQLrelERKIEELEAQIEKKRKRLSE----------LKAKLE-A 928
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1207141765 1893 LKEKEAENDRLKRKAEEEGYQRKVLEDQAAQhKQAIEEKIGQL 1935
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEEIPEEELSLEDVQAE-LQRVEEEIRAL 970
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1403-1860 |
8.34e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1403 AEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAvDSEKQKHNIQRELQELKtlSEQEIKAKSQQVEE 1482
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELR--EELEKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1483 ALLSRTRIEEEIHIIRLQLETtmkqkntAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKse 1562
Cdd:COG4717 130 LYQELEALEAELAELPERLEE-------LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1563 aEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQiQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVM--- 1639
Cdd:COG4717 201 -LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIagv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1640 ------VIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKkTAAQEEAEKQKEEAKREAKKR 1713
Cdd:COG4717 279 lflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP-EELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1714 AKAEEAALKQKEAAEMELGNQRKMA-EETAKQKLAAEQELIRLRADFEHAEQQ----------------RTVLDDELQRL 1776
Cdd:COG4717 358 ELEEELQLEELEQEIAALLAEAGVEdEEELRAALEQAEEYQELKEELEELEEQleellgeleellealdEEELEEELEEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1777 KNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsntekskQLLESEAAKMRELAEEATKLRSVAEEAKKQRQI 1856
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEEDGELAELL---------QELEELKAELRELAEEWAALKLALELLEEAREE 508
|
....
gi 1207141765 1857 AEEE 1860
Cdd:COG4717 509 YREE 512
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
179-277 |
8.86e-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: 61.60 E-value: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 179 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 258
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90
....*....|....*....
gi 1207141765 259 VdVPHPDEKSIITYVSSMY 277
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFH 102
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1429-1749 |
1.01e-10 |
|
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: 68.12 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1429 EANELKTKMKDEV-----SKRQDVAVDSEKQKH----NIQRELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRL 1499
Cdd:NF033838 51 SGNESQKEHAKEVeshleKILSEIQKSLDKRKHtqnvALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1500 QLETTMKQKNTAET----ELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakeKKKAL 1575
Cdd:NF033838 131 KKDTLEPGKKVAEAtkkvEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKE----------EAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1576 EDLEKFKlqAEEAERHLKQAELEKQRQIQV----VEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLK 1651
Cdd:NF033838 201 RDEEKIK--QAKAKVESKKAEATRLEKIKTdrekAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1652 KQQ-------------------------AEADKAREQAEKELETWRQK------ANEALRLRLQ-AEEEAN-KKTAAQEE 1698
Cdd:NF033838 279 KENdakssdssvgeetlpspslkpekkvAEAEKKVEEAKKKAKDQKEEdrrnypTNTYKTLELEiAESDVKvKEAELELV 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 1699 AEKQKEEAKREAKKRAKAEEAAlKQKEAAEME-LGNQRKMAEETAKQKLAAE 1749
Cdd:NF033838 359 KEEAKEPRNEEKIKQAKAKVES-KKAEATRLEkIKTDRKKAEEEAKRKAAEE 409
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3828-3866 |
1.29e-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: 1.29e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1207141765 3828 LLEAQVATGGLMDPEYYFRLPIDIAMQRGYMNKETSERI 3866
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2033-2390 |
1.47e-10 |
|
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: 67.23 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2033 AEEEAARQHKAAQEEVGRLMK-LAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVL----VQQNKDSMAQDKL 2107
Cdd:pfam07888 67 DREQWERQRRELESRVAELKEeLRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEArireLEEDIKTLTQRVL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2108 KEEfekakklaQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKL 2187
Cdd:pfam07888 147 ERE--------TELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2188 KQEADSEMAKYKKLaEKTLKQKSSVEEELvkvkvqldETDKQKSVLdvelkrLKQEVSDAIKQKAQVEDELSKVKI---Q 2264
Cdd:pfam07888 219 TQKLTTAHRKEAEN-EALLEELRSLQERL--------NASERKVEG------LGEELSSMAAQRDRTQAELHQARLqaaQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2265 MEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKK 2344
Cdd:pfam07888 284 LTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESR 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1207141765 2345 QAIQEaakLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETE 2390
Cdd:pfam07888 364 RELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1258-1931 |
1.93e-10 |
|
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: 67.44 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1258 WLIRWIADAKQRQDKLH---AVPIGGSKGLQE-QLTQEK---KLLEEIEKNKDKV--------------EDCQKFAKGYI 1316
Cdd:pfam05483 93 WKVSIEAELKQKENKLQenrKIIEAQRKAIQElQFENEKvslKLEEEIQENKDLIkennatrhlcnllkETCARSAEKTK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1317 DAIKDYELQLVTYKAL---VEPIASPLKKAKMEsASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRR-----LQDEE 1388
Cdd:pfam05483 173 KYEYEREETRQVYMDLnnnIEKMILAFEELRVQ-AENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQvslllIQITE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1389 KAAEKLKEEERKKMAEMQA-ELEKQKQLAETHAKAIAKAE----QEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQ 1463
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKAnQLEEKTKLQDENLKELIEKKdhltKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1464 ELKTLSEQEIKAKSQQ---VEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLR 1540
Cdd:pfam05483 332 EKEAQMEELNKAKAAHsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1541 KQVAE------ETQKKRKAEEELKRKSEAEKdaakekkkaledlekFKLQAEEAERHLKQAEL-----EKQRQIQVVEEV 1609
Cdd:pfam05483 412 KILAEdeklldEKKQFEKIAEELKGKEQELI---------------FLLQAREKEIHDLEIQLtaiktSEEHYLKEVEDL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1610 akKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEA 1689
Cdd:pfam05483 477 --KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1690 NKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVL 1769
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1770 DDELQRLKNDVNSAvkqKKELEEELIKVRKEMEIllqqKSKAEKETMSNTEKSKQlleseaakmreLAEEATKLRSVAEE 1849
Cdd:pfam05483 635 EIKVNKLELELASA---KQKFEEIIDNYQKEIED----KKISEEKLLEEVEKAKA-----------IADEAVKLQKEIDK 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1850 aKKQRQIAEEEA--ARQRAEAEKILKEKLTAI-------NEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQ 1920
Cdd:pfam05483 697 -RCQHKIAEMVAlmEKHKHQYDKIIEERDSELglyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKME 775
|
730
....*....|.
gi 1207141765 1921 AAQHKQAIEEK 1931
Cdd:pfam05483 776 AKENTAILKDK 786
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2360-2628 |
2.70e-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: 67.07 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2360 LQKQKDQAQVEAQKLLEakKEMQQRLDQETEgfQKSLEAERKRQLEitaEAEKLKvKVTQLSDAQSKAEEEAKKFKKQAD 2439
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE--KMEQERLRQEKE--EKAREVERRRKLE---EAEKAR-QAEMDRQAAIYAEQERMAMERERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2440 EIKIRLQETEKHTS-----------EKHTVVEKLEVQRLQS----KQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEM 2504
Cdd:pfam17380 350 LERIRQEERKRELErirqeeiameiSRMRELERLQMERQQKnervRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2505 ANVQQEQLQQektiLQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQ-------RKLMEEERKKLQ 2577
Cdd:pfam17380 430 EEARQREVRR----LEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRkraeeqrRKILEKELEERK 505
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1207141765 2578 SAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQ 2628
Cdd:pfam17380 506 QAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQE 556
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1002-1789 |
2.86e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.02 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1002 EQEPALIQKDSTSGEQDESVCKSyitQIKDLRLRLEGCESRTVN----RLRQMVDKEPL-KACTQRATEQKKVQTELEGI 1076
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLER---SIAEKERELEDAEERLAKleaeIDKLLAEIEELeREIEEERKRRDKLTEEYAEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1077 KKDLDKVVEKSEAVLATSQQSSSAPV-LRSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQ----GAEDILNKYENQ 1151
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKdYREKLEKLKREINELKRELDRLQEELQRLSEELADLNaaiaGIEAKINELEEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1152 LREVN-KVPVNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELqraTEVNKRMSQLHSERDV---ELEHYRQLVGNLRER 1227
Cdd:TIGR02169 443 KEDKAlEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL---SKLQRELAEAEAQARAseeRVRGGRAVEEVLKAS 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1228 WQAVFAQIelrqreldllnRQMQAYRESYDWLIRWIADAKqrqdkLHAVPIGGSKGLQE--QLTQEKKL--LEEIEKNKD 1303
Cdd:TIGR02169 520 IQGVHGTV-----------AQLGSVGERYATAIEVAAGNR-----LNNVVVEDDAVAKEaiELLKRRKAgrATFLPLNKM 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1304 KVEDCQKfAKGYIDAIKDYELQLVTYKALVEPI-----ASPLKKAKMESASDDIIQ-EYVTLRTRYSE---LMTLSSQYI 1374
Cdd:TIGR02169 584 RDERRDL-SILSEDGVIGFAVDLVEFDPKYEPAfkyvfGDTLVVEDIEAARRLMGKyRMVTLEGELFEksgAMTGGSRAP 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1375 KFIIETQRRLQDEEkaaeklkeeerkkmAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQ 1454
Cdd:TIGR02169 663 RGGILFSRSEPAEL--------------QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1455 KHNIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVdadklrnaaQE 1534
Cdd:TIGR02169 729 EQEEEKLKERLEEL-EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEI---------QA 798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1535 EAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERhlKQAELEKQrqiqvveevaKKTA 1614
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK--EIENLNGK----------KEEL 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1615 ATQLESKQVALtARLEESLKNeqvmviqLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEaLRLRLQAEEEANK--- 1691
Cdd:TIGR02169 867 EEELEELEAAL-RDLESRLGD-------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSE-LKAKLEALEEELSeie 937
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1692 KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMelgnqrkmaeetakqklAAEQELIRLRADFEHAEQQRTVLDD 1771
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNM-----------------LAIQEYEEVLKRLDELKEKRAKLEE 1000
|
810
....*....|....*...
gi 1207141765 1772 ELQRLKNDVNSAVKQKKE 1789
Cdd:TIGR02169 1001 ERKAILERIEEYEKKKRE 1018
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1515-1945 |
3.34e-10 |
|
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: 66.90 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1515 LLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELK------RKSEAEKDAAKEKKKALEDLEKFKLQAEE- 1587
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQaasdhlNLVQTALRQQEKIERYQEDLEELTERLEEq 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1588 ----AERHLKQAELEKQRQiQVVEEVakKTAATQLESKQVALTARLEESLKNEQVmvIQLQEEAEHLkkqQAEADKAREQ 1663
Cdd:COG3096 367 eevvEEAAEQLAEAEARLE-AAEEEV--DSLKSQLADYQQALDVQQTRAIQYQQA--VQALEKARAL---CGLPDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1664 AEKELETWRQKANEALRLRLQAEEEANkktaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMElgnqRKMAEETAK 1743
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLS----------------VADAARRQFEKAYELVCKIAGEVE----RSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1744 qklaaeqELIRLRADFEHAEQQRTVLDDELQRLkndvnsavkqkkeleEELIKVRKEMEILLQQKSKAEKETMSNTEKSK 1823
Cdd:COG3096 499 -------ELLRRYRSQQALAQRLQQLRAQLAEL---------------EQRLRQQQNAERLLEEFCQRIGQQLDAAEELE 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1824 QLLESEAAKMRELAEEAtklRSVAEEAKKQRQiAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRL 1903
Cdd:COG3096 557 ELLAELEAQLEELEEQA---AEAVEQRSELRQ-QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAM 632
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1207141765 1904 KRKAEEEgYQRKVLEDQAAQHKQAIEEKIGQLKK---SSDTELDR 1945
Cdd:COG3096 633 QQLLERE-REATVERDELAARKQALESQIERLSQpggAEDPRLLA 676
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1374-2088 |
4.51e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1374 IKFIIETQRRLQDEE-------------------------KAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQ 1428
Cdd:TIGR02169 193 IDEKRQQLERLRRERekaeryqallkekreyegyellkekEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1429 EANELKTKMKDEVSKRQ--------DVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQqveeallsRTRIEEEIHIIRLQ 1500
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQlrvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAE--------IDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1501 LETTMKQKNTAETELLQLRAKavdADKLRNAAQEEAEKLRKQVaEETQKKRKAEEELKRKSEAEKDaakekkkaledlEK 1580
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEE---LEDLRAELEEVDKEFAETR-DELKDYREKLEKLKREINELKR------------EL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1581 FKLQAEEAERHLKQAELEKqrQIQVVEEvAKKTAATQLESKQVALTArLEESLKNEQVMVIQLQEEAEHLKKQQAEADKA 1660
Cdd:TIGR02169 409 DRLQEELQRLSEELADLNA--AIAGIEA-KINELEEEKEDKALEIKK-QEWKLEQLAADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1661 REQAEKEL---ETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREakkRAKAEEAA----------------- 1720
Cdd:TIGR02169 485 LSKLQRELaeaEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGER---YATAIEVAagnrlnnvvveddavak 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1721 -----LKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQ-----RTVLDDELqrLKNDVNSAVKQKKE- 1789
Cdd:TIGR02169 562 eaielLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafKYVFGDTL--VVEDIEAARRLMGKy 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1790 ----LEEELIK---------VRKEMEILLQQKSKAEKETMSNT----EKSKQLLESEAAKMRELAEEATKLRSVAE---- 1848
Cdd:TIGR02169 640 rmvtLEGELFEksgamtggsRAPRGGILFSRSEPAELQRLRERleglKRELSSLQSELRRIENRLDELSQELSDASrkig 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1849 EAKKQRQIAEEEAARQRAEAEKiLKEKLTAINEAtrlKTEAEIALKEKEAENDRLKRKAEEEgyqRKVLEDQAAQHKQAI 1928
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQE---IENVKSELKELEARIEELEEDLHKL---EEALNDLEARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1929 EEKIGQLKKSSDTELDRQKKIVEETlkqrKVVEEEIHILKLNFEKASSGKQELElelkklkgIADETQKSKAKAEEEAEK 2008
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREI----EQKLNRLTLEKEYLEKEIQELQEQR--------IDLKEQIKSIEKEIENLN 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2009 FRKLALeeekkrkeaEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQ 2088
Cdd:TIGR02169 861 GKKEEL---------EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1532-1751 |
6.91e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.44 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1532 AQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaledLEKFKLQA-EEAERHLKQAELEKQRQIQVVEEVA 1610
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQ-----------------LEKERLAAqEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1611 KKTAATQLESKQVAltARLEESLKneqvmviqlQEEAEHLKKQQAEAD-KAREQAEKELETWRQKANEALRlRLQAEEEA 1689
Cdd:PRK09510 140 KAAAAAKAKAEAEA--KRAAAAAK---------KAAAEAKKKAEAEAAkKAAAEAKKKAEAEAAAKAAAEA-KKKAEAEA 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 1690 NKKTaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQE 1751
Cdd:PRK09510 208 KKKA-------------AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2088-2471 |
7.05e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 65.53 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2088 QKAQNVLVQQNK-DSMAQDKLKEEFEKakkLAQEAEKAKDNAEKEAAllhkKAEEAERQKKAAEAEAAKQAKAQEDAEKL 2166
Cdd:pfam17380 281 QKAVSERQQQEKfEKMEQERLRQEKEE---KAREVERRRKLEEAEKA----RQAEMDRQAAIYAEQERMAMERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2167 RKEAEKEASRRAEaeaaalklKQEADSEMAKYKKLAektlkqkssveeelvkvKVQLDETDKQKsvldvelkRLKQEVSD 2246
Cdd:pfam17380 354 RQEERKRELERIR--------QEEIAMEISRMRELE-----------------RLQMERQQKNE--------RVRQELEA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2247 AIKQKAQVEDELSKVKIQMEDllklklkiekenQELMKKDKDNTKKlleeeaENMKKLAEEAARlnieaqEAARLRQiae 2326
Cdd:pfam17380 401 ARKVKILEEERQRKIQQQKVE------------MEQIRAEQEEARQ------REVRRLEEERAR------EMERVRL--- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2327 SDLAKQRElaekmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEakKEMQQRLdqetegfQKSLEAERKRQLeI 2406
Cdd:pfam17380 454 EEQERQQQ-----VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE--KELEERK-------QAMIEEERKRKL-L 518
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141765 2407 TAEAEKlkvKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQ 2471
Cdd:pfam17380 519 EKEMEE---RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1579-1927 |
8.42e-10 |
|
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: 65.42 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1579 EKFKLQAEEAERHLK------QAELEKQRQIQVVE----------------EVAKKTAATQLESK-QVALTARLEESLKN 1635
Cdd:NF033838 54 ESQKEHAKEVESHLEkilseiQKSLDKRKHTQNVAlnkklsdikteylyelNVLKEKSEAELTSKtKKELDAAFEQFKKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1636 eqvmVIQLQEEAEHLKKQQAEAD-KAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRA 1714
Cdd:NF033838 134 ----TLEPGKKVAEATKKVEEAEkKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1715 KAEEAAlKQKEAAEME-LGNQRKMAEETAKQKLAAEQE--LIRLRADFEHAEQQRTVLDDELQRL------KNDVNS--- 1782
Cdd:NF033838 210 KAKVES-KKAEATRLEkIKTDREKAEEEAKRRADAKLKeaVEKNVATSEQDKPKRRAKRGVLGEPatpdkkENDAKSsds 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1783 ----------AVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSkqlLESEAAKMRELAEEAtKLRSVAEEAKK 1852
Cdd:NF033838 289 svgeetlpspSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKT---LELEIAESDVKVKEA-ELELVKEEAKE 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141765 1853 QRQIAEEEAARQRAEAEKIlkekltainEATRL-KTEAEIALKEKEAendrlKRKAEEEgyqRKVLEDQAAQHKQA 1927
Cdd:NF033838 365 PRNEEKIKQAKAKVESKKA---------EATRLeKIKTDRKKAEEEA-----KRKAAEE---DKVKEKPAEQPQPA 423
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2200-2631 |
9.62e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 9.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2200 KLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEdllklklkieken 2279
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE------------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2280 qelmkkdkdntkklLEEEAENMKKL-AEEAARLNIEAQEAARLRQIAEsdlaKQRELAEKMLEEKKQAIQEAAKLKAEAE 2358
Cdd:COG4717 141 --------------LAELPERLEELeERLEELRELEEELEELEAELAE----LQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2359 KLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQ-SKAEEEAKKFKKQ 2437
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLlSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2438 ADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKT 2517
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2518 ILQQSFFAEKETLLKKEKAIEEEK-KKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQ-KEAEEEMN 2595
Cdd:COG4717 363 LQLEELEQEIAALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELE 442
|
410 420 430
....*....|....*....|....*....|....*...
gi 1207141765 2596 GKQKEMQDL--EKKRIEQEKLLAEENKNLREKLQQLQS 2631
Cdd:COG4717 443 ELEEELEELreELAELEAELEQLEEDGELAELLQELEE 480
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1579-2353 |
1.01e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 65.24 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1579 EKFKLQAEEAERHLKQAELekqrqIQVVEEVAKKTAATQLESKQVaLTARLEESLKNEQVMVIQLQEEAEHLKKQQAEAD 1658
Cdd:pfam12128 214 PKSRLNRQQVEHWIRDIQA-----IAGIMKIRPEFTKLQQEFNTL-ESAELRLSHLHFGYKSDETLIASRQEERQETSAE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1659 KAREQAEKELEtWRQKANEaLRLRLQAEEEANKKTAAQEEAEKQKEEAKREA---KKRAKAEEAALKQKEAAEME----- 1730
Cdd:pfam12128 288 LNQLLRTLDDQ-WKEKRDE-LNGELSAADAAVAKDRSELEALEDQHGAFLDAdieTAAADQEQLPSWQSELENLEerlka 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1731 -LGNQRKMAEETAKQKLAAEQELIR--------LRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKK---ELEEELIKVR 1798
Cdd:pfam12128 366 lTGKHQDVTAKYNRRRSKIKEQNNRdiagikdkLAKIREARDRQLAVAEDDLQALESELREQLEAGKlefNEEEYRLKSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1799 KEMEILLQQKSKAEKETMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTA 1878
Cdd:pfam12128 446 LGELKLRLNQATATPELLLQLENFDERIE----RAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSA 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1879 INEATRLKTEAEIALKEkeaendrlkrkaeeegyqrkVLEDQAAQHKQAIEEKIgqlkkssDTELDRQKKIVEETLKQRK 1958
Cdd:pfam12128 522 LDELELQLFPQAGTLLH--------------------FLRKEAPDWEQSIGKVI-------SPELLHRTDLDPEVWDGSV 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1959 VVEEEIHILKLNFEKAS-----SGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKlaleeekkrkeaeaKVKQIQAA 2033
Cdd:pfam12128 575 GGELNLYGVKLDLKRIDvpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANG--------------ELEKASRE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2034 EEEAARQHKAAQEEVGRL--MKLAEEAKKQKEIAEKEAEKQVILVQEAAQKcSAAEQKAQNVLVQQNKD----SMAQDKL 2107
Cdd:pfam12128 641 ETFARTALKNARLDLRRLfdEKQSEKDKKNKALAERKDSANERLNSLEAQL-KQLDKKHQAWLEEQKEQkreaRTEKQAY 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2108 KEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER------------QKKAAEAEAAKQAKAQEDAEKLRKEA-EKEA 2174
Cdd:pfam12128 720 WQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYkrdlaslgvdpdVIAKLKREIRTLERKIERIAVRRQEVlRYFD 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2175 SRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQK--- 2251
Cdd:pfam12128 800 WYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKeda 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2252 --AQVEDELSKVKIQMED-LLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNieaqeAARLRQIAESD 2328
Cdd:pfam12128 880 nsEQAQGSIGERLAQLEDlKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREEDHYQN-----DKGIRLLDYRK 954
|
810 820
....*....|....*....|....*.
gi 1207141765 2329 LAKQRE-LAEKMLEEKKQAIQEAAKL 2353
Cdd:pfam12128 955 LVPYLEqWFDVRVPQSIMVLREQVSI 980
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2283-2445 |
1.06e-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: 63.71 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2283 MKKDKDNTKKLLEEEAENMKK--LAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKL 2360
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAEEAEKqrAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2361 QKQKDQAQveAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEIT--AEAEKLKVKVTQlsdAQSKAEEEAKKFKKQA 2438
Cdd:TIGR02794 142 RKAKEEAA--KQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEakAKAEEAKAKAEA---AKAKAAAEAAAKAEAE 216
|
....*..
gi 1207141765 2439 DEIKIRL 2445
Cdd:TIGR02794 217 AAAAAAA 223
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1531-1964 |
1.15e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1531 AAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVA 1610
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1611 KKTAATQLESKQVALTARLEESLKNEqvmviqlQEEAEHLKKQQAEADKAREQAEKELETWRQKANEaLRLRLQAEEEAN 1690
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEK-------AEEYIKLSEFYEEYLDELREIEKRLSRLEEEING-IEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1691 KKTAAQEEAEKQKEEAKREAKKRAKAEEAALK--------QKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHA 1762
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAkkeelerlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1763 EQQRTVLDDELQRLKNDVNSAVKQKKELEE------------ELIKVRKEMEILLQQKSKAEKEtMSNTEKsKQLLESEA 1830
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKCPVCGRELTEehrkelleeytaELKRIEKELKEIEEKERKLRKE-LRELEK-VLKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1831 AKMRELAEEATKLRSV--------AEEAKKQRQIAEEEAARQRAEAeKILKEKLTAINEATRLKTEAEIALKEKEAENDR 1902
Cdd:PRK03918 496 IKLKELAEQLKELEEKlkkynleeLEKKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEELKKKLAELEKKLDELEEELAE 574
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141765 1903 LKRKAEEEGYqrKVLEDqaaqhkqaIEEKIGQLKKSSD--TELDRQKKIVEETLKQRKVVEEEI 1964
Cdd:PRK03918 575 LLKELEELGF--ESVEE--------LEERLKELEPFYNeyLELKDAEKELEREEKELKKLEEEL 628
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2841-2879 |
1.21e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 56.18 E-value: 1.21e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1207141765 2841 LLDCQYATGGIIDPVNSHHVPVQLACTQGQLDEDLSKIL 2879
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1642-1969 |
1.76e-09 |
|
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: 64.37 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1642 QLQEEAEHLKKQ---QAEADKAREQAEK----ELETWRQKANEAlRLRLQAEEEANKKTAAQEEAEKQKEEAKREaKKRA 1714
Cdd:pfam17380 288 QQQEKFEKMEQErlrQEKEEKAREVERRrkleEAEKARQAEMDR-QAAIYAEQERMAMERERELERIRQEERKRE-LERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1715 KAEEAALKQKEAAEME-LGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQK--KELE 1791
Cdd:pfam17380 366 RQEEIAMEISRMRELErLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRleEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1792 EELIKVRKEmEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEeaaRQRAEAEKI 1871
Cdd:pfam17380 446 REMERVRLE-EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEE---RKRKLLEKE 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1872 LKEKLTAINEATRLKTEAEIALKEKEAENDR----LKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQK 1947
Cdd:pfam17380 522 MEERQKAIYEEERRREAEEERRKQQEMEERRriqeQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIK 601
|
330 340
....*....|....*....|..
gi 1207141765 1948 KIVEETLKQRKVVEEEIHILKL 1969
Cdd:pfam17380 602 PIYRPRISEYQPPDVESHMIRF 623
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2189-2410 |
1.96e-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: 63.24 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2189 QEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDL 2268
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2269 LKLKLKIEKENQElmkkDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQ 2348
Cdd:COG4942 117 GRQPPLALLLSPE----DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 2349 EAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQetegfqksLEAERKRQLEITAEA 2410
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR--------LEAEAAAAAERTPAA 246
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1489-1844 |
1.99e-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: 64.32 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1489 RIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKL-------RNAAQEEAEKLRKQVAEETQKKRKAEEELKRKS 1561
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiekeIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1562 EAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAEL-EKQRQIQVVEEVAkktaatqleSKQVALTARLEESLKNEQVMV 1640
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEV---------SRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1641 IQLQEEAEHLKKQQAEADKAREQAEKELetwrqkanEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAA 1720
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEI--------ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1721 LKQKEaaemelgNQRKMAEETAKQKLAaeqeliRLRADFEHAEQQRTVLDDELQRLKNDVNSA------VKQKKELEEEL 1794
Cdd:TIGR02169 901 LERKI-------EELEAQIEKKRKRLS------ELKAKLEALEEELSEIEDPKGEDEEIPEEElsledvQAELQRVEEEI 967
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1795 IKVrKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLR 1844
Cdd:TIGR02169 968 RAL-EPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1134-1859 |
2.17e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1134 VIRSTQGAEDILNKYENqLREVnkvpvnEKEIEASQTQLQKLRSEAEGKQatfDRLEEELQRATEVNKRMSQLHSERDvE 1213
Cdd:PRK03918 150 VVRQILGLDDYENAYKN-LGEV------IKEIKRRIERLEKFIKRTENIE---ELIKEKEKELEEVLREINEISSELP-E 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1214 LEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYdwlirwiadakqrqdklhavpiggsKGLQEQLTQEKK 1293
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI-------------------------RELEERIEELKK 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1294 LLEEIEKNKDKVEDCQKFAKGYIDAIKDYElqlvtykalvepiasplkkaKMESASDDIIQEYVTLRTRYSELmtlssqy 1373
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYE--------------------EYLDELREIEKRLSRLEEEINGI------- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1374 ikfiietQRRLQDEEKaaeklkeeerkkMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKdevskrqdvavdsek 1453
Cdd:PRK03918 327 -------EERIKELEE------------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE--------------- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1454 qkhNIQRELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAV---------D 1524
Cdd:PRK03918 373 ---ELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPvcgrelteeH 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1525 ADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRkseaeKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRqiq 1604
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELRE-----LEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELE--- 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1605 vveevAKKTAATQLESKQVALTARLeESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQ 1684
Cdd:PRK03918 522 -----KKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLK 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1685 AEEEANKKTAaqeeaekqkeeakrEAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQ 1764
Cdd:PRK03918 596 ELEPFYNEYL--------------ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1765 QRtvLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILlqqksKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLR 1844
Cdd:PRK03918 662 EE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKL-----KEELEEREKAKKELEKLEKALERVEELREKVKKYK 734
|
730
....*....|....*..
gi 1207141765 1845 SVAEEA--KKQRQIAEE 1859
Cdd:PRK03918 735 ALLKERalSKVGEIASE 751
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4417-4455 |
2.26e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 55.41 E-value: 2.26e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1207141765 4417 FLEVQYLTGGLIEPDVTGRVSLDEAVRKGSLDARTAQKL 4455
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
177-274 |
2.31e-09 |
|
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: 58.16 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGVTRLLD 255
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90
....*....|....*....
gi 1207141765 256 PEDVDVPHPDEKSIITYVS 274
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLS 106
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
46-159 |
2.53e-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: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 46 KKTFTKWVNKHL-----VKHWKAEAQRHItDLYEDLRDGHNLISLLEVLSGETLPrERdvvrnsRLPREKGRMRFHKLQN 120
Cdd:cd21217 3 KEAFVEHINSLLaddpdLKHLLPIDPDGD-DLFEALRDGVLLCKLINKIVPGTID-ER------KLNKKKPKNIFEATEN 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141765 121 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 159
Cdd:cd21217 75 LNLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
944-1752 |
2.70e-09 |
|
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: 63.84 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 944 KTLRVEEYRLTLKNLEQHYQAFLRDSQDSGLFGADDRMQAENSYNKATQHYDNLLRSVEQEPALIQKDSTSGEQDESVCK 1023
Cdd:pfam02463 217 EKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1024 SYITQIKDLRLRLEGCESRTVNRLRQMVDKEplkactqraTEQKKVQTELEGIKKDLDKVVEKSEAVLATSQQSSSAPVL 1103
Cdd:pfam02463 297 ELKSELLKLERRKVDDEEKLKESEKEKKKAE---------KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1104 RSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQGAEDILNKYENQLREVNKVpvNEKEIEASQTQLQKLRSEAEGKQ 1183
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLK--EEKKEELEILEEEEESIELKQGK 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1184 ATFDRLEEELQRATEVNKRMS------QLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAY----- 1252
Cdd:pfam02463 446 LTEEKEELEKQELKLLKDELElkksedLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggrii 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1253 RESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEE----------IEKNKDKVEDCQKFAKGYIDAIKDY 1322
Cdd:pfam02463 526 SAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALtelplgarklRLLIPKLKLPLKSIAVLEIDPILNL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1323 EL---------QLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEK 1393
Cdd:pfam02463 606 AQldkatleadEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1394 LKEEERkkmAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQdvAVDSEKQKHNIQRELQELKTLSEQEI 1473
Cdd:pfam02463 686 ESELAK---EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI--NEELKLLKQKIDEEEEEEEKSRLKKE 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1474 KAKSQQVEEALLSRTRIEEEIHIIRLQLEttmKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKA 1553
Cdd:pfam02463 761 EKEEEKSELSLKEKELAEEREKTEKLKVE---EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1554 EEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESL 1633
Cdd:pfam02463 838 LALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1634 KNEQVMV------IQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRL------RLQAEEEANKKTAAQEEAEK 1701
Cdd:pfam02463 918 EIEERIKeeaeilLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEElgkvnlMAIEEFEEKEERYNKDELEK 997
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1207141765 1702 QKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQEL 1752
Cdd:pfam02463 998 ERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAEL 1048
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
40-164 |
4.84e-09 |
|
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: 57.70 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 40 ERDRVQKKTFTKWVNKHLVkhwkaeaQRHITDLYEDLRDGHNLISLLEVLSgetLPRERDVVRNSRLPREKGRMRfhKLQ 119
Cdd:cd21331 18 EGETREERTFRNWMNSLGV-------NPHVNHLYGDLQDALVILQLYEKIK---VPVDWNKVNKPPYPKLGANMK--KLE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1207141765 120 NVQIALDFLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 164
Cdd:cd21331 86 NCNYAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2105-2624 |
4.92e-09 |
|
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: 62.73 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2105 DKLKEEFEKAKKLAQEAEKAKD-------NAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRR 2177
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDkflteikKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2178 AEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEE---ELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQ- 2253
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKkqqEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQn 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2254 ------VEDELSKVKIQMEDLLKLKlkiekeNQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARL---RQI 2324
Cdd:TIGR04523 280 nkkikeLEKQLNQLKSEISDLNNQK------EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLkkeLTN 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2325 AESD-LAKQRELAEKmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQveaQKLLEAKKEMQQrLDQETEGFQKSLEAERKRQ 2403
Cdd:TIGR04523 354 SESEnSEKQRELEEK-QNEIEKLKKENQSYKQEIKNLESQINDLE---SKIQNQEKLNQQ-KDEQIKKLQQEKELLEKEI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2404 LEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADL 2483
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2484 EKEKEklkkeaaDLQKQSKEMaNVQQEQLQQEKTILQQSFFAEKETLLKKekaieeekkklekqfeDEVKKAEALKAE-Q 2562
Cdd:TIGR04523 509 EEKVK-------DLTKKISSL-KEKIEKLESEKKEKESKISDLEDELNKD----------------DFELKKENLEKEiD 564
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 2563 ERQRKLmeeerKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLRE 2624
Cdd:TIGR04523 565 EKNKEI-----EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1321-1968 |
4.95e-09 |
|
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: 62.82 E-value: 4.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1321 DYELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKE---E 1397
Cdd:pfam05483 38 DPAFQKLNFLPMLEQVANSGDCHYQEGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKiieA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1398 ERKKMAEMQAELEKqkqlaethakaiakaeqeaneLKTKMKDEVSKRQDVAVDSEKQKHnIQRELQELKTLSEQEIKAKS 1477
Cdd:pfam05483 118 QRKAIQELQFENEK---------------------VSLKLEEEIQENKDLIKENNATRH-LCNLLKETCARSAEKTKKYE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1478 QQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETEL-LQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEE 1556
Cdd:pfam05483 176 YEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMhFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1557 LKRKSEAEKDAAKEKKKALedlEKFKLQAEeaerHLKQAELEKQRQIQVVEEVakKTAATQLESKQVAltarLEESLKNE 1636
Cdd:pfam05483 256 MKDLTFLLEESRDKANQLE---EKTKLQDE----NLKELIEKKDHLTKELEDI--KMSLQRSMSTQKA----LEEDLQIA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1637 QVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRL---RLQAEEEANKKTAAQEEAEKQKEEAKREAKKR 1713
Cdd:pfam05483 323 TKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTeqqRLEKNEDQLKIITMELQKKSSELEEMTKFKNN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1714 AKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRL----RADFEHAEQQRTVLD-------DELQRLKNDVNS 1782
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKtseehylKEVEDLKTELEK 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1783 AVKQKKELEEELIKVRKEMEILLQQKS------KAEKETMSNTEKSKQ--------LLESEAAKMRELAEEATKLRSVAE 1848
Cdd:pfam05483 483 EKLKNIELTAHCDKLLLENKELTQEASdmtlelKKHQEDIINCKKQEErmlkqienLEEKEMNLRDELESVREEFIQKGD 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1849 EAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIA---LKEKEAENDRLKRKAEEEGYQRKV-------LE 1918
Cdd:pfam05483 563 EVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknIEELHQENKALKKKGSAENKQLNAyeikvnkLE 642
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1919 DQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILK 1968
Cdd:pfam05483 643 LELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1501-1745 |
6.77e-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: 61.01 E-value: 6.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1501 LETTMKQKNTAETELLQLRAKAVDADKlrnaAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaledlEK 1580
Cdd:TIGR02794 38 IQAVLVDPGAVAQQANRIQQQKKPAAK----KEQERQKKLEQQAEEAEKQRAAEQARQKE------------------LE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1581 FKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNeqvmviqlQEEAEHLKKQQAEADKA 1660
Cdd:TIGR02794 96 QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--------QAEEEAKAKAAAEAKKK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1661 REQAEKELETWRQKANEALRlRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAalkQKEAAEMELGNQRKMAEE 1740
Cdd:TIGR02794 168 AEEAKKKAEAEAKAKAEAEA-KAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEA---ERKADEAELGDIFGLASG 243
|
....*
gi 1207141765 1741 TAKQK 1745
Cdd:TIGR02794 244 SNAEK 248
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4339-4376 |
8.13e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 53.64 E-value: 8.13e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1207141765 4339 QRLLEAQACTGGIIDPNTGEKFSVADAQNKGLVDKIMV 4376
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1406-1947 |
9.21e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 62.16 E-value: 9.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1406 QAELEKQKQLAETHAKAIAKAEQEANELKTKMKDE-VSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEAL 1484
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1485 LsRTRIEEEIHIIRL-QLETTMKQKNTAETELLQLRAKavdaDKLRNAAQEEAEKLRKQVaeetqkkrkaeEELKRksea 1563
Cdd:pfam12128 433 L-EFNEEEYRLKSRLgELKLRLNQATATPELLLQLENF----DERIERAREEQEAANAEV-----------ERLQS---- 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1564 ekdaakekkkaleDLEKFKLQAEEAERHLKQAELEKQRQiqvveevakKTAATQLESKQVALTARLEESLKNEqvmviqL 1643
Cdd:pfam12128 493 -------------ELRQARKRRDQASEALRQASRRLEER---------QSALDELELQLFPQAGTLLHFLRKE------A 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1644 QEEAEHLKKQQAEADKAREQAEKELETWRQKANEAL---RLRLQAEEeankktaaQEEAEKQKEEAKREAKKRAKAEEAA 1720
Cdd:pfam12128 545 PDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLygvKLDLKRID--------VPEWAASEEELRERLDKAEEALQSA 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1721 LKQKEAAEMELGNQRKMAEEtakqklaAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKEL-EEELIKVRK 1799
Cdd:pfam12128 617 REKQAAAEEQLVQANGELEK-------ASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSaNERLNSLEA 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1800 EMEIL---LQQKSKAEKETMSNTEKSKQlleseaAKMRELAEEatklRSVAEEAKKQRQIAEEEAARQRAEA-EKILKEK 1875
Cdd:pfam12128 690 QLKQLdkkHQAWLEEQKEQKREARTEKQ------AYWQVVEGA----LDAQLALLKAAIAARRSGAKAELKAlETWYKRD 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1876 LTA--INEATRLKTEAEIALKEKEAENDRLKRKA---------EEEGYQRKVLEDQAAQHKQAIEEKIGQL-KKSSDTEL 1943
Cdd:pfam12128 760 LASlgVDPDVIAKLKREIRTLERKIERIAVRRQEvlryfdwyqETWLQRRPRLATQLSNIERAISELQQQLaRLIADTKL 839
|
....
gi 1207141765 1944 DRQK 1947
Cdd:pfam12128 840 RRAK 843
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2213-2440 |
9.54e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 9.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2213 EEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekeNQELmkkdkdntKK 2292
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----------QAEI--------AE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2293 LLEEEAENMKKLAEEAARLNIEAQEAARLRQIAES----DLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQ 2368
Cdd:COG3883 77 AEAEIEERREELGERARALYRSGGSVSYLDVLLGSesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 2369 VEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2440
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1579-2246 |
9.84e-09 |
|
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: 62.05 E-value: 9.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1579 EKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALtaRLEESLKNEQVMVIQ----------LQE--- 1645
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSL--KLEEEIQENKDLIKEnnatrhlcnlLKEtca 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1646 -EAEHLKKQQAEADKARE-------------QAEKELETWRQKANEALRLRLQA--------EEEANKKTAAQEEAEKQK 1703
Cdd:pfam05483 166 rSAEKTKKYEYEREETRQvymdlnnniekmiLAFEELRVQAENARLEMHFKLKEdhekiqhlEEEYKKEINDKEKQVSLL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1704 EEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQ----RTVLDDELQRLKND 1779
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRsmstQKALEEDLQIATKT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1780 VNSAVKQKKELEEELIKVRKEMEIL----------LQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLrsvaee 1849
Cdd:pfam05483 326 ICQLTEEKEAQMEELNKAKAAHSFVvtefeattcsLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKF------ 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1850 aKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLK-TEAEIAL----KEKEAENDRLK---RKAEEEGYQRKVLEDQA 1921
Cdd:pfam05483 400 -KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKgKEQELIFllqaREKEIHDLEIQltaIKTSEEHYLKEVEDLKT 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1922 AQHKQAIE---------------EKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKlnfEKASSGKQELELELK 1986
Cdd:pfam05483 479 ELEKEKLKnieltahcdklllenKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVRE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1987 KLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAE 2066
Cdd:pfam05483 556 EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2067 KEAEKQVILVQEAAQKcsaAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAAllHKKAEEAERQk 2146
Cdd:pfam05483 636 IKVNKLELELASAKQK---FEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQ--HKIAEMVALM- 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2147 kaaeaeaakqakaqedaEKLRKEAEkeasrraeaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDET 2226
Cdd:pfam05483 710 -----------------EKHKHQYD--------------KIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSL 758
|
730 740
....*....|....*....|
gi 1207141765 2227 DKQKSVLDVELKRLKQEVSD 2246
Cdd:pfam05483 759 KKQLEIEKEEKEKLKMEAKE 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1700-1909 |
1.60e-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: 60.16 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1700 EKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKmaeetakqklAAEQELIRLRADFEHAEQQRTVLDDELQRLKND 1779
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA----------ALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1780 VNSAVKQKKELEEELIKV---------RKEMEILLQQKSKAEKETMSNTEKS-KQLLESEAAKMRELAEEATKLRSVAEE 1849
Cdd:COG4942 92 IAELRAELEAQKEELAELlralyrlgrQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1850 AKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEE 1909
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1028-1758 |
1.62e-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: 61.24 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1028 QIKDLRLRLEGCESR------TVNRLRQMVDKEPLKACTQRATEQKKVQTELEGIKKDLDKVvEKSEAVLATSQQSSSAP 1101
Cdd:TIGR02169 245 QLASLEEELEKLTEEiselekRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASL-ERSIAEKERELEDAEER 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1102 V--LRSEIDITQKKMEhvyGLSSVYLDKLKTIDLVIRSTQGAEDILNKYENQLREVNK-VPVNEKEIEASQTQLQKLRSE 1178
Cdd:TIGR02169 324 LakLEAEIDKLLAEIE---ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKeFAETRDELKDYREKLEKLKRE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1179 AEGKQATFDRLEEELQRATE-----------VNKRMSQLHSERDV-----------------ELEHYRQLVGNLRERWQA 1230
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEeladlnaaiagIEAKINELEEEKEDkaleikkqewkleqlaaDLSKYEQELYDLKEEYDR 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1231 VFAQIELRQRELDLLNRQMQAYRESydwlirwIADAKQRQDKLHAvPIGGSKGLQEQLTQ-EKKLLEEIE---------- 1299
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEER-------VRGGRAVEEVLKA-SIQGVHGTVAQLGSvGERYATAIEvaagnrlnnv 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1300 --KNKDKVEDCQKFAK------------------------GYIDAIKDYELQLVTYKALVEPI-----ASPLKKAKMESA 1348
Cdd:TIGR02169 553 vvEDDAVAKEAIELLKrrkagratflplnkmrderrdlsiLSEDGVIGFAVDLVEFDPKYEPAfkyvfGDTLVVEDIEAA 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1349 SDDIIQ-EYVTLRTRYSE---LMTLSSQYIKFIIETQRRLQDEEkaaeklkeeerkkmAEMQAELEKQKQLAETHAKAIA 1424
Cdd:TIGR02169 633 RRLMGKyRMVTLEGELFEksgAMTGGSRAPRGGILFSRSEPAEL--------------QRLRERLEGLKRELSSLQSELR 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1425 KAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETT 1504
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL-EEDLSSLEQEIENVKSELKELEARIEELEEDLHKL 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1505 MKQKNTAETELLQLRAKAVdadklrnaaQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQ 1584
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEI---------QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1585 AEEAERhlKQAELEKQrqiqvveevaKKTAATQLESKQVALtARLEESLKNeqvmviqLQEEAEHLKKQQAEADKAREQA 1664
Cdd:TIGR02169 849 IKSIEK--EIENLNGK----------KEELEEELEELEAAL-RDLESRLGD-------LKKERDELEAQLRELERKIEEL 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1665 EKELETWRQKANEaLRLRLQAEEEANK---KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEET 1741
Cdd:TIGR02169 909 EAQIEKKRKRLSE-LKAKLEALEEELSeieDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKR 987
|
810 820
....*....|....*....|...
gi 1207141765 1742 ------AKQKLAAEQELIRLRAD 1758
Cdd:TIGR02169 988 ldelkeKRAKLEEERKAILERIE 1010
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
177-274 |
1.84e-08 |
|
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: 55.56 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 177 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGVTRLLD 255
Cdd:cd21315 16 TPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIK 92
|
90
....*....|....*....
gi 1207141765 256 PEDVDVPHPDEKSIITYVS 274
Cdd:cd21315 93 PEEMVNPKVDELSMMTYLS 111
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2189-2467 |
2.21e-08 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 60.12 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2189 QEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQldetdkqksvldvELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDL 2268
Cdd:pfam03528 14 EKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEE-------------DLKRQNAVLQEAQVELDALQNQLALARAEMENI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2269 LKLKLKIEKENQELMkkdkDNTKKLLEEEAENMKKLAEEAARlNIEAQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQ 2348
Cdd:pfam03528 81 KAVATVSENTKQEAI----DEVKSQWQEEVASLQAIMKETVR-EYEVQFHRRLEQ-ERAQWNQYRESAEREIADLRRRLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2349 EAAklkaEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ------ETEGFQKSLEAERKRQLEITAEAEK-----LKVKV 2417
Cdd:pfam03528 155 EGQ----EEENLEDEMKKAQEDAEKLRSVVMPMEKEIAAlkakltEAEDKIKELEASKMKELNHYLEAEKscrtdLEMYV 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141765 2418 TQLSDAQSKAEEEAKKFKKQADEIKIRL-QETEKHTSEKHTVVEK----LEVQRL 2467
Cdd:pfam03528 231 AVLNTQKSVLQEDAEKLRKELHEVCHLLeQERQQHNQLKHTWQKAndqfLESQRL 285
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1053-1907 |
2.21e-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: 60.85 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1053 KEPLKACTQRATEQKKVQT---ELEGIKKDLDKVVEKSEAVLATSQQSSS--APVLRSEIDITQKKMEHVYGlssvyldk 1127
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASleeELEKLTEEISELEKRLEEIEQLLEELNKkiKDLGEEEQLRVKEKIGELEA-------- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1128 lkTIDLVIRSTQGAEDILNKYENQLREVnkvpvnEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQ-RATEVNKRMSQL 1206
Cdd:TIGR02169 302 --EIASLERSIAEKERELEDAEERLAKL------EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAeLKEELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1207 HSErDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQE 1286
Cdd:TIGR02169 374 EEV-DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1287 QLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKALVEPI--ASPLKKAKMESASDDIIQEYVTLRtrys 1364
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASeeRVRGGRAVEEVLKASIQGVHGTVA---- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1365 ELMTLSSQYIKFI-IETQRRLQ-----DEEKAAEKLkeeerkkmaemqaELEKQKQLAETHAKAIAKAEQEANELKTKMK 1438
Cdd:TIGR02169 529 QLGSVGERYATAIeVAAGNRLNnvvveDDAVAKEAI-------------ELLKRRKAGRATFLPLNKMRDERRDLSILSE 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1439 DEVSKRQDVAVDSEKQKHNIQRE-------LQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKnta 1511
Cdd:TIGR02169 596 DGVIGFAVDLVEFDPKYEPAFKYvfgdtlvVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSE--- 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1512 ETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSeaekdaaKEKKKALEDLEKFKLQAEEAERH 1591
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE-------KEIEQLEQEEEKLKERLEELEED 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1592 LKQAELEKQRQIQVVEEVAKKTAATQLESKQVALT-ARLEESLKNEQVMviQLQEEAEHLKKQQAEADKAREQAEKELet 1670
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlNDLEARLSHSRIP--EIQAELSKLEEEVSRIEARLREIEQKL-- 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1671 wrqkaNEALRLRLQAEEEANKKtaaqeeaekqkEEAKREAKKRAKAEEAALkqkEAAEMELGNQRKMAEETAKQKLAAEQ 1750
Cdd:TIGR02169 822 -----NRLTLEKEYLEKEIQEL-----------QEQRIDLKEQIKSIEKEI---ENLNGKKEELEEELEELEAALRDLES 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1751 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELikvrkemEILLQQKSKAEKETMSNTEKSKQLLESE- 1829
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL-------EALEEELSEIEDPKGEDEEIPEEELSLEd 955
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141765 1830 -AAKMRELAEEATKLRSVAEEAKKQrqiAEEEAARQraeaeKILKEKLtaineaTRLKTEAEiALKEKEAENDRLKRKA 1907
Cdd:TIGR02169 956 vQAELQRVEEEIRALEPVNMLAIQE---YEEVLKRL-----DELKEKR------AKLEEERK-AILERIEEYEKKKREV 1019
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2549-2733 |
3.69e-08 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 59.84 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2549 EDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQ--------KEAEEEMNGKQKEMQDLEKKRIEQ--EKLLAEE 2618
Cdd:PRK00409 533 EQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqqaiKEAKKEADEIIKELRQLQKGGYASvkAHELIEA 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2619 NKNLREKLQQLQSSQKASYTKEIEIQT-DKVPEEELVQMTMVETTKKvlngstevdgvKKDVPLAFDGIREKVPASRLHE 2697
Cdd:PRK00409 613 RKRLNKANEKKEKKKKKQKEKQEELKVgDEVKYLSLGQKGEVLSIPD-----------DKEAIVQAGIMKMKVPLSDLEK 681
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207141765 2698 IGVLSKKEydklKKGKTTVQELSKNDKVKMCLKGKD 2733
Cdd:PRK00409 682 IQKPKKKK----KKKPKTVKPKPRTVSLELDLRGMR 713
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
172-274 |
3.77e-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: 54.33 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 172 QSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGV 250
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....
gi 1207141765 251 TRLLDPEDVDVPHPDEKSIITYVS 274
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLS 103
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2128-2631 |
4.00e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2128 AEKEAALLHKKAEEAErqkkaaeaeaakQAKAQEDAEKLRKEAEKEASRRAeaeaaalklKQEADSEMAKYkklaEKTLK 2207
Cdd:PRK02224 197 EEKEEKDLHERLNGLE------------SELAELDEEIERYEEQREQARET---------RDEADEVLEEH----EERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2208 QKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSD-----------------AIKQKAQVEDELSKVKIQMEDLLK 2270
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEleeerddllaeaglddaDAEAVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2271 LKLKIEKENQELMKKDKDNTKKlLEEEAenmKKLAEEAARLNIEAQEAARLRQIAESDLAK-----------------QR 2333
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADD-LEERA---EELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdapvDL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2334 ELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKL 2413
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2414 KVKVTQLSDAQSKAeEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEvQRLQSKQEADGLHKAIADLEKEKEKLKKE 2493
Cdd:PRK02224 488 EEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKR-ERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2494 AADLQKQSKEMANVQQEQLQQEKTILqqsffAEKETLLKKEKAIEEEKKKLEKQFED----EVKKAEALKAEQERQRKL- 2568
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESL-----ERIRTLLAAIADAEDEIERLREKREAlaelNDERRERLAEKRERKRELe 640
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 2569 --MEEER-KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKK------RIEQEKLLAEENKNLREKLQQLQS 2631
Cdd:PRK02224 641 aeFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigavenELEELEELRERREALENRVEALEA 712
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1769-2522 |
4.22e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.98 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1769 LDDELQRLKNDVNSAVKQKKELEEELIKV--RKEMEILLQQKSKAEKETMSNT--------EKSKQLLESEAAK-MRELA 1837
Cdd:TIGR00618 83 LGTKIYRVHRTLRCTRSHRKTEQPEQLYLeqKKGRGRILAAKKSETEEVIHDLlkldyktfTRVVLLPQGEFAQfLKAKS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1838 EEATKLRSVAEEAKKQRQIAeeeaarqrAEAEKILKEkltaineatrLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVL 1917
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLA--------LMEFAKKKS----------LHGKAELLTLRSQLLTLCTPCMPDTYHERKQVL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1918 EDQAAQhkqaIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKL-NFEKASSGKQELELELKKLKGIADETQ 1996
Cdd:TIGR00618 225 EKELKH----LREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELrAQEAVLEETQERINRARKAAPLAAHIK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1997 ----------------KSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAA---QEEVGRLMKLAEE 2057
Cdd:TIGR00618 301 avtqieqqaqrihtelQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAtsiREISCQQHTLTQH 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2058 AKKQKEIAEKEAEKQVILVQE-----AAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEA 2132
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKEldilqREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2133 ALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSV 2212
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQL 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2213 EEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVK---------IQMEDLLKLKLKIEKENQELM 2283
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQnitvrlqdlTEKLSEAEDMLACEQHALLRK 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2284 KKDKDNTKKLLEEEAENMKKLAEEAARLNIEA--------QEAARLRQIAESDLAKQRELAEKMLEEKKQAI-------- 2347
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQltltqervREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkemla 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2348 QEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEgFQKSLEAERKRQLEITAEAEKLK----VKVTQLSDA 2423
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ-SLKELMHQARTVLKARTEAHFNNneevTAALQTGAE 779
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2424 QSKAEEEAKKFKKQADEIKIRLQETE-KHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKeaadLQKQSK 2502
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEaEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITH----QLLKYE 855
|
810 820
....*....|....*....|
gi 1207141765 2503 EMANVQQEQLQQEKTILQQS 2522
Cdd:TIGR00618 856 ECSKQLAQLTQEQAKIIQLS 875
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1728-2471 |
4.40e-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: 59.75 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1728 EMELGNQRKMAEETAKQKLAaeqeliRLRADFEHAEQqrtvlddELQRLKNDVNSA-VKQKKELEEELIKVRKEMeillq 1806
Cdd:pfam15921 58 EVELDSPRKIIAYPGKEHIE------RVLEEYSHQVK-------DLQRRLNESNELhEKQKFYLRQSVIDLQTKL----- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1807 QKSKAEKETMSNTEKSkqllesEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLK 1886
Cdd:pfam15921 120 QEMQMERDAMADIRRR------ESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1887 TEAEIALKEKEAENDRL-----KRKAEEEGYQRKVLEDQAAQHKQAI---EEKIGQLKKSSDTELDRQKKIVEETLKQRk 1958
Cdd:pfam15921 194 VDFEEASGKKIYEHDSMstmhfRSLGSAISKILRELDTEISYLKGRIfpvEDQLEALKSESQNKIELLLQQHQDRIEQL- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1959 VVEEEIHILKLNfEKASSGKQELELELKKLKGIADETQKskakaeEEAEKFRKLAleeekkrkEAEAKVKQIQAAEEEAA 2038
Cdd:pfam15921 273 ISEHEVEITGLT-EKASSARSQANSIQSQLEIIQEQARN------QNSMYMRQLS--------DLESTVSQLRSELREAK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2039 RQHKAAQEEVGRLMKLAE----EAKKQKEIAEKEA-------EKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKL 2107
Cdd:pfam15921 338 RMYEDKIEELEKQLVLANseltEARTERDQFSQESgnlddqlQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2108 KEEFEKAKKLAQEAE--------KAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKL--RKEAEKEASRR 2177
Cdd:pfam15921 418 RRELDDRNMEVQRLEallkamksECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtaKKMTLESSERT 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2178 AEAEAAALKLKQEA----DSEMAKYK-----KLAE-KTLKQKS----SVEEELVKVKVQLDETDKQKSVLDVELKRLKQE 2243
Cdd:pfam15921 498 VSDLTASLQEKERAieatNAEITKLRsrvdlKLQElQHLKNEGdhlrNVQTECEALKLQMAEKDKVIEILRQQIENMTQL 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2244 V------SDAIK-QKAQVEDELSKVKIQMEDLlklklkiekenqELMKKDKDNTKKLLEEEAENMkklaeEAARLNIEAQ 2316
Cdd:pfam15921 578 VgqhgrtAGAMQvEKAQLEKEINDRRLELQEF------------KILKDKKDAKIRELEARVSDL-----ELEKVKLVNA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2317 EAARLRqiAESDLAKQRElaeKMLEEKKQAIQEAAKLKAEAEKLQK----QKDQAQVEAQKLLEAKKEMQQRLDQeTEGF 2392
Cdd:pfam15921 641 GSERLR--AVKDIKQERD---QLLNEVKTSRNELNSLSEDYEVLKRnfrnKSEEMETTTNKLKMQLKSAQSELEQ-TRNT 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2393 QKSLEAERKR--------QLEITA---EAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEK 2461
Cdd:pfam15921 715 LKSMEGSDGHamkvamgmQKQITAkrgQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS---QELSTVATEKNKMAGE 791
|
810
....*....|
gi 1207141765 2462 LEVQRLQSKQ 2471
Cdd:pfam15921 792 LEVLRSQERR 801
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2028-2172 |
4.40e-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: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2028 KQIQAAEEE---AARQHKAAQEEvgrlMKLAEEAKKQKEIAEKEAEKQviLVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ 2104
Cdd:TIGR02794 81 EKQRAAEQArqkELEQRAAAEKA----AKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEE 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 2105 DKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEK 2172
Cdd:TIGR02794 155 EAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAA 222
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1718-2405 |
5.04e-08 |
|
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: 59.85 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1718 EAALKQKEAAEMELGNQRKmaEETAKQKLAAEQELIRLRADFEHAEQQRTvLDDELQRLKNDVNSavkQKKELEEELIKV 1797
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHF--GYKSDETLIASRQEERQETSAELNQLLRT-LDDQWKEKRDELNG---ELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1798 RKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEE----ATKLRSVAEEAKKQRQIAEEEAARQRAEaekiLK 1873
Cdd:pfam12128 321 RSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERlkalTGKHQDVTAKYNRRRSKIKEQNNRDIAG----IK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1874 EKLTAINEA-TRLKTEAEIALKEKEA----ENDRLKRKAEEEGYQrkvledqaaqhkqaIEEKIGQLKKSSDteldrQKK 1948
Cdd:pfam12128 397 DKLAKIREArDRQLAVAEDDLQALESelreQLEAGKLEFNEEEYR--------------LKSRLGELKLRLN-----QAT 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1949 IVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQkskakaeeeaekfRKLALeeekkrkeAEAKVK 2028
Cdd:pfam12128 458 ATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQAS-------------EALRQ--------ASRRLE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2029 QIQAAEEEAARQHKAAQeevGRLMK-LAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVL---------VQQN 2098
Cdd:pfam12128 517 ERQSALDELELQLFPQA---GTLLHfLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLygvkldlkrIDVP 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2099 KDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakAQEDAEKLRKEAEkeasrra 2178
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR--------------EETFARTALKNAR------- 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2179 eaeaaaLKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDEL 2258
Cdd:pfam12128 653 ------LDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGA 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2259 SKVKI-QMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAES---------- 2327
Cdd:pfam12128 727 LDAQLaLLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwl 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2328 ----DLAKQRELAEKMLEEKKQ---AIQEAAKLK-AEAEKLQKQKDQAQVEAQKLLEAKKEMQQRL-----DQETEGFQK 2394
Cdd:pfam12128 807 qrrpRLATQLSNIERAISELQQqlaRLIADTKLRrAKLEMERKASEKQQVRLSENLRGLRCEMSKLatlkeDANSEQAQG 886
|
730
....*....|.
gi 1207141765 2395 SLeAERKRQLE 2405
Cdd:pfam12128 887 SI-GERLAQLE 896
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2292-2642 |
5.99e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2292 KLLEEEAENMKKLAEEAARLnieaqeaarlrqiaeSDLAKQRELAEKMLEEKKQAIQE----AAKLKAEAEKLQKQKDQA 2367
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAGI---------------SKYKERRKETERKLERTRENLDRlediLNELERQLKSLERQAEKA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2368 QvEAQKLLEAKKEMQ--------QRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2439
Cdd:TIGR02168 213 E-RYKELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2440 EIKIRLQETEKhtsekhtvveklEVQRLQSKQEADglhkaiadlekekeklkkeaadlqKQSKEMANVQQEQLQQEKTIL 2519
Cdd:TIGR02168 292 ALANEISRLEQ------------QKQILRERLANL------------------------ERQLEELEAQLEELESKLDEL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2520 QQSffaeketlLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQK 2599
Cdd:TIGR02168 336 AEE--------LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1207141765 2600 EMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIE 2642
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
47-158 |
6.20e-08 |
|
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: 53.50 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 47 KTFTKWVNKHLVKhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLpreRDVvrnSRLPREKGRMrfhkLQNVQIALD 126
Cdd:cd21286 3 KIYTDWANHYLAK---SGHKRLIKDLQQDIADGVLLAEIIQIIANEKV---EDI---NGCPRSQSQM----IENVDVCLS 69
|
90 100 110
....*....|....*....|....*....|..
gi 1207141765 127 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTI 158
Cdd:cd21286 70 FLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1457-1978 |
8.44e-08 |
|
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: 58.50 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1457 NIQRELQELKTLSEQEIKAKSQQVEEaLLSRTRIEEEIhiiRLQLETTMKQKNTA--ETELLQLRAKAVD---ADKLRNA 1531
Cdd:pfam05701 46 KVQEEIPEYKKQSEAAEAAKAQVLEE-LESTKRLIEEL---KLNLERAQTEEAQAkqDSELAKLRVEEMEqgiADEASVA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1532 AQE--EAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKAledlekfklQAEEAERHLKQAElekqrqiQVVEEV 1609
Cdd:pfam05701 122 AKAqlEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIK---------RAEEAVSASKEIE-------KTVEEL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1610 AKKTAATQlESKQVALTARLEeslKNEQVMVIQLQEEAEHLKKQqaeadKAREQAEKELETWRQK------------ANE 1677
Cdd:pfam05701 186 TIELIATK-ESLESAHAAHLE---AEEHRIGAALAREQDKLNWE-----KELKQAEEELQRLNQQllsakdlkskleTAS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1678 ALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKaeeAALKQKEAAEMElGNQRKMAEETAKQKLAAEQelirLRA 1757
Cdd:pfam05701 257 ALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAA---LASAKKELEEVK-ANIEKAKDEVNCLRVAAAS----LRS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1758 DFehaEQQRTVLdDELQRLKNDVNSAVKQkkeLEEELIKVRKEMEiLLQQKSKAEKETMSNTEKskqlleseaaKMRELA 1837
Cdd:pfam05701 329 EL---EKEKAEL-ASLRQREGMASIAVSS---LEAELNRTKSEIA-LVQAKEKEAREKMVELPK----------QLQQAA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1838 EEATKLRSVAEEAKKQRQIAEEEAARQRAEA-------EKILKEKLtAINEATRLKTEAEIALKEKEAEndrlKRKAEEE 1910
Cdd:pfam05701 391 QEAEEAKSLAQAAREELRKAKEEAEQAKAAAstvesrlEAVLKEIE-AAKASEKLALAAIKALQESESS----AESTNQE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1911 GYQRKV---LEDQAAQHKQA----------IEEKIGQLKKSSDTELDRQKKI--VEETLKQRKvveEEIHILKLNFEKAS 1975
Cdd:pfam05701 466 DSPRGVtlsLEEYYELSKRAheaeelankrVAEAVSQIEEAKESELRSLEKLeeVNREMEERK---EALKIALEKAEKAK 542
|
...
gi 1207141765 1976 SGK 1978
Cdd:pfam05701 543 EGK 545
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1354-1956 |
9.85e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1354 QEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEkaaeklkeeerkkMAEMQAELEKQKQLAETHAKAIAKAEQEANEL 1433
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEAE-------------LEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1434 KTKMKDevskrqdvavdsekqkhNIQRELQELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTmkqkntaET 1513
Cdd:COG4913 329 EAQIRG-----------------NGGDRLEQL----EREIERLERELEERERRRARLEALLAALGLPLPAS-------AE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1514 ELLQLRAKAVDadkLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEA----- 1588
Cdd:COG4913 381 EFAALRAEAAA---LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlglde 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1589 -------------------------------------ERHLKQA-------ELEKQRQIQVVEEVAKKTAATQLESKQVA 1624
Cdd:COG4913 458 aelpfvgelievrpeeerwrgaiervlggfaltllvpPEHYAAAlrwvnrlHLRGRLVYERVRTGLPDPERPRLDPDSLA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1625 ---------LTARLEESLkNEQVMVIQLqEEAEHLKKqqaeADKA----------REQAEKELETWRQKA------NEAL 1679
Cdd:COG4913 538 gkldfkphpFRAWLEAEL-GRRFDYVCV-DSPEELRR----HPRAitragqvkgnGTRHEKDDRRRIRSRyvlgfdNRAK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1680 RLRLQAEEEAnkktaaqeeaEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQR---KMAEETAKQKLAAEQELIRLR 1756
Cdd:COG4913 612 LAALEAELAE----------LEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeIDVASAEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1757 ADFEHAEQqrtvLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMREL 1836
Cdd:COG4913 682 ASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1837 AEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKE-KLTAINEATRLKTEAEiALKEKEAENDRLkrkaEEEGyqrk 1915
Cdd:COG4913 758 ALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLE-SLPEYLALLDRL----EEDG---- 828
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1207141765 1916 vLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQ 1956
Cdd:COG4913 829 -LPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2027-2231 |
1.11e-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: 57.16 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2027 VKQIQAAEEEAArqhKAAQEEVGRLMKLAEEAKKQKEiAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDsmAQDK 2106
Cdd:TIGR02794 52 ANRIQQQKKPAA---KKEQERQKKLEQQAEEAEKQRA-AEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA--EEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2107 LKEEFEKAKKLAQEAE-KAKDNAEKEAALLHKKAEEAERQKKAAEaeAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAAL 2185
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAErKAKEEAAKQAEEEAKAKAAAEAKKKAEE--AKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207141765 2186 KLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKS 2231
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1711-2447 |
1.15e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.19 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1711 KKRAKAEEAALKQKEAaemELGNQRKM--AEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQR-----LKNDVNSA 1783
Cdd:pfam05483 91 KKWKVSIEAELKQKEN---KLQENRKIieAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnlLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1784 VKQKKELEEELIKVRkemEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAAR 1863
Cdd:pfam05483 168 AEKTKKYEYEREETR---QVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1864 ---QRAEAEKILKEkLTAINEATRLKTEAeiaLKEK-EAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIeekigqlkkSS 1939
Cdd:pfam05483 245 lliQITEKENKMKD-LTFLLEESRDKANQ---LEEKtKLQDENLKELIEKKDHLTKELEDIKMSLQRSM---------ST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1940 DTELDRQKKIVEETLKQRkVVEEEIHILKLNfeKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKK 2019
Cdd:pfam05483 312 QKALEEDLQIATKTICQL-TEEKEAQMEELN--KAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2020 RKEAEAKVKQIQAAEEEAARQHKAAqeeVGRLMKLAEEAKKQKEIAEKEAEKQvilvQEAAQKCSAAEQKAQNVLVQQNK 2099
Cdd:pfam05483 389 KSSELEEMTKFKNNKEVELEELKKI---LAEDEKLLDEKKQFEKIAEELKGKE----QELIFLLQAREKEIHDLEIQLTA 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2100 DSMAQDKLKEEFEKAKKlaqEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAE 2179
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKT---ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2180 AEAAALKLKQEADSemakykklAEKTLKQKSSveeelvKVKVQLDETDKQKsvldvelKRLKQEVSDAIKQKAQVEDELS 2259
Cdd:pfam05483 539 LEEKEMNLRDELES--------VREEFIQKGD------EVKCKLDKSEENA-------RSIEYEVLKKEKQMKILENKCN 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2260 KVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAE-NMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEk 2338
Cdd:pfam05483 598 NLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKvNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE- 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2339 mLEEKKQAIQEAAKLKAEAEKLQKQKdqaQVEAQKLLEAKKEMQQRLDQETE---GFQKSLEAERKR-QLEITAEAEKLK 2414
Cdd:pfam05483 677 -VEKAKAIADEAVKLQKEIDKRCQHK---IAEMVALMEKHKHQYDKIIEERDselGLYKNKEQEQSSaKAALEIELSNIK 752
|
730 740 750
....*....|....*....|....*....|...
gi 1207141765 2415 VKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQE 2447
Cdd:pfam05483 753 AELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2315-2450 |
1.60e-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: 56.78 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2315 AQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQK 2394
Cdd:TIGR02794 49 AQQANRIQQ-QKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141765 2395 SlEAERKRQLEitAEAEKlkvkvTQLSDAQSKAEEEAKKfkKQADEIKIRLQETEK 2450
Cdd:TIGR02794 128 Q-AAEAKAKAE--AEAER-----KAKEEAAKQAEEEAKA--KAAAEAKKKAEEAKK 173
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1106-1962 |
1.62e-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: 58.13 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1106 EIDITQKKMEHVYGLSSVYLDKLKTIDLVIRST--------QGAEDILNKYENQLREVNKvpvNEKEIEASQTQLQKLRS 1177
Cdd:TIGR00606 193 QVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQitskeaqlESSREIVKSYENELDPLKN---RLKEIEHNLSKIMKLDN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1178 EAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFaqielrQRELDLLNRQMQAYRESYD 1257
Cdd:TIGR00606 270 EIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDC------QRELEKLNKERRLLNQEKT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1258 WLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKklLEEIEKNKDKVEDCQKFAKGYIDAIKDyelqlvtykalvepia 1337
Cdd:TIGR00606 344 ELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE--LDGFERGPFSERQIKNFHTLVIERQED---------------- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1338 splkKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQR-RLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLA 1416
Cdd:TIGR00606 406 ----EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKeILEKKQEELKFVIKELQQLEGSSDRILELDQELR 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1417 ETHAKaIAKAEQEANeLKTKMKDEVSkRQDVAVDSEKQKHNIQRELQELKTLSEQEikaksQQVEEALLSRTRIEEEIHI 1496
Cdd:TIGR00606 482 KAERE-LSKAEKNSL-TETLKKEVKS-LQNEKADLDRKLRKLDQEMEQLNHHTTTR-----TQMEMLTKDKMDKDEQIRK 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1497 IRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKE------ 1570
Cdd:TIGR00606 554 IKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcg 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1571 KKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALT-ARLEESLKNEQVMVIQLQEEAEH 1649
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTeAELQEFISDLQSKLRLAPDKLKS 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1650 LKKQQAEADKAREQAEKELETwrqKANEaLRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEM 1729
Cdd:TIGR00606 714 TESELKKKEKRRDEMLGLAPG---RQSI-IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLT 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1730 ELGNQRKMAEETAK-----QKLAAEQELIRLRADFEHAEQQRTVLDDELQRlkndvnsaVKQKKELEEELIKVRKEMEIL 1804
Cdd:TIGR00606 790 DVTIMERFQMELKDverkiAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDT--------VVSKIELNRKLIQDQQEQIQH 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1805 LQQKS---KAEKETMS-NTEKSKQLLESEAAKMRELAEEATKLRSVAEE------AKKQRQIAEEEAARQRAEAEKILKE 1874
Cdd:TIGR00606 862 LKSKTnelKSEKLQIGtNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdspletFLEKDQQEKEELISSKETSNKKAQD 941
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1875 KLTAINEATRLKTEAEIALKEKEAEN-DRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTElDRQKKIVEET 1953
Cdd:TIGR00606 942 KVNDIKEKVKNIHGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQ-KIQERWLQDN 1020
|
....*....
gi 1207141765 1954 LKQRKVVEE 1962
Cdd:TIGR00606 1021 LTLRKRENE 1029
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2191-2432 |
1.62e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2191 ADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlk 2270
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2271 lklkiekeNQELMKKDKDNTKKLLEEEAENMKKLAEEAARLN-IEAQEAARLRQIAEsdlakQRELAEKMLEEKKQAIQE 2349
Cdd:COG3883 92 --------ARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSkIADADADLLEELKA-----DKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2350 AAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEE 2429
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
...
gi 1207141765 2430 EAK 2432
Cdd:COG3883 239 AAA 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2027-2608 |
1.65e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2027 VKQIQAAEEEAARQHKAAQEEVGRLMKLAE---EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQnVLVQQNKDSMA 2103
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKELEELKEeieELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-ELEEKVKELKE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2104 QDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKaaeaeaakqakaqeDAEKLRKEAEKEASRRAEAEAA 2183
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK--------------ELEEKEERLEELKKKLKELEKR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2184 ALKLKQEADS-EMAKYKKLAEKTLKQKSSvEEELVKVKVQLDETDKQKSVLDVELKRLKQEvsdaikqKAQVEDELSKVK 2262
Cdd:PRK03918 354 LEELEERHELyEEAKAKKEELERLKKRLT-GLTPEKLEKELEELEKAKEEIEEEISKITAR-------IGELKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2263 IQMEDLLKLKLKIEKENQELmkkDKDNTKKLLEEEAENMKKLAEEAARL-NIEAQEAARLRQI-----AESDLAKQRELA 2336
Cdd:PRK03918 426 KAIEELKKAKGKCPVCGREL---TEEHRKELLEEYTAELKRIEKELKEIeEKERKLRKELRELekvlkKESELIKLKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2337 EKMLE-EKKQAIQEAAKLKAEAEKLQKQKdqaqveaQKLLEAKKEmqqrldqetegfQKSLEAERKRQLEITAEAEKLKV 2415
Cdd:PRK03918 503 EQLKElEEKLKKYNLEELEKKAEEYEKLK-------EKLIKLKGE------------IKSLKKELEKLEELKKKLAELEK 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2416 KVTQLSDAQSKAEEEAKKFK-KQADEIKIRLQETEKHTSEKHTVVE-KLEVQRLQSKQE--ADGLHKAIADLEKEKEKLK 2491
Cdd:PRK03918 564 KLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDaEKELEREEKELKklEEELDKAFEELAETEKRLE 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2492 KEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKkklekqfedevKKAEALKAEQERqrklMEE 2571
Cdd:PRK03918 644 ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK-----------KTLEKLKEELEE----REK 708
|
570 580 590
....*....|....*....|....*....|....*..
gi 1207141765 2572 ERKKLQSamdaaIKKQKEAEEEMNGKQKEMQDLEKKR 2608
Cdd:PRK03918 709 AKKELEK-----LEKALERVEELREKVKKYKALLKER 740
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1586-2144 |
1.69e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1586 EEAERHLKQAElEKQRQIQVVEEVAKK-TAATQLESKQVALTARLEesLKNEQVMVIQLQEEAEHLKKQQAEADKAREQA 1664
Cdd:COG4913 238 ERAHEALEDAR-EQIELLEPIRELAERyAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1665 EKELETWRQKANEALRLRLQAEEEAnkktaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKq 1744
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDR-----------------LEQLEREIERLERELEERERRRARLEALLAALGLPLP- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1745 klAAEQELIRLRADfehAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSkaeketmsntekskq 1824
Cdd:COG4913 377 --ASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS--------------- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1825 LLESEAAKMRELAEEATK-----LRSVAEEAkkqrQIAEEEAARQRAeAEKIL--------------KEKLTAINE---A 1882
Cdd:COG4913 437 NIPARLLALRDALAEALGldeaeLPFVGELI----EVRPEEERWRGA-IERVLggfaltllvppehyAAALRWVNRlhlR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1883 TRLKTEaeialKEKEAENDRLKRKAEEEGYQRKVL-------------------------EDQAAQHKQAIEEKiGQLKK 1937
Cdd:COG4913 512 GRLVYE-----RVRTGLPDPERPRLDPDSLAGKLDfkphpfrawleaelgrrfdyvcvdsPEELRRHPRAITRA-GQVKG 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1938 SSDT-ELDRQKKIVEE------TLKQRKVVEEEIHILKLNFEKASSgkqelelELKKLKGIADETQKskakaeeeaekfR 2010
Cdd:COG4913 586 NGTRhEKDDRRRIRSRyvlgfdNRAKLAALEAELAELEEELAEAEE-------RLEALEAELDALQE------------R 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2011 KLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEiAEKEAEKQVILVQEAAQKCSAAEQKA 2090
Cdd:COG4913 647 REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEA-ELEELEEELDELKGEIGRLEKELEQA 725
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 2091 QNVL--VQQNKDSMAQDKLKEEFEKAKKLAQEA------EKAKDNAEKEAALLHKKAEEAER 2144
Cdd:COG4913 726 EEELdeLQDRLEAAEDLARLELRALLEERFAAAlgdaveRELRENLEERIDALRARLNRAEE 787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1458-1965 |
1.70e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1458 IQRELQELKTLseQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAE-----TELLQLRAKAVDADKLRNAA 1532
Cdd:COG4913 244 LEDAREQIELL--EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEleelrAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1533 QEEAEKLRKQVAE-ETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAK 1611
Cdd:COG4913 322 REELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1612 K--TAATQLESKQVALTARLEEslkneqvmviqLQEEAEHLKKQQ----AEADKAREQAEKEL----------------- 1668
Cdd:COG4913 402 AleEALAEAEAALRDLRRELRE-----------LEAEIASLERRKsnipARLLALRDALAEALgldeaelpfvgelievr 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1669 ---ETWRQKANEAL---RLRL----QAEEEANK---KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQK---------EA 1726
Cdd:COG4913 471 peeERWRGAIERVLggfALTLlvppEHYAAALRwvnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKldfkphpfrAW 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1727 AEMELGNQRKMAeetakqKLAAEQELIRL-RA----------------DFEHAEQQRTVLddelqrlkndVNSAVKQKKE 1789
Cdd:COG4913 551 LEAELGRRFDYV------CVDSPEELRRHpRAitragqvkgngtrhekDDRRRIRSRYVL----------GFDNRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1790 LEEELIKVRKEMEILLQQKSKAEKEtMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEE-AKKQRQIAE--------EE 1860
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAE-LDALQERREALQ----RLAEYSWDEIDVASAEREiAELEAELERldassddlAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1861 AARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEegyqrkVLEDQAAQHKQAIEEKIGQLKKSsd 1940
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA------AEDLARLELRALLEERFAAALGD-- 761
|
570 580
....*....|....*....|....*
gi 1207141765 1941 telDRQKKIVEETLKQRKVVEEEIH 1965
Cdd:COG4913 762 ---AVERELRENLEERIDALRARLN 783
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4069-4105 |
1.79e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.17 E-value: 1.79e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1207141765 4069 IRLLEAQIATGGIIDPEESHRLPVEMAYKRGLFDEEM 4105
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1763-1959 |
1.86e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 57.53 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1763 EQQRTVLDDELQRLKNDVNSAVKQKKELEEElikvRKEMEILLQQkskAEKETMSNTEKSKQLLESEAAKMRELAEEATK 1842
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQK----AEEAEALLKE---AEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1843 LRSVAEEAKKQ--RQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE---NDRLK-RKAEEEGYQRKV 1916
Cdd:PRK00409 578 AIKEAKKEADEiiKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEElkvGDEVKyLSLGQKGEVLSI 657
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207141765 1917 LEDQAAQHKQAI---EEKIGQLKKSSDTELDRQKKIVEETLKQRKV 1959
Cdd:PRK00409 658 PDDKEAIVQAGImkmKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTV 703
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2291-2614 |
1.92e-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: 56.47 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2291 KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQrELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVE 2370
Cdd:pfam13868 35 KAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQ-ELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2371 AQKLLEAKKEMQQRLDQETEGFQKsLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQA--DEIKIRLQET 2448
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNE-EQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEekEREIARLRAQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2449 EKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKtilqqsffAEKE 2528
Cdd:pfam13868 193 QEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREE--------EEFE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2529 TLLkkekaieeekkklekqfEDEVKKAEALKAEQERQRKLMEEERKKLQSAMD---AAIKKQKEAEEEMNGKQKEMQDLE 2605
Cdd:pfam13868 265 RML-----------------RKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEereEQRAAEREEELEEGERLREEEAER 327
|
....*....
gi 1207141765 2606 KKRIEQEKL 2614
Cdd:pfam13868 328 RERIEEERQ 336
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
181-274 |
2.12e-07 |
|
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: 53.07 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 181 KLLL-WSQrMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN-------------------------- 233
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTqtvdraqdeaedfwvaefspstgdsg 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207141765 234 -----LENLEQAFSIAE---RDLG-VTRLLDPEDVDVPHPDEKSIITYVS 274
Cdd:cd21224 82 lsselLANEKRNFKLVQqavAELGgVPALLRASDMSNTIPDEKVVILFLS 131
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1631-1870 |
2.12e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1631 ESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQeeaekqkeeakREA 1710
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-----------AEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1711 KKRAKAEEAALKQKEA--AEMELGNQRKMAEETAKQKLAAE--QELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQ 1786
Cdd:COG4942 89 EKEIAELRAELEAQKEelAELLRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1787 KKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRA 1866
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
....
gi 1207141765 1867 EAEK 1870
Cdd:COG4942 249 AALK 252
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1475-2075 |
3.01e-07 |
|
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: 57.07 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1475 AKSQQVEeaLLSRT-----RIEEEIHIIRlqlETTMKQKNTAETELLQLRAKAVdADKlrnAAQEEAEKLRKQVAEETQK 1549
Cdd:pfam07111 60 ALSQQAE--LISRQlqelrRLEEEVRLLR---ETSLQQKMRLEAQAMELDALAV-AEK---AGQAEAEGLRAALAGAEMV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1550 KRKAEEELKR-----KSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAA--TQLESKQ 1622
Cdd:pfam07111 131 RKNLEEGSQReleeiQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELlrKQLSKTQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1623 VALTAR--LEESLKN---EQVMVIQLQEEAEHLKK------QQAEADKAREQAEKELETWR-QKANEALRLRlqaEEEAN 1690
Cdd:pfam07111 211 EELEAQvtLVESLRKyvgEQVPPEVHSQTWELERQelldtmQHLQEDRADLQATVELLQVRvQSLTHMLALQ---EEELT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1691 KKTAAQEEAEKQKEEAKREAKKRAKAEEAALK-QKEAAEMELGNQRKmaeeTAKQKLAAEQELIRLRAdfehaeQQRTVL 1769
Cdd:pfam07111 288 RKIQPSDSLEPEFPKKCRSLLNRWREKVFALMvQLKAQDLEHRDSVK----QLRGQVAELQEQVTSQS------QEQAIL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1770 DDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKE---TMSNTEKSKQLLESEAAKMRELAEEATKLRSV 1846
Cdd:pfam07111 358 QRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQlkfVVNAMSSTQIWLETTMTRVEQAVARIPSLSNR 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1847 AEEAKKQRQIAEEEAARQRAEAEkILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRkaeeegyqrkvlEDQAAQHkq 1926
Cdd:pfam07111 438 LSYAVRKVHTIKGLMARKVALAQ-LRQESCPPPPPAPPVDADLSLELEQLREERNRLDA------------ELQLSAH-- 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1927 AIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEea 2006
Cdd:pfam07111 503 LIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQ-- 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2007 ekfRKLALEEEKKRKEAEAKVKQIQAAEEEAAR--------QHKAAQEE--VGRLMKLAEEAKKQ------KEIAEKEAE 2070
Cdd:pfam07111 581 ---EKVAEVETRLREQLSDTKRRLNEARREQAKavvslrqiQHRATQEKerNQELRRLQDEARKEegqrlaRRVQELERD 657
|
....*
gi 1207141765 2071 KQVIL 2075
Cdd:pfam07111 658 KNLML 662
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1711-1911 |
3.35e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 56.32 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1711 KKRAKAEEAALKQKEAAEMElgnqrkmAEETAKQK-LAAEQELIRLRADFEhaeqqrtvlddelqrlkndvnsavKQKKE 1789
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKE-------AEAIKKEAlLEAKEEIHKLRNEFE------------------------KELRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1790 LEEELikvrKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEA-KKQRQIAEEEAARQRAEA 1868
Cdd:PRK12704 80 RRNEL----QKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQELERISGLTAEEA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207141765 1869 EKILKEKLTAineatrlKTEAEIALKEKEAENdrlkrKAEEEG 1911
Cdd:PRK12704 156 KEILLEKVEE-------EARHEAAVLIKEIEE-----EAKEEA 186
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1642-1898 |
3.40e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 56.99 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1642 QLQEEAEHLkkqQAEADKAREQAEkELETWRQKANEALRL------RLQAEEEANKKTaaqeeaekqkeeakreakkrAK 1715
Cdd:PRK10929 117 QLLEKSRQA---QQEQDRAREISD-SLSQLPQQQTEARRQlneierRLQTLGTPNTPL--------------------AQ 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1716 AEEAALKQKEAAEMELGNQRKMAEETAKQKlaaeQELIRLRADFehAEQQRTVLDDELQRLKNDVNSAVKQK-------- 1787
Cdd:PRK10929 173 AQLTALQAESAALKALVDELELAQLSANNR----QELARLRSEL--AKKRSQQLDAYLQALRNQLNSQRQREaeralest 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1788 ---------------------KELEEELIKVRKEMEILLQQKSKAEKETM------------------SNT--------- 1819
Cdd:PRK10929 247 ellaeqsgdlpksivaqfkinRELSQALNQQAQRMDLIASQQRQAASQTLqvrqalntlreqsqwlgvSNAlgealraqv 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1820 ----EKSK-QLLESEAAKMR-------ELAEEATKLRSVAEE-----AKKQRQIAEEEAARQRAEAEKILKEKLTAINEA 1882
Cdd:PRK10929 327 arlpEMPKpQQLDTEMAQLRvqrlryeDLLNKQPQLRQIRQAdgqplTAEQNRILDAQLRTQRELLNSLLSGGDTLILEL 406
|
330 340
....*....|....*....|
gi 1207141765 1883 TRLK---TEAEIALKE-KEA 1898
Cdd:PRK10929 407 TKLKvanSQLEDALKEvNEA 426
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2280-2442 |
3.66e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 56.76 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2280 QELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAE 2358
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAiKEAKKEAD 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2359 KLQK------QKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKS------------------------LEAERKRQLEITA 2408
Cdd:PRK00409 588 EIIKelrqlqKGGYASVKAHELIEARKRLNKANEKKEKKKKKQkekqeelkvgdevkylslgqkgevLSIPDDKEAIVQA 667
|
170 180 190
....*....|....*....|....*....|....
gi 1207141765 2409 EAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2442
Cdd:PRK00409 668 GIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1727-1931 |
3.88e-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: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1727 AEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM----- 1801
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1802 ------------EILLQQKSKAEkeTMSNTEKSKQLLESEAAKMRELAEEATKLrsvaEEAKKQRQIAEEEAARQRAEAE 1869
Cdd:COG3883 94 alyrsggsvsylDVLLGSESFSD--FLDRLSALSKIADADADLLEELKADKAEL----EAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 1870 KILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEK 1931
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2284-2497 |
4.02e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.97 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2284 KKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAE--SDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQ 2361
Cdd:PRK09510 76 RAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKqaEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2362 KQKDQAQVEAqkllEAKKemqqrldQETEGFQKSLEAERKRQleitAEAEklkvkvtqlsdAQSKAEEEAKKFKKQADEI 2441
Cdd:PRK09510 156 AAAAAKKAAA----EAKK-------KAEAEAAKKAAAEAKKK----AEAE-----------AAAKAAAEAKKKAEAEAKK 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141765 2442 KIRLQETEKHTSEKHTVVEKLEVqrlQSKQEADGLHKAIADLEKEKEKLKKEAADL 2497
Cdd:PRK09510 210 KAAAEAKKKAAAEAKAAAAKAAA---EAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1067-1601 |
4.03e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.67 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1067 KKVQTELEGIKKDLDKVVEKSEAVLATSQQSSSAPVLRSEIDITQKKMEHVYGLSSVyLDKLKTIDLVIRSTQGAEDILn 1146
Cdd:pfam15921 227 RELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGL-TEKASSARSQANSIQSQLEII- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1147 kyENQLREVNKVPVNE-KEIEASQTQLqklRSE-AEGKQATFDRLEEELQRATEVNKRMSQLHSERDveleHYRQLVGNL 1224
Cdd:pfam15921 305 --QEQARNQNSMYMRQlSDLESTVSQL---RSElREAKRMYEDKIEELEKQLVLANSELTEARTERD----QFSQESGNL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1225 RERWQAVFAQIELRQRELDLLNRQMQAYRE-------SYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQE------ 1291
Cdd:pfam15921 376 DDQLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQmaaiqg 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1292 -KKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAkmESASDDIIQEYVTLRTRYsELMTLS 1370
Cdd:pfam15921 456 kNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK--ERAIEATNAEITKLRSRV-DLKLQE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1371 SQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVD 1450
Cdd:pfam15921 533 LQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1451 SEKQKHNIQR--------ELQELKTLSE--------QEIKA-KSQQVEEALLSRTRIE---EEIHIIRL-------QLET 1503
Cdd:pfam15921 613 KDKKDAKIRElearvsdlELEKVKLVNAgserlravKDIKQeRDQLLNEVKTSRNELNslsEDYEVLKRnfrnkseEMET 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1504 TMK----QKNTAETELLQLR-------------------------AKAVDADKLRNAAQ-----------------EEAE 1537
Cdd:pfam15921 693 TTNklkmQLKSAQSELEQTRntlksmegsdghamkvamgmqkqitAKRGQIDALQSKIQfleeamtnankekhflkEEKN 772
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141765 1538 KLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQR 1601
Cdd:pfam15921 773 KLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVR 836
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1579-1899 |
4.07e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.49 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1579 EKFKLQAEEAERhlKQAELEKQRqiqvveevakktaatqLESKQvaltARLEEslkneqvmviqlqEEAEHLKKQQAEAD 1658
Cdd:PRK05035 434 AKAEIRAIEQEK--KKAEEAKAR----------------FEARQ----ARLER-------------EKAAREARHKKAAE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1659 KAREQAEKELetwrQKANEALRLRlQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEmelgNQRK-- 1736
Cdd:PRK05035 479 ARAAKDKDAV----AAALARVKAK-KAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAA----DPKKaa 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1737 --MAEETAKQKLAAEQElirlradfEHAEQQRTVlDDELQRLKNDVNSAVKQKKELEEElikvrkemeillqQKSKAEKE 1814
Cdd:PRK05035 550 vaAAIARAKAKKAAQQA--------ANAEAEEEV-DPKKAAVAAAIARAKAKKAAQQAA-------------SAEPEEQV 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1815 TMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKqrqiAEEEAARQRAEAEKILKEKLTAINEAT----RLKTEAE 1890
Cdd:PRK05035 608 AEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRK----AAVAAAIARAKARKAAQQQANAEPEEAedpkKAAVAAA 683
|
330
....*....|
gi 1207141765 1891 IA-LKEKEAE 1899
Cdd:PRK05035 684 IArAKAKKAA 693
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1584-1793 |
5.36e-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: 55.24 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1584 QAEEAErhlKQAELEKQRQIQVVEEVAKKTAATQLEskqvalTARLEESLKneqvmviqlQEEAEHLKKQQAEADKAREQ 1663
Cdd:TIGR02794 76 QAEEAE---KQRAAEQARQKELEQRAAAEKAAKQAE------QAAKQAEEK---------QKQAEEAKAKQAAEAKAKAE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1664 AEKEletwRQKANEALRlrlQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAK 1743
Cdd:TIGR02794 138 AEAE----RKAKEEAAK---QAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAA 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1744 QKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEE 1793
Cdd:TIGR02794 211 AKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
45-161 |
5.47e-07 |
|
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: 50.96 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 45 QKKTFTKWVNKhlvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSgetlPRERDVVRNSRLPRekgRMRFHKLQNVQIA 124
Cdd:cd21299 5 EERCFRLWINS-------LGIDTYVNNVFEDVRDGWVLLEVLDKVS----PGSVNWKHANKPPI---KMPFKKVENCNQV 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141765 125 LDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 161
Cdd:cd21299 71 VKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1445-1667 |
5.85e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1445 QDVAVDSEKQKHNIQRELQELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAvd 1524
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1525 aDKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLK-----QAELEK 1599
Cdd:COG4942 93 -AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAelaalRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141765 1600 QRQIQVV---EEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKE 1667
Cdd:COG4942 172 ERAELEAllaELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1172-1901 |
6.10e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 56.00 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1172 LQKLRSEAEGKQATFDRLEEELQRATEVNK-------RMSQLHSERDVELEHYRQLVGNLRERWQAVFAQIELR------ 1238
Cdd:pfam12128 236 IMKIRPEFTKLQQEFNTLESAELRLSHLHFgyksdetLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGElsaada 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1239 -----QRELDLLNRQMQAYR----ESY----DWLIRWIADAKQRQDKLHAVPigGSKGLQEQLTQEKKLLEEiEKNKDKV 1305
Cdd:pfam12128 316 avakdRSELEALEDQHGAFLdadiETAaadqEQLPSWQSELENLEERLKALT--GKHQDVTAKYNRRRSKIK-EQNNRDI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1306 EDCQKfakgYIDAIKD-YELQLVTYKALVEPIASPLKKaKMESASDDIIQEYVTLRTRYSELMTL--SSQYIKFIIETQR 1382
Cdd:pfam12128 393 AGIKD----KLAKIREaRDRQLAVAEDDLQALESELRE-QLEAGKLEFNEEEYRLKSRLGELKLRlnQATATPELLLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1383 RLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMkDEVSKRQDvavdseKQKHNIQREL 1462
Cdd:pfam12128 468 NFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSAL-DELELQLF------PQAGTLLHFL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1463 QELKTLSEQEIkakSQQVEEALLSRTRIEEEIhiirlqLETTMKQKNTAETelLQLRAKAVDADK---LRNAAQEEAEKL 1539
Cdd:pfam12128 541 RKEAPDWEQSI---GKVISPELLHRTDLDPEV------WDGSVGGELNLYG--VKLDLKRIDVPEwaaSEEELRERLDKA 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1540 RKQVAEETQKKRKAEEELKRKSEAekdaakekkkaledLEKFKLQAEEAERHLKQAElEKQRQIQVVEEVAKKTAATQLE 1619
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGE--------------LEKASREETFARTALKNAR-LDLRRLFDEKQSEKDKKNKALA 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1620 SKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEAnkktaaqeea 1699
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSG---------- 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1700 ekqkeeakreakkrAKAEEAALKQKEAAEMElgnqRKMAEETAKQKLAAE-QELIRLRADFEHAEQQRTVLDDELQrlkn 1778
Cdd:pfam12128 745 --------------AKAELKALETWYKRDLA----SLGVDPDVIAKLKREiRTLERKIERIAVRRQEVLRYFDWYQ---- 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1779 dvNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKET-MSNTEKSKQLLESEAAKMReLAEEATKLRSVaeeakkQRQIA 1857
Cdd:pfam12128 803 --ETWLQRRPRLATQLSNIERAISELQQQLARLIADTkLRRAKLEMERKASEKQQVR-LSENLRGLRCE------MSKLA 873
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1207141765 1858 EEEAARQRAEAEKILKEKLTAINEaTRLKTEAEIALKEKEAEND 1901
Cdd:pfam12128 874 TLKEDANSEQAQGSIGERLAQLED-LKLKRDYLSESVKKYVEHF 916
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2028-2170 |
6.54e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.20 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2028 KQIQAAEEEAARQHKAAQEEVgrlmklAEEAKKQKEIAEKEAEKQVILVQEAAQKcsAAEQKAQNVLVQQNKDSMAQDKL 2107
Cdd:PRK09510 114 QEQKKQAEEAAKQAALKQKQA------EEAAAKAAAAAKAKAEAEAKRAAAAAKK--AAAEAKKKAEAEAAKKAAAEAKK 185
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141765 2108 KEEFEKAKKLAQEAE-KAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEA 2170
Cdd:PRK09510 186 KAEAEAAAKAAAEAKkKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEK 249
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4172-4200 |
6.94e-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: 6.94e-07
10 20
....*....|....*....|....*....
gi 1207141765 4172 IVDPETGKEMSVYEAYRKGLIDHQTYIEL 4200
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1735-1874 |
7.02e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.78 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1735 RKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVR---------KEMEILL 1805
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyealqKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141765 1806 QQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKE 1874
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1164-1692 |
7.15e-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: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1164 EIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELE-HYRQLVGNLRERWQAVFAQIELRQREL 1242
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQkRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1243 DLLNRQMQAYRESYDWL-------------IRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQ 1309
Cdd:pfam05557 83 KYLEALNKKLNEKESQLadarevisclkneLSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1310 KFAKGYIDAIKD--YELQLVTYKALVepiaspLKKAKMESAS-DDIIQEYVTLRTRYSELMTLSSQyiKFIIETQ----- 1381
Cdd:pfam05557 163 SSLAEAEQRIKEleFEIQSQEQDSEI------VKNSKSELARiPELEKELERLREHNKHLNENIEN--KLLLKEEvedlk 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1382 RRLQDEEKaAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDE-VSKRQDVAVDSE-KQKHNIQ 1459
Cdd:pfam05557 235 RKLEREEK-YREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREiVLKEENSSLTSSaRQLEKAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1460 RELQE-----LKTLSEQEIKAKSQQVEEALLSRTRI--EEEIHIIRLQL-----ETTMKQKNTAETELLQLRAKAVDADK 1527
Cdd:pfam05557 314 RELEQelaqyLKKIEDLNKKLKRHKALVRRLQRRVLllTKERDGYRAILesydkELTMSNYSPQLLERIEEAEDMTQKMQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1528 LRNA--------AQEEAE--KLRKQVAEETQKKRKAEEELKRKSeaekDAAKEKKKALEDLEKFKLQAEEAERHLKQAEL 1597
Cdd:pfam05557 394 AHNEemeaqlsvAEEELGgyKQQAQTLERELQALRQQESLADPS----YSKEEVDSLRRKLETLELERQRLREQKNELEM 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1598 EKQRQIQVVEEVAKKTAATQLESKQvalTARLEESLKNeqvMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKAN- 1676
Cdd:pfam05557 470 ELERRCLQGDYDPKKTKVLHLSMNP---AAEAYQQRKN---QLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFk 543
|
570
....*....|....*.
gi 1207141765 1677 EALRLRLQAeEEANKK 1692
Cdd:pfam05557 544 EVLDLRKEL-ESAELK 558
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2076-2647 |
7.59e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.89 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2076 VQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEkAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAK 2155
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE-ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSD 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2156 QAKAQEDAEKLRKEAEKEASRRAEAEAAALKLkqeADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDV 2235
Cdd:pfam15921 322 LESTVSQLRSELREAKRMYEDKIEELEKQLVL---ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2236 ELKRL--------------KQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLlEEEAENM 2301
Cdd:pfam15921 399 QNKRLwdrdtgnsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQL-ESTKEML 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2302 KKLAEE--AARLNIEAQEaarlRQIaeSDLAKQRELAEKMLEEKKQAI-----------QEAAKLKAEAEKLQKQkdQAQ 2368
Cdd:pfam15921 478 RKVVEEltAKKMTLESSE----RTV--SDLTASLQEKERAIEATNAEItklrsrvdlklQELQHLKNEGDHLRNV--QTE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2369 VEAQKLLEAKKemqqrlDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQET 2448
Cdd:pfam15921 550 CEALKLQMAEK------DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2449 EKHTSEKHtvVEKLEV-----QRLQS----KQEADGLHKAI----ADLEKEKEKLKKEAADLQKQSKEM---ANVQQEQL 2512
Cdd:pfam15921 624 EARVSDLE--LEKVKLvnagsERLRAvkdiKQERDQLLNEVktsrNELNSLSEDYEVLKRNFRNKSEEMettTNKLKMQL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2513 QQEKTILQQSffaeKETLLKKekaieeekkklekqfedEVKKAEALKAEQERQRKLMEEerkklQSAMDAAIKKQKEAEE 2592
Cdd:pfam15921 702 KSAQSELEQT----RNTLKSM-----------------EGSDGHAMKVAMGMQKQITAK-----RGQIDALQSKIQFLEE 755
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2593 EMNGKQKEMQDL--EKKRIEQE-KLLAEENKNLREKLQQLQSSQKASYTK--EIEIQTDK 2647
Cdd:pfam15921 756 AMTNANKEKHFLkeEKNKLSQElSTVATEKNKMAGELEVLRSQERRLKEKvaNMEVALDK 815
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1267-1602 |
8.19e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.51 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1267 KQRQDKLHavpiggsKGLQEQLTQEKK-LLEEIEKNKdKVEDCQKFAKGYID---AI-KDYELQLVTYKALVEPIASPLK 1341
Cdd:pfam17380 287 RQQQEKFE-------KMEQERLRQEKEeKAREVERRR-KLEEAEKARQAEMDrqaAIyAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1342 KAKMESASDDIIQEYVTlRTRYSELMTLSSQyikfiiETQRRLQDEEKAAEKLKEEERkkmaEMQAELEKQKQLAEThak 1421
Cdd:pfam17380 359 KRELERIRQEEIAMEIS-RMRELERLQMERQ------QKNERVRQELEAARKVKILEE----ERQRKIQQQKVEMEQ--- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1422 aIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHniQRELQELKTlSEQEIKAKSQQVEEALLSRTRIEEEihiirlql 1501
Cdd:pfam17380 425 -IRAEQEEARQREVRRLEEERAREMERVRLEEQER--QQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQ-------- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1502 ettmkQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEEtQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKF 1581
Cdd:pfam17380 493 -----RRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-ERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566
|
330 340
....*....|....*....|...
gi 1207141765 1582 KLQAEEAERHLKQ--AELEKQRQ 1602
Cdd:pfam17380 567 RLEAMEREREMMRqiVESEKARA 589
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1408-1890 |
9.84e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 9.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1408 ELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIqRELQELKTLSEQ---------EIKAKSQ 1478
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-KELKELKEKAEEyiklsefyeEYLDELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1479 QVEEALlsrTRIEEEIHIIRLQL----------ETTMKQKNTAETELLQLRAKAVDADKLRnAAQEEAEKLRKQVAEETQ 1548
Cdd:PRK03918 311 EIEKRL---SRLEEEINGIEERIkeleekeerlEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTP 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1549 KKRKAE-EELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQA---------ELEKQRQIQVVEEVAKKTAATql 1618
Cdd:PRK03918 387 EKLEKElEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrELTEEHRKELLEEYTAELKRI-- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1619 eSKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANK-KTAAQE 1697
Cdd:PRK03918 465 -EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKlKGEIKS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1698 EAEKQKEEAKREAKKRAKAEEAALKQKEAAEM--ELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQR 1775
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELlkELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1776 LKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQ 1855
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE---ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
490 500 510
....*....|....*....|....*....|....*...
gi 1207141765 1856 IAEEEAARQRAEAEKILK--EKLTAINEATR-LKTEAE 1890
Cdd:PRK03918 701 EELEEREKAKKELEKLEKalERVEELREKVKkYKALLK 738
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
46-162 |
1.06e-06 |
|
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: 50.66 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 46 KKTFTKWVNKHLvkhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDVVRNSRLPrekgrmrfHKLQNVQIAL 125
Cdd:cd21222 18 KELLLQFVNKHL-----AKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPLHEYHLTPSTDD--------EKLHNVKLAL 84
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141765 126 DFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 162
Cdd:cd21222 85 ELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1528-1969 |
1.18e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1528 LRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVE 1607
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1608 EVAKKTAATQLESKQVALTARLEEsLKNEQVMVIQLQEEAEHLKKQQAEADKAREQA--------EKELETWRQKANEAL 1679
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1680 RLRLQAEEEANKKTAAQEEAEKQKEEAkrEAKKRAKAEEAALKQKE------AAEMELGNQRKMAEETAKQKLAAEQELI 1753
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQL--ENELEAAALEERLKEARlllliaAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1754 RLRAD-FEHAEQQRTVLDDELQRLkndvNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAK 1832
Cdd:COG4717 284 GLLALlFLLLAREKASLGKEAEEL----QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1833 MRELAEEAtkLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAEND--RLKRKAEEE 1910
Cdd:COG4717 360 EEELQLEE--LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEEL 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1911 GYQRKVLEDQAAQHKQAIEEKIGQLKK-SSDTELDRQKKIVEETLKQRKVVEEEIHILKL 1969
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2028-2213 |
1.27e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.04 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2028 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKdsmAQDKL 2107
Cdd:PRK09510 93 QQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA---AEAKK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2108 KEEFEKAKKLAQEA-EKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakaqedAEKLRKEAEKEASRRAEAEAAALK 2186
Cdd:PRK09510 170 KAEAEAAKKAAAEAkKKAEAEAAAKAAAEAKKKAEAEA------------------KKKAAAEAKKKAAAEAKAAAAKAA 231
|
170 180
....*....|....*....|....*..
gi 1207141765 2187 LKQEADSEMAKYKKLAEKTLKQKSSVE 2213
Cdd:PRK09510 232 AEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2398-2620 |
1.49e-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: 54.00 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2398 AERKRQLEitAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLH 2477
Cdd:COG4942 19 ADAAAEAE--AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2478 KAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQ--QSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKA 2555
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141765 2556 EALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENK 2620
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2421-2636 |
1.74e-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: 53.61 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2421 SDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQ 2500
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2501 SKEmanvQQEQLQQEKTILQQSFFAEKETLL------KKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERK 2574
Cdd:COG4942 99 LEA----QKEELAELLRALYRLGRQPPLALLlspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141765 2575 KLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAE---ENKNLREKLQQLQSSQKAS 2636
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAEAAAA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1762-1932 |
1.78e-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: 52.23 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1762 AEQQRTVLDdeLQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtMSNTEKSKQLLESEAAKMRELAEEAT 1841
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1842 KLrsvAEEAKKQRQIA-----EEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKV 1916
Cdd:COG1579 80 EQ---LGNVRNNKEYEalqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*.
gi 1207141765 1917 LEDQAAQHKQAIEEKI 1932
Cdd:COG1579 157 ELEELEAEREELAAKI 172
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1744-1939 |
1.92e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1744 QKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILlQQKSKAEKETMSNTEKSK 1823
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-EAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1824 Q-----------LLESEAAKmrELAEEATKLRSVAEEAKK---QRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEA 1889
Cdd:COG3883 96 YrsggsvsyldvLLGSESFS--DFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1890 EIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSS 1939
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1785-1932 |
1.96e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 53.72 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1785 KQKKELEEELIKVRKEMEILLQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEATKLRSV---------AEEAKKQRQ 1855
Cdd:COG2268 216 IAQANREAEEAELEQEREIETARIAEAEAEL----AKKKAEERREAETARAEAEAAYEIAEAnaerevqrqLEIAERERE 291
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141765 1856 IAEEEAARQRAEAEKILKEKLTAinEATRLKTEAEialKEKEAENDRLKRKAEEEGYQRKVlEDQAAQHKQAIEEKI 1932
Cdd:COG2268 292 IELQEKEAEREEAELEADVRKPA--EAEKQAAEAE---AEAEAEAIRAKGLAEAEGKRALA-EAWNKLGDAAILLML 362
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1743-2450 |
2.07e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1743 KQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKeTMSNTEKS 1822
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK-NIDKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1823 KQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAE---EEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE 1899
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKdniEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1900 NDRLKRKAEEegyqrkvLEDQAAQHKQAIE----EKIGQLKKSSDTELDRQKKIVEETlkQRKVVEEEIHILKLNfekas 1975
Cdd:TIGR04523 276 LEQNNKKIKE-------LEKQLNQLKSEISdlnnQKEQDWNKELKSELKNQEKKLEEI--QNQISQNNKIISQLN----- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1976 sgkqelelelkklkgiadetqkskakaeeeaekfrklaleeekkrkeaeakvKQIQAAEEEaarqhkaaqeevgRLMKLA 2055
Cdd:TIGR04523 342 ----------------------------------------------------EQISQLKKE-------------LTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2056 EEAKKQKEIAEKEAEKQVILVQEAAQKcsaaeQKAQNVLVQQNkdsmaqdKLKEEFEKAKKLAQEAEKAKDNAEKEAALL 2135
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYK-----QEIKNLESQIN-------DLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2136 HKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASrraeaeaaalKLKQEADSEMAKYKKLaEKTLKQKssvEEE 2215
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE----------SLETQLKVLSRSINKI-KQNLEQK---QKE 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2216 LVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDllklklkiekENQELMKKDKDNTKKLLE 2295
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD----------LEDELNKDDFELKKENLE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2296 EEAENMKKLAEEaarlnieaqeaarLRQIAESDLAKQRELAEKMLE---EKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQ 2372
Cdd:TIGR04523 561 KEIDEKNKEIEE-------------LKQTQKSLKKKQEEKQELIDQkekEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2373 KLLEAKK---EMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETE 2449
Cdd:TIGR04523 628 KLSSIIKnikSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDLP 707
|
.
gi 1207141765 2450 K 2450
Cdd:TIGR04523 708 K 708
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1427-1771 |
2.09e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 53.72 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1427 EQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSeqeikAKSQQVEEALLSRTRIEEEIHIIRLQlETTMK 1506
Cdd:pfam02029 12 RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG-----QGGLDEEEAFLDRTAKREERRQKRLQ-EALER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1507 QKNTAETellQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEE--LKRKSEAEKDAAKEKKKALEDLEKFKLQ 1584
Cdd:pfam02029 86 QKEFDPT---IADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEEteIREKEYQENKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1585 AEEAERHLKQAEL-EKQRQIQVVEEVAKKTAATQLESKQVALTarlEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQ 1663
Cdd:pfam02029 163 SEEAEEVPTENFAkEEVKDEKIKKEKKVKYESKVFLDQKRGHP---EVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1664 AEKELETwrQKANEALRLRLQA--EEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMElgnqRKMAEET 1741
Cdd:pfam02029 240 AEVFLEA--EQKLEELRRRRQEkeSEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAE----RKLREEE 313
|
330 340 350
....*....|....*....|....*....|
gi 1207141765 1742 AKQKLaaEQELIRLRAdfEHAEQQRTVLDD 1771
Cdd:pfam02029 314 EKRRM--KEEIERRRA--EAAEKRQKLPED 339
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
648-740 |
2.24e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 48.87 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 648 HAFVVAATKELMWLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNVQMTGDKLLKDGHPARKTIEAFTA 727
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1207141765 728 ALQTQWSWILQLC 740
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1768-1968 |
2.26e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1768 VLDDelQRLKNDVNSAVKQKKEL---EEELIKVRKEMEIL-----LQQKSKAEKETMSNTEKSKQLLESEAA--KMRELA 1837
Cdd:COG4913 217 MLEE--PDTFEAADALVEHFDDLeraHEALEDAREQIELLepireLAERYAAARERLAELEYLRAALRLWFAqrRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1838 EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTA----INEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQ 1913
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141765 1914 ----RKVLEDQAAQHKQAIEEkIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILK 1968
Cdd:COG4913 375 lpasAEEFAALRAEAAALLEA-LEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1757-2496 |
2.31e-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: 53.96 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1757 ADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKsKAEKETMSNTEKSKQLLESEAAKMREL 1836
Cdd:pfam05483 68 SDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQR-KAIQELQFENEKVSLKLEEEIQENKDL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1837 AEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIAlkEKEAENDRLKrkaeeegYQRKV 1916
Cdd:pfam05483 147 IKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL--RVQAENARLE-------MHFKL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1917 LEDQaaqhkqaieEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKAssgkQELELELKKLKGIADETQ 1996
Cdd:pfam05483 218 KEDH---------EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEES----RDKANQLEEKTKLQDENL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1997 KskakaeeeaekfrklalEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEV----GRLMKLAEEAKKQKEIAEKEAEKQ 2072
Cdd:pfam05483 285 K-----------------ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLqiatKTICQLTEEKEAQMEELNKAKAAH 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2073 VILVQE-AAQKCSAAEQ-KAQNVLVQQNKDSMAQdkLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAE 2150
Cdd:pfam05483 348 SFVVTEfEATTCSLEELlRTEQQRLEKNEDQLKI--ITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2151 AeaakqakaqedAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQK 2230
Cdd:pfam05483 426 Q-----------FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHC 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2231 SVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQ----------MEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAEN 2300
Cdd:pfam05483 495 DKLLLENKELTQEASDMTLELKKHQEDIINCKKQeermlkqienLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2301 MKKLAEEAarlnIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAiQEAAKLKAEAEklQKQKDQAQVEAQKLLEAKKE 2380
Cdd:pfam05483 575 ARSIEYEV----LKKEKQMKILENKCNNLKKQIENKNKNIEELHQE-NKALKKKGSAE--NKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2381 MQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAK-----------KFKKQADEIkIRLQETE 2449
Cdd:pfam05483 648 AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhkiaemvalmeKHKHQYDKI-IEERDSE 726
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 2450 -----KHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAAD 2496
Cdd:pfam05483 727 lglykNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2297-2439 |
2.54e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 53.34 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2297 EAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAE----KMLEEKKQAIQEAAKLKAEAEKLQKQkDQAQVEA- 2371
Cdd:COG2268 187 DALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAEleqeREIETARIAEAEAELAKKKAEERREA-ETARAEAe 265
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 2372 QKLLEAKKEMQQRLDQETEgfqkslEAERKRQLEItAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2439
Cdd:COG2268 266 AAYEIAEANAEREVQRQLE------IAEREREIEL-QEKEAEREEAELEADVRKPAEAEKQAAEAEAE 326
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2316-2593 |
3.51e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 53.41 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2316 QEAARLRQIAE----SDLAKQR-ELAEKMLEEKKQAiqEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKemqqrlDQETE 2390
Cdd:PRK05035 433 QAKAEIRAIEQekkkAEEAKARfEARQARLEREKAA--REARHKKAAEARAAKDKDAVAAALARVKAKK------AAATQ 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2391 GFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQA----DEIKIRLQETEKHTSEKHTVVEKLEVQR 2466
Cdd:PRK05035 505 PIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAaiarAKAKKAAQQAANAEAEEEVDPKKAAVAA 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2467 LQSKQEAdglHKAIADLEKEKEKLKKEAADLQKQSKEMANVQ---QEQLQQEKTILQQSFFAEKETLlkkekaieeekkk 2543
Cdd:PRK05035 585 AIARAKA---KKAAQQAASAEPEEQVAEVDPKKAAVAAAIARakaKKAEQQANAEPEEPVDPRKAAV------------- 648
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 2544 lekqfEDEVKKAEALKAEQER--QRKLMEEERKKLQSAMDAAIKKQKEAEEE 2593
Cdd:PRK05035 649 -----AAAIARAKARKAAQQQanAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2286-2482 |
4.55e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2286 DKDNTKKLLEEEAENMKKL--AEEAARlnIEAQEAARLRQI---------AESDLAKQREL--------AEKMLEEKKQA 2346
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLerAHEALE--DAREQIELLEPIrelaeryaaARERLAELEYLraalrlwfAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2347 I----QEAAKLKAEAEKLQKQKDQAQveaQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKvkvTQLSD 2422
Cdd:COG4913 297 LeelrAELARLEAELERLEARLDALR---EELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE---ALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2423 AQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIAD 2482
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1420-1660 |
4.59e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1420 AKAIAKAEQEANELKTKMKDEVSKRQDVavdsEKQKHNIQRELQELktlsEQEIKAKSQQVEEallsrtrIEEEIHIIRL 1499
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAAL----ERRIAALARRIRA-------LEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1500 QLETTMKQKNTAETELLQLR---AKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALE 1576
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKeelAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1577 DLEKfKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQvmviQLQEEAEHLKKQQAE 1656
Cdd:COG4942 164 ALRA-ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE----ELEALIARLEAEAAA 238
|
....
gi 1207141765 1657 ADKA 1660
Cdd:COG4942 239 AAER 242
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2227-2442 |
5.24e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2227 DKQKSVLDVELKRLKQEvsdaikqkAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEE--AENMKKL 2304
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKE--------QQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQkqAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2305 AEEAARLNIEAQeaarlrQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQr 2384
Cdd:PRK09510 141 AAAAAKAKAEAE------AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA- 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 2385 ldqetegfqkslEAERKrqleitAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2442
Cdd:PRK09510 214 ------------EAKKK------AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAA 253
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1475-1724 |
5.36e-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: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1475 AKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAE 1554
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1555 EELK-RKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAE----LEKQRQIQVVEEVAKKTAATQLESKQVALTARL 1629
Cdd:COG4942 97 AELEaQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkyLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1630 EESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEAnkktaaqeeaekqkeeaKRE 1709
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA-----------------AAA 239
|
250
....*....|....*
gi 1207141765 1710 AKKRAKAEEAALKQK 1724
Cdd:COG4942 240 AERTPAAGFAALKGK 254
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1679-2097 |
5.59e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1679 LRLRLQAE-EEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAE------ETAKQKLAAEQE 1751
Cdd:COG4717 47 LLERLEKEaDELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEaeleelREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1752 LIRLRADFEHAEQQRTVLDDELQRLKN---DVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNT--------- 1819
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLaeeleelqq 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1820 --EKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAArQRAEAEKILKEKLTAINEATRLKTEAEIAL---- 1893
Cdd:COG4717 207 rlAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1894 ------------KEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDT-----ELDRQKKIVEETLkQ 1956
Cdd:COG4717 286 lallflllarekASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRieelqELLREAEELEEEL-Q 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1957 RKVVEEEIHILkLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEE 2036
Cdd:COG4717 365 LEELEQEIAAL-LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEE 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141765 2037 AARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQvilvQEAAQKCSAAEQKAQNVLVQQ 2097
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQELE----ELKAELRELAEEWAALKLALE 500
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
166-274 |
5.66e-06 |
|
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: 48.26 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 166 DIQVNGQSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIA 244
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|
gi 1207141765 245 ERDLGVTRLLDPEDVDVPHPDEKSIITYVS 274
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLS 107
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1529-1744 |
6.30e-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: 52.26 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1529 RNAAQEEAEKLRKQVAE----ETQKKRKAEEELKRkseAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQaELEKQRQIQ 1604
Cdd:pfam15709 328 REQEKASRDRLRAERAEmrrlEVERKRREQEEQRR---LQQEQLERAEKMREELELEQQRRFEEIRLRKQ-RLEEERQRQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1605 VVEEvakKTAATQLESKQVALTARLEESLKNEQvmviQLQEeaehlKKQQAEADKAREQAEKELETWRQKANEALRLRLQ 1684
Cdd:pfam15709 404 EEEE---RKQRLQLQAAQERARQQQEEFRRKLQ----ELQR-----KKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEM 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1685 AEEEankktaaqeEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQ 1744
Cdd:pfam15709 472 AEEE---------RLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1783-2652 |
6.34e-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: 52.74 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1783 AVKQKKELEEELIKVRKEMEILlQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKlRSVAEEAKKQRQIAEEEAA 1862
Cdd:TIGR00606 170 ALKQKFDEIFSATRYIKALETL-RQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITS-KEAQLESSREIVKSYENEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1863 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEE-------------EGYQRKVLEDQaaQHKQAIE 1929
Cdd:TIGR00606 248 DPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvfqgtdeqlndlyHNHQRTVREKE--RELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1930 EKIGQLKKSSdTELDRQKK--IVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKA-KAEEEA 2006
Cdd:TIGR00606 326 RELEKLNKER-RLLNQEKTelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTlVIERQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2007 EKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAK-KQKEIAEKEAEKQVILVQEAAQKCSA 2085
Cdd:TIGR00606 405 DEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKfVIKELQQLEGSSDRILELDQELRKAE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2086 AEqkaqnvLVQQNKDSMAQDKLKEEF----EKA---KKLAQEAEK-AKDNAEKEA-----ALLHKKAEEAERQKKAAEAE 2152
Cdd:TIGR00606 485 RE------LSKAEKNSLTETLKKEVKslqnEKAdldRKLRKLDQEmEQLNHHTTTrtqmeMLTKDKMDKDEQIRKIKSRH 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2153 AAKQAKAQEDAEKlRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSv 2232
Cdd:TIGR00606 559 SDELTSLLGYFPN-KKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQD- 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2233 LDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKD------NTKKLLEEEAENMKKLAE 2306
Cdd:TIGR00606 637 EESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAElqefisDLQSKLRLAPDKLKSTES 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2307 EAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKD--QAQVEAQKLLEAKKEMQQR 2384
Cdd:TIGR00606 717 ELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtiMPEEESAKVCLTDVTIMER 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2385 LDQETEGFQKSLEAERKR------QLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTV 2458
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKlqgsdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQI 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2459 VE------KLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMAN-------VQQEQLQQEKTILQQSFFA 2525
Cdd:TIGR00606 877 GTnlqrrqQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISsketsnkKAQDKVNDIKEKVKNIHGY 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2526 EKETllkkEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQ----------------KE 2589
Cdd:TIGR00606 957 MKDI----ENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQErwlqdnltlrkrenelKE 1032
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141765 2590 AEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEE 2652
Cdd:TIGR00606 1033 VEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2295-2431 |
6.60e-06 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 52.31 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2295 EEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAA------------KLKAEAEKLQK 2362
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADtsspkedkqvaeNQKREIEKAQI 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141765 2363 QKDQAQVEAQKLLEAKKE--MQQRLDQETEGFQKSLEAERKRqLEITAEAEKLKVKVtqlsDAQSKAEEEA 2431
Cdd:pfam05262 289 EIKKNDEEALKAKDHKAFdlKQESKASEKEAEDKELEAQKKR-EPVAEDLQKTKPQV----EAQPTSLNED 354
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
40-165 |
6.70e-06 |
|
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: 48.06 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 40 ERDRVQKKTFTKWVNKHLVKHWkaeaqrhITDLYEDLRDGHNLISLLEVLSgetLPRERDVVRNSRLPREKGRMRfhKLQ 119
Cdd:cd21329 2 EGESSEERTFRNWMNSLGVNPY-------VNHLYSDLCDALVIFQLYEMTR---VPVDWGHVNKPPYPALGGNMK--KIE 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207141765 120 NVQIALDFLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 165
Cdd:cd21329 70 NCNYAVELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1594-1814 |
6.80e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.73 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1594 QAELEKQRQIQVveevakKTAATQLESKQVALTARLEESLKNEQvmviQLQEEaehlKKQQAEADKAREQAEKELETWRQ 1673
Cdd:PRK09510 74 AKRAEEQRKKKE------QQQAEELQQKQAAEQERLKQLEKERL----AAQEQ----KKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1674 KANEALRLRLQAEEEAnkktaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQEli 1753
Cdd:PRK09510 140 KAAAAAKAKAEAEAKR-----------------AAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAK-- 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141765 1754 rlradfEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKE 1814
Cdd:PRK09510 201 ------KKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2162-2635 |
6.83e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.92 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2162 DAEKLRKEAEKEASRRAEAEAAALKLK---------QEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVqlDETDKQKSV 2232
Cdd:pfam12128 235 GIMKIRPEFTKLQQEFNTLESAELRLShlhfgyksdETLIASRQEERQETSAELNQLLRTLDDQWKEKR--DELNGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2233 LDVELKRLKQEVSDAIKQKAQVEDE-LSKVKIQMEDLLKLKLKIEKENQELmkkdkdntkKLLEEEAENMKKlAEEAARL 2311
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERL---------KALTGKHQDVTA-KYNRRRS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2312 NIEAQEAARLRQIaESDLAKQRELAEKMLEEKKQAIQeaaKLKAE-AEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQET- 2389
Cdd:pfam12128 383 KIKEQNNRDIAGI-KDKLAKIREARDRQLAVAEDDLQ---ALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATa 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2390 --------EGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEK-HTVVE 2460
Cdd:pfam12128 459 tpelllqlENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQaGTLLH 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2461 KLevqRLQSKQEADGLHKAIADLEKEKeklkkeaADLQKQSKEMANVQQEQLQQEKTILQQ----SFFAEKETLlkkeka 2536
Cdd:pfam12128 539 FL---RKEAPDWEQSIGKVISPELLHR-------TDLDPEVWDGSVGGELNLYGVKLDLKRidvpEWAASEEEL------ 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2537 ieeekKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRieqEKLLA 2616
Cdd:pfam12128 603 -----RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK---NKALA 674
|
490
....*....|....*....
gi 1207141765 2617 EENKNLREKLQQLQSSQKA 2635
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQ 693
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1642-1931 |
6.98e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1642 QLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLR-----LQ---AEEEANKKTAAQEEAEKQKEEAKREAKKR 1713
Cdd:PRK02224 217 ELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEaeiedLRetiAETEREREELAEEVRDLRERLEELEEERD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1714 AKAEEAAL----------------KQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLK 1777
Cdd:PRK02224 297 DLLAEAGLddadaeavearreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1778 NDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsnteksKQLLESEAAKMRE-LAEEATKLRSVAEEAKKQRQI 1856
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF--------LEELREERDELRErEAELEATLRTARERVEEAEAL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1857 AEE-----------------EAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAEnDRLKRKAEeegyQRKVLED 1919
Cdd:PRK02224 449 LEAgkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAE-DRIERLEE----RREDLEE 523
|
330
....*....|..
gi 1207141765 1920 QAAQHKQAIEEK 1931
Cdd:PRK02224 524 LIAERRETIEEK 535
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1708-2143 |
7.18e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 52.22 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1708 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQK 1787
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1788 KELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAE 1867
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1868 AEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQK 1947
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1948 KIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKV 2027
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2028 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKL 2107
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430
....*....|....*....|....*....|....*.
gi 1207141765 2108 KEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAE 2143
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAAL 517
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2033-2577 |
7.31e-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: 52.42 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2033 AEEEAARQHKAAQEEVGRLMKLAEEAkkQKEIAEKEAEKQVILVQEAAQKcsaAEQKAQNVLVQQNKDSMAQ-------- 2104
Cdd:pfam05483 206 AENARLEMHFKLKEDHEKIQHLEEEY--KKEINDKEKQVSLLLIQITEKE---NKMKDLTFLLEESRDKANQleektklq 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2105 -DKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAE---KEASRRAEA 2180
Cdd:pfam05483 281 dENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSfvvTEFEATTCS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2181 EAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVK----VQLDE-------------TDKQKSVLDVELKRLKQE 2243
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKnnkeVELEElkkilaedeklldEKKQFEKIAEELKGKEQE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2244 VSDAIKQKaqvEDELSKVKIQMEDLLKLKLKIEKENQElMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQ 2323
Cdd:pfam05483 441 LIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVED-LKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2324 IAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQ 2403
Cdd:pfam05483 517 KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2404 LEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQ--ADEIKIRLQETEKHTSEK------HTVVEKLEVQRLQSKQEADG 2475
Cdd:pfam05483 597 NNLKKQIENKNKNIEELHQENKALKKKGSAENKQlnAYEIKVNKLELELASAKQkfeeiiDNYQKEIEDKKISEEKLLEE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2476 LHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQqsffaEKETLLKKEKAIEEEKKKLEKQFEDEVKKA 2555
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIE-----ERDSELGLYKNKEQEQSSAKAALEIELSNI 751
|
570 580
....*....|....*....|..
gi 1207141765 2556 EALKAEQERQRKLMEEERKKLQ 2577
Cdd:pfam05483 752 KAELLSLKKQLEIEKEEKEKLK 773
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2213-2642 |
7.79e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2213 EEELVKVKVQLDETDKQKSvldvELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKK 2292
Cdd:PRK02224 212 ESELAELDEEIERYEEQRE----QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2293 LLEEEAENMKKLAE-EAARLNIEAQEAARlrqiaeSDLAKQRELAEKMLEEKKQAIQEAAKlkaEAEKLQKQKDQAQVEA 2371
Cdd:PRK02224 288 LEELEEERDDLLAEaGLDDADAEAVEARR------EELEDRDEELRDRLEECRVAAQAHNE---EAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2372 QKLLEAKKEmqqrLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKH 2451
Cdd:PRK02224 359 EELREEAAE----LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2452 TSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLqkqSKEMANVQQEQLQQEKTILQQSFFAEketll 2531
Cdd:PRK02224 435 LRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEEL---EAELEDLEEEVEEVEERLERAEDLVE----- 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2532 kkekaieeekkkLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQ 2611
Cdd:PRK02224 507 ------------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
410 420 430
....*....|....*....|....*....|....*
gi 1207141765 2612 EKLLAE--ENKNLREKLQQLQSSQK--ASYTKEIE 2642
Cdd:PRK02224 575 AELNSKlaELKERIESLERIRTLLAaiADAEDEIE 609
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2195-2403 |
8.55e-06 |
|
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: 51.38 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2195 MAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAikQKAQVEDELSKVKIQMEdllklklk 2274
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAE--KAAKQAEQAAKQAEEKQ-------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2275 iekeNQELMKKDKDNTKKLLEEEAENMKKLAEEAARL-----NIEAQEAARLRQ-----IAESDLAKQRELAEKMLEEKK 2344
Cdd:TIGR02794 119 ----KQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQaeeeaKAKAAAEAKKKAeeakkKAEAEAKAKAEAEAKAKAEEA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141765 2345 QAIQEAAKLKAEAEklQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQ 2403
Cdd:TIGR02794 195 KAKAEAAKAKAAAE--AAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGG 251
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2498-2664 |
1.03e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.88 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2498 QKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQ 2577
Cdd:pfam15709 354 RREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2578 SAMDaaiKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKnlREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMT 2657
Cdd:pfam15709 434 ELQR---KKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAE--EERLEYQRQKQEAEEKARLEAEERRQKEEEAARLA 508
|
....*..
gi 1207141765 2658 MVETTKK 2664
Cdd:pfam15709 509 LEEAMKQ 515
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2280-2647 |
1.05e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2280 QELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAES--DLAKQRELAEKMLEEKKQAIQ------EAA 2351
Cdd:COG4717 56 DELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEleELEAELEELREELEKLEKLLQllplyqELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2352 KLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEA 2431
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2432 KKFKKQADEIKIRLQETEKhTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAA--------------DL 2497
Cdd:COG4717 216 EEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllallfllLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2498 QKQSKEMANVQQEQLQQEKTILQQsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKA-----EALKAEQERQRKLMEEE 2572
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEE---EELEELLAALGLPPDLSPEELLELLDRIEELqellrEAEELEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2573 RKKLQSAMDA-----------AIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENknLREKLQQLQSSQKASYTKEI 2641
Cdd:COG4717 372 IAALLAEAGVedeeelraaleQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELE 449
|
....*.
gi 1207141765 2642 EIQTDK 2647
Cdd:COG4717 450 ELREEL 455
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1625-1963 |
1.06e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1625 LTARLEESLkneqvmviqlQEEAEHLKKQQAeadkAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQeeaekqke 1704
Cdd:pfam07888 32 LQNRLEECL----------QERAELLQAQEA----ANRQREKEKERYKRDREQWERQRRELESRVAELKEEL-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1705 eakreAKKRAKAEEAALKQKEAAEMelgnQRKMAEETA---KQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVN 1781
Cdd:pfam07888 90 -----RQSREKHEELEEKYKELSAS----SEELSEEKDallAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1782 SAVKQKKELEEElikvRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAkkQRQIAEEEA 1861
Cdd:pfam07888 161 KAGAQRKEEEAE----RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA--HRKEAENEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1862 ARQRAEAekiLKEKLTAINEATR-LKTEaeiaLKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQ------ 1934
Cdd:pfam07888 235 LLEELRS---LQERLNASERKVEgLGEE----LSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARwaqere 307
|
330 340 350
....*....|....*....|....*....|
gi 1207141765 1935 -LKKSSDTELDRQKKIVEETLKQRKVVEEE 1963
Cdd:pfam07888 308 tLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1430-1890 |
1.07e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1430 ANELKTKMKDEVSKRQDVA-----VDSEKQKHN-IQRELQELK---TLSEQEIKAKS---QQVEEALLSRTRIE---EEI 1494
Cdd:PRK04863 278 ANERRVHLEEALELRRELYtsrrqLAAEQYRLVeMARELAELNeaeSDLEQDYQAASdhlNLVQTALRQQEKIEryqADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1495 HIIRLQLETTMKQKNTAETELLQLRAKAvdadklrNAAQEEAEKLRKQVAEETQkkrkAEEELKRKSeaekdaakekkka 1574
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQEENEARA-------EAAEEEVDELKSQLADYQQ----ALDVQQTRA------------- 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1575 ledlekfkLQAEEAerhlKQAeLEKQRQIQVVEEVAKKTAATQLEskqvALTARLEEslkneqvmviqLQEEAEHLKKQQ 1654
Cdd:PRK04863 414 --------IQYQQA----VQA-LERAKQLCGLPDLTADNAEDWLE----EFQAKEQE-----------ATEELLSLEQKL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1655 AEADKAREQAEKELETWRQKANEALRLrlQAEEEAnkktaaqeeaekqkeeakREAKKRAKAEEAALKQKEAAEMELGnq 1734
Cdd:PRK04863 466 SVAQAAHSQFEQAYQLVRKIAGEVSRS--EAWDVA------------------RELLRRLREQRHLAEQLQQLRMRLS-- 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1735 rkmaeeTAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEillQQKSKAEKE 1814
Cdd:PRK04863 524 ------ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALR---QQLEQLQAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1815 TMSNTEKSKQLLESEAA--KMRELAEEATK--------LRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATR 1884
Cdd:PRK04863 595 IQRLAARAPAWLAAQDAlaRLREQSGEEFEdsqdvteyMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPR 674
|
....*.
gi 1207141765 1885 LKTEAE 1890
Cdd:PRK04863 675 LNALAE 680
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1342-1918 |
1.09e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 51.67 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1342 KAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELE----KQKQLAE 1417
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlKKKYLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1418 THAKAIAK--AEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEqEIKAKSQQVEEALLS-----RTRI 1490
Cdd:pfam05557 88 LNKKLNEKesQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLD-LLKAKASEAEQLRQNlekqqSSLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1491 EEEIHIIRLQLETTMKQKNTAETELLQLR-AKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAeEELKRKSEAEKDAAK 1569
Cdd:pfam05557 167 EAEQRIKELEFEIQSQEQDSEIVKNSKSElARIPELEKELERLREHNKHLNENIENKLLLKEEV-EDLKRKLEREEKYRE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1570 EKKKALEDLEKFKLQAEEAERhlkqaeLEKQRQIQVVEEVAKKTAATQLESKQVALTAR---LEESLKNEQVMVIQLQEE 1646
Cdd:pfam05557 246 EAATLELEKEKLEQELQSWVK------LAQDTGLNLRSPEDLSRRIEQLQQREIVLKEEnssLTSSARQLEKARRELEQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1647 AEHLKKQQAEADKAREQAEKELETWRQKANEALRLR--LQAEEEANKKTAAQEEAEKQKEEAKREAKK---RAKAEEAAL 1721
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgYRAILESYDKELTMSNYSPQLLERIEEAEDmtqKMQAHNEEM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1722 K-QKEAAEMELGNQRKMAEetakqklAAEQELIRLRADFEHAEQQRTvlddelqrlKNDVNSAVKQKKELEEELIKVRKE 1800
Cdd:pfam05557 400 EaQLSVAEEELGGYKQQAQ-------TLERELQALRQQESLADPSYS---------KEEVDSLRRKLETLELERQRLREQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1801 MEILLQQKSKAEKETMSNTEKSK--QLLESEAAKMRE-LAEEATKLRsvaeeakkqrqiAEEEAARQRAEAEKILKEKLT 1877
Cdd:pfam05557 464 KNELEMELERRCLQGDYDPKKTKvlHLSMNPAAEAYQqRKNQLEKLQ------------AEIERLKRLLKKLEDDLEQVL 531
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1207141765 1878 AINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLE 1918
Cdd:pfam05557 532 RLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQAKIQE 572
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2281-2455 |
1.11e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.49 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2281 ELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEA--E 2358
Cdd:pfam15709 351 ERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2359 KLQKQKDQAQVEAQKLLEAKKEMQQRLDQEtegfqksLEAERKRQLEItAEAEKLKVKvTQLSDAQSKAEEEAKKFKKQA 2438
Cdd:pfam15709 431 KLQELQRKKQQEEAERAEAEKQRQKELEMQ-------LAEEQKRLMEM-AEEERLEYQ-RQKQEAEEKARLEAEERRQKE 501
|
170
....*....|....*...
gi 1207141765 2439 DE-IKIRLQETEKHTSEK 2455
Cdd:pfam15709 502 EEaARLALEEAMKQAQEQ 519
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1801-2133 |
1.13e-05 |
|
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: 51.66 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1801 MEILLQQKSKAEKETMSNTEKSKQlleseaAKMRELAEEatklrsVAEEAKKQRQIAEEEAARQRAeaekiLKEKLTAIN 1880
Cdd:pfam17380 275 LHIVQHQKAVSERQQQEKFEKMEQ------ERLRQEKEE------KAREVERRRKLEEAEKARQAE-----MDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1881 EATRLKTEAE-----IALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQlkkssDTELDRQKKIVEETlK 1955
Cdd:pfam17380 338 EQERMAMERErelerIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ-----ELEAARKVKILEEE-R 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1956 QRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLalEEEKKRKEAEAKVKQIQAAEE 2035
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ--EEERKRKKLELEKEKRDRKRA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2036 EAARQHKAAQEEVGRLMKLAEEAKKQKeIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ-DKLKEEFEKA 2114
Cdd:pfam17380 490 EEQRRKILEKELEERKQAMIEEERKRK-LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQmRKATEERSRL 568
|
330
....*....|....*....
gi 1207141765 2115 KKLAQEAEKAKDNAEKEAA 2133
Cdd:pfam17380 569 EAMEREREMMRQIVESEKA 587
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1141-1801 |
1.14e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.97 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1141 AEDILNKYENQLREVNKVPVNEKEI-EASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQ 1219
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKEIlEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEV 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1220 L------------VGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYD----------WLIRWIADAKQRQDKLHAVP 1277
Cdd:TIGR00606 504 KslqnekadldrkLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKiksrhsdeltSLLGYFPNKKQLEDWLHSKS 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1278 iGGSKGLQEQLTQEKKLLEEIEKNKD--------KVEDCQKFAKGYIDAIKDYELQlVTYKALVEPIASPLKKAKMESAS 1349
Cdd:TIGR00606 584 -KEINQTRDRLAKLNKELASLEQNKNhinnelesKEEQLSSYEDKLFDVCGSQDEE-SDLERLKEEIEKSSKQRAMLAGA 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1350 DDIIQEYVTLRTRYSE----LMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAK 1425
Cdd:TIGR00606 662 TAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1426 AEQEANELKTKMkdevskrQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTM 1505
Cdd:TIGR00606 742 KEKEIPELRNKL-------QKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1506 KQKNTAETELLQLRAKAVDAD-KLRNAAQ--EEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFK 1582
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQhELDTVVSkiELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELS 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1583 LQAEEAERHLKQAElekqrqiqvVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHL--------KKQQ 1654
Cdd:TIGR00606 895 TEVQSLIREIKDAK---------EQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgymkdieNKIQ 965
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1655 AEADKAREQAEKELETWRQKANEALRLRLQAEEEankktaaqeeaekqkEEAKREAKKRAKAEEAALkQKEAAEMELGNQ 1734
Cdd:TIGR00606 966 DGKDDYLKQKETELNTVNAQLEECEKHQEKINED---------------MRLMRQDIDTQKIQERWL-QDNLTLRKRENE 1029
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141765 1735 RKMAEETAKQKLAAEQELIRLRADFEHAEqqrtvLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM 1801
Cdd:TIGR00606 1030 LKEVEEELKQHLKEMGQMQVLQMKQEHQK-----LEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1607-1829 |
1.23e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.49 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1607 EEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQA- 1685
Cdd:pfam15709 317 EEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRl 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1686 ------EEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEEtaKQKLAAEQELIRLRADF 1759
Cdd:pfam15709 397 eeerqrQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKEL--EMQLAEEQKRLMEMAEE 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1760 EHAEQQRtvlddelqrlkndvnsavkQKKELEEeliKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESE 1829
Cdd:pfam15709 475 ERLEYQR-------------------QKQEAEE---KARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1431-1978 |
1.29e-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: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1431 NELKTKmKDEVSKRQDVAVDSEKQKHNIQRELQELKTlSEQEIKAKSQQVEEALlsrTRIEEEIHIIRLQLETTMKQKNT 1510
Cdd:TIGR04523 47 NELKNK-EKELKNLDKNLNKDEEKINNSNNKIKILEQ-QIKDLNDKLKKNKDKI---NKLNSDLSKINSEIKNDKEQKNK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1511 AETELLQLRAKAvdadklrnaaqEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAER 1590
Cdd:TIGR04523 122 LEVELNKLEKQK-----------KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1591 HLKQAELEKQRQIQVVEEvakktaatqLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAeKELET 1670
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKK---------KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL-NQLKD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1671 WRQKANEALRLRLQAEEEANKKTAAQEEAEkqkeeakreakKRAKAEEAALKQKEAAEMelgnQRKMAEETAKQklaaEQ 1750
Cdd:TIGR04523 261 EQNKIKKQLSEKQKELEQNNKKIKELEKQL-----------NQLKSEISDLNNQKEQDW----NKELKSELKNQ----EK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1751 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKaEKETMSNTEKSKQLLESea 1830
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS-YKQEIKNLESQINDLES-- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1831 aKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEkltaINEATRLKTEAEIALKEKEAENDRLKRKAEEE 1910
Cdd:TIGR04523 399 -KIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE----IKDLTNQDSVKELIIKNLDNTRESLETQLKVL 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 1911 GYQRKVLEDQAAQHKQAIEEKIGQLKKssdteLDRQKKIVEETLkqrKVVEEEIHILKLNFEKASSGK 1978
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKK-----LNEEKKELEEKV---KDLTKKISSLKEKIEKLESEK 533
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1411-1802 |
1.35e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.72 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1411 KQKQLAEThAKAIAKAEQEANELKTKMKDevsKRQDVavdSEKQKHniqreLQELKTLSEQEIKAKSQQVEEALL----- 1485
Cdd:PRK10246 438 QQKRLAQL-QVAIQNVTQEQTQRNAALNE---MRQRY---KEKTQQ-----LADVKTICEQEARIKDLEAQRAQLqagqp 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1486 -------SRTRIEE----EIHIIRLQLETTMKQKNTAETELLQLRAKaVDAdklrnaaqeeaekLRKQV---AEETQKKR 1551
Cdd:PRK10246 506 cplcgstSHPAVEAyqalEPGVNQSRLDALEKEVKKLGEEGAALRGQ-LDA-------------LTKQLqrdESEAQSLR 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1552 KAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAT-QLESKQVALTARLE 1630
Cdd:PRK10246 572 QEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQqQIEQRQQQLLTALA 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1631 E-SLK-----NEQVMVIQLQEEAEHLKKQQAEADKAREQ---------------------AEKELETWRQKANEALRLR- 1682
Cdd:PRK10246 652 GyALTlpqedEEASWLATRQQEAQSWQQRQNELTALQNRiqqltplletlpqsddlphseETVALDNWRQVHEQCLSLHs 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1683 ---------LQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAE---ETAKQKLAAEQ 1750
Cdd:PRK10246 732 qlqtlqqqdVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQtlvTQTAQALAQHQ 811
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141765 1751 ----ELIRLRADFEHAEQQRTVLDDEL-----------QRLKNDVNSAvKQKKELEEELIKVRKEME 1802
Cdd:PRK10246 812 qhrpDGLDLTVTVEQIQQELAQLAQQLrenttrqgeirQQLKQDADNR-QQQQALMQQIAQATQQVE 877
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1747-1946 |
1.35e-05 |
|
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: 50.61 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1747 AAEQELIRLRADFEHAEQQRTVLDDELQRLKndvnSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLL 1826
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQA----EEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1827 ESEA--AKMRELAEEATKLRSVAEEAKKQRQI-----AEEEAARQRAEAEKILKEKLTAINEATRlKTEAEIALKEKEAE 1899
Cdd:TIGR02794 123 EAKAkqAAEAKAKAEAEAERKAKEEAAKQAEEeakakAAAEAKKKAEEAKKKAEAEAKAKAEAEA-KAKAEEAKAKAEAA 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207141765 1900 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQ 1946
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2164-2436 |
1.45e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.29 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2164 EKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKV---KVQLDETDKQKSVLDVELKRL 2240
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVkelKEERDELNEKLNELREELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2241 KQEVSDAIKQKAQVeDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLleEEAENMKKLAEEAARLNIEAQEAAR 2320
Cdd:COG1340 98 RKELAELNKAGGSI-DKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKEL--EKAKKALEKNEKLKELRAELKELRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2321 LRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQetegFQKSLEAER 2400
Cdd:COG1340 175 EAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE----LRKELKKLR 250
|
250 260 270
....*....|....*....|....*....|....*.
gi 1207141765 2401 KRQLEITAEAEKlkvkvtqlSDAQSKAEEEAKKFKK 2436
Cdd:COG1340 251 KKQRALKREKEK--------EELEEKAEEIFEKLKK 278
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2203-2607 |
1.50e-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: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2203 EKTLKQKSSVEEELVKVKVQLDETDKQK-----SVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEK 2277
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2278 ENQELMKKDKDNTKKLLEEEAEN------MKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAA 2351
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENqsykqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2352 KLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQetegFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEA 2431
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV----LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2432 KKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQE--ADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQ 2509
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2510 EQLQQEKTILQQsfFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKE 2589
Cdd:TIGR04523 593 QKEKEKKDLIKE--IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKE 670
|
410
....*....|....*...
gi 1207141765 2590 AEEEMNGKQKEMQDLEKK 2607
Cdd:TIGR04523 671 SKTKIDDIIELMKDWLKE 688
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1648-1934 |
1.64e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 50.75 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1648 EHLKKQQAEadKAREQAEKELetwrqKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAAL-KQKEA 1726
Cdd:PRK07735 8 EDLKKEAAR--RAKEEARKRL-----VAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALaKQKRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1727 A-----EMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM 1801
Cdd:PRK07735 81 GteevtEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1802 EILLQQKSKAEKETMSNTEKSKQllesEAAKMRELAEEATKLRSVAEEAKKqrqiaeeeAARQRAEAEKILKEKLTAIN- 1880
Cdd:PRK07735 161 DKEKAKAKAAAAAKAKAAALAKQ----KAAEAGEGTEEVTEEEKAKAKAKA--------AAAAKAKAAALAKQKASQGNg 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141765 1881 --EATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAA-------QHKQAIEEKIGQ 1934
Cdd:PRK07735 229 dsGDEDAKAKAIAAAKAKAAAAARAKTKGAEGKKEEEPKQEEPSvnqpylnKYVEVIKEKLGE 291
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2188-2383 |
1.64e-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: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2188 KQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMED 2267
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2268 LLKLKLKIEK-----------ENQELMKKDKDNTKKLLEE------EAENMK-KLAEEAARLNIEAQEAARLRQIAESDL 2329
Cdd:COG3883 98 SGGSVSYLDVllgsesfsdflDRLSALSKIADADADLLEElkadkaELEAKKaELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207141765 2330 AKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQ 2383
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
199-275 |
1.70e-05 |
|
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: 46.53 E-value: 1.70e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141765 199 DNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSiAERDLGVTRLLDPEDVDVPHPDEKSIITYVSS 275
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAYAAQ 95
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1593-1749 |
1.74e-05 |
|
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: 50.23 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1593 KQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWR 1672
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1673 QKANEALRLRLQAE------EEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKL 1746
Cdd:TIGR02794 126 AKQAAEAKAKAEAEaerkakEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKA 205
|
...
gi 1207141765 1747 AAE 1749
Cdd:TIGR02794 206 AAE 208
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4165-4193 |
1.85e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.85e-05
10 20
....*....|....*....|....*....
gi 1207141765 4165 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4193
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1423-1689 |
2.10e-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: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1423 IAKAEQEaNELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQElktlsEQEIKAKsQQVEEALLSRTRIEEEIhiirlqle 1502
Cdd:pfam15709 325 LEKREQE-KASRDRLRAERAEMRRLEVERKRREQEEQRRLQQ-----EQLERAE-KMREELELEQQRRFEEI-------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1503 ttmkqkntaetellQLRAKAVDADKLRNAAQEEAEKLRKQVAEEtqKKRKAEEELKRKSEAEKDaakekkkaledlekfK 1582
Cdd:pfam15709 390 --------------RLRKQRLEEERQRQEEEERKQRLQLQAAQE--RARQQQEEFRRKLQELQR---------------K 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1583 LQAEEAERhlkqAELEKQRQIQvveevakktaatqleskqvaltarLEESLKNEQVMVIQLQEEA--EHLKKQQAEADKA 1660
Cdd:pfam15709 439 KQQEEAER----AEAEKQRQKE------------------------LEMQLAEEQKRLMEMAEEErlEYQRQKQEAEEKA 490
|
250 260 270
....*....|....*....|....*....|....
gi 1207141765 1661 REQAEKEletwRQKANEALRLRL-----QAEEEA 1689
Cdd:pfam15709 491 RLEAEER----RQKEEEAARLALeeamkQAQEQA 520
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2028-2434 |
2.13e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 51.21 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2028 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEK--QVI-----LVQEAAQKCSAAEQKAQNVLVQQNKD 2100
Cdd:PRK10929 26 KQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQyqQVIdnfpkLSAELRQQLNNERDEPRSVPPNMSTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2101 SMAQDKLK---EEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEeaerqkkaaeaeaakqakaqedAEKLRKEAEKEasrr 2177
Cdd:PRK10929 106 ALEQEILQvssQLLEKSRQAQQEQDRAREISDSLSQLPQQQTE----------------------ARRQLNEIERR---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2178 aeaeaaaLKLKQEADS--EMAKYKKLAEKTLKQKSSVEE-ELVkvkvQLDETDKQksvldvELKRLKQEVsdAIKQKAQV 2254
Cdd:PRK10929 160 -------LQTLGTPNTplAQAQLTALQAESAALKALVDElELA----QLSANNRQ------ELARLRSEL--AKKRSQQL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2255 EDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLeeeAENMKKLAEEAARLNIEAQE----AARLRQIAESDLa 2330
Cdd:PRK10929 221 DAYLQALRNQLNSQRQREAERALESTELLAEQSGDLPKSI---VAQFKINRELSQALNQQAQRmdliASQQRQAASQTL- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2331 kQRELAEKMLEEKKQ------AIQEAakLKAEAEKL-------QKQKDQAQVEAQKL-LEAKKEMQQRLDQE-------- 2388
Cdd:PRK10929 297 -QVRQALNTLREQSQwlgvsnALGEA--LRAQVARLpempkpqQLDTEMAQLRVQRLrYEDLLNKQPQLRQIrqadgqpl 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141765 2389 TEGFQKSLEAERKRQ---------------LEITaeaeKLKVKVTQLSDAQSKAEEEAKKF 2434
Cdd:PRK10929 374 TAEQNRILDAQLRTQrellnsllsggdtliLELT----KLKVANSQLEDALKEVNEATHRY 430
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1160-1330 |
2.19e-05 |
|
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: 48.60 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1160 VNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQ----RATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFAQI 1235
Cdd:cd00176 16 LSEKEELLSSTDYGDDLESVEALLKKHEALEAELAaheeRVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1236 ELRQRELDLLNRQMQAYRESYDwLIRWIADAKQRQDKLhaVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGY 1315
Cdd:cd00176 96 EERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEEL 172
|
170
....*....|....*
gi 1207141765 1316 IDAIKDYELQLVTYK 1330
Cdd:cd00176 173 LEEGHPDADEEIEEK 187
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1163-1852 |
2.26e-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: 51.11 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1163 KEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATE-VNKRMSQL-HSERdveLEHYRQLVGNLRERWQAVFAQIELRQR 1240
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhLNLVQTALrQQEK---IERYQEDLEELTERLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1241 ELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQeQLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIK 1320
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ-ALEKARALCGLPDLTPENAEDYLAAFRAKEQQAT 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1321 DYELQLVTY------------KA--LVEPIASPLKKAKMESASDDIIQEY----------VTLRTRYSELMTLSSQYikf 1376
Cdd:COG3096 455 EEVLELEQKlsvadaarrqfeKAyeLVCKIAGEVERSQAWQTARELLRRYrsqqalaqrlQQLRAQLAELEQRLRQQ--- 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1377 iiETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQK-QLAETHAKAIAKA---EQEANELKTKMKdEVSKRQDVAVDSE 1452
Cdd:COG3096 532 --QNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLeELEEQAAEAVEQRselRQQLEQLRARIK-ELAARAPAWLAAQ 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1453 KQKHNIQRELQELKTlSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTA----ETELLQLR--------A 1520
Cdd:COG3096 609 DALERLREQSGEALA-DSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPggaeDPRLLALAerlggvllS 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1521 KAVDADKLRNAAQEEA--------------EKLRKQVAE-------------------------ETQKKR---KAEEELK 1558
Cdd:COG3096 688 EIYDDVTLEDAPYFSAlygparhaivvpdlSAVKEQLAGledcpedlyliegdpdsfddsvfdaEELEDAvvvKLSDRQW 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1559 RKSEAEKDAAKEKKKALEDLEKFKLQAEE-AERHLKQA-ELEK-QR-----------QIQVVEEVAKKTAATQLESKQVA 1624
Cdd:COG3096 768 RYSRFPEVPLFGRAAREKRLEELRAERDElAEQYAKASfDVQKlQRlhqafsqfvggHLAVAFAPDPEAELAALRQRRSE 847
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1625 LTARLEESLKNEQvmviQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEA------NKKTAAQEE 1698
Cdd:COG3096 848 LERELAQHRAQEQ----QLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAqafiqqHGKALAQLE 923
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1699 AEK-------QKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRK-MAEETAKQKLAAEQELI-RLRADFEHAEQQRTVL 1769
Cdd:COG3096 924 PLVavlqsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLGENSDLNeKLRARLEQAEEARREA 1003
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1770 DDELQRLKNDVNSA------------VKQK--KELEEEL----IKVRKEMEIL-------LQQKSKAEKETMSNTEKSKQ 1824
Cdd:COG3096 1004 REQLRQAQAQYSQYnqvlaslkssrdAKQQtlQELEQELeelgVQADAEAEERarirrdeLHEELSQNRSRRSQLEKQLT 1083
|
810 820 830
....*....|....*....|....*....|..
gi 1207141765 1825 LLESEAA----KMRELAEEATKLRSVAEEAKK 1852
Cdd:COG3096 1084 RCEAEMDslqkRLRKAERDYKQEREQVVQAKA 1115
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1402-1557 |
2.30e-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: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1402 MAEMQAELEKQKQLAETHA-KAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKhniQRELQELKTLSEQEIKAKSQQV 1480
Cdd:COG2268 194 IAEIIRDARIAEAEAERETeIAIAQANREAEEAELEQEREIETARIAEAEAELAK---KKAEERREAETARAEAEAAYEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1481 EEALLSRTrIEEEIHIIRLQLETTMKQKNtAETELLQLRA---KAVDADKLRNAAQEEAE------KLRKQvAEETQKKR 1551
Cdd:COG2268 271 AEANAERE-VQRQLEIAEREREIELQEKE-AEREEAELEAdvrKPAEAEKQAAEAEAEAEaeairaKGLAE-AEGKRALA 347
|
....*.
gi 1207141765 1552 KAEEEL 1557
Cdd:COG2268 348 EAWNKL 353
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1676-1908 |
2.30e-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: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1676 NEALRLRLQAEEEANKKTAaqeeaEKQKEEAKREAKKRAKAEEAALKQkeaaEMELGNQRKMAEETAKQKLAAEQeliRL 1755
Cdd:COG2268 188 ALGRRKIAEIIRDARIAEA-----EAERETEIAIAQANREAEEAELEQ----EREIETARIAEAEAELAKKKAEE---RR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1756 RADFEHAEQQRTVlddELQRlkndvnsaVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsntekskqllESEAAKMRE 1835
Cdd:COG2268 256 EAETARAEAEAAY---EIAE--------ANAEREVQRQLEIAEREREIELQEKEAEREE------------AELEADVRK 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141765 1836 LAeeatklrsvaeEAKKQRQIAEEEaarqrAEAEKIlKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAE 1908
Cdd:COG2268 313 PA-----------EAEKQAAEAEAE-----AEAEAI-RAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE 368
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1579-1881 |
2.31e-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: 49.92 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1579 EKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLK-NEQVMVIQLQEEAEHLKKQQAEA 1657
Cdd:pfam13868 43 RRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1658 DKaREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKM 1737
Cdd:pfam13868 123 EK-QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1738 AEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDvnSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMS 1817
Cdd:pfam13868 202 ERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREE--QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQE 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141765 1818 NTEKSKQLLESEAAKMRELAEEATKLRsvAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINE 1881
Cdd:pfam13868 280 EAEKRRMKRLEHRRELEKQIEEREEQR--AAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1624-1930 |
2.39e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1624 ALTARLE-----ESLKNEQVMVIQLQEEAEhlkkQQAEADKAREQAEKELETWRQKANEALRLRLQ---AEEEANKKTaa 1695
Cdd:PRK04863 288 ALELRRElytsrRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQAASDHLNLVQTALRQQEKierYQADLEELE-- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1696 qeeaekqkeeakreakkrAKAEEAALKQKEAAEmelgnQRKMAEEtakQKLAAEQELIRLR---ADFEHA--EQQRTVLD 1770
Cdd:PRK04863 362 ------------------ERLEEQNEVVEEADE-----QQEENEA---RAEAAEEEVDELKsqlADYQQAldVQQTRAIQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1771 --------DELQRLKNDVNSAVKQKKELEEELikVRKEMEIL-----LQQKSKAEKETMSNTEKSKQLLESEAAKM---- 1833
Cdd:PRK04863 416 yqqavqalERAKQLCGLPDLTADNAEDWLEEF--QAKEQEATeellsLEQKLSVAQAAHSQFEQAYQLVRKIAGEVsrse 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1834 -----RELAEEATKLRSVAEEAK---------KQRQIAEEEAARQRAEAEKILKEKLTAINEATRLkteaeiaLKEKEAE 1899
Cdd:PRK04863 494 awdvaRELLRRLREQRHLAEQLQqlrmrlselEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQL-------QEELEAR 566
|
330 340 350
....*....|....*....|....*....|.
gi 1207141765 1900 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE 1930
Cdd:PRK04863 567 LESLSESVSEARERRMALRQQLEQLQARIQR 597
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2302-2453 |
2.48e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2302 KKLAEEAARLNIEAQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEA-----AKLKAEAEKLQKQKDQAQVEAQKLLE 2376
Cdd:COG4913 288 RRLELLEAELEELRAELARLEA-ELERLEARLDALREELDELEAQIRGNggdrlEQLEREIERLERELEERERRRARLEA 366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141765 2377 AKKEMQQRLDQETEGFQksleaerKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTS 2453
Cdd:COG4913 367 LLAALGLPLPASAEEFA-------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1452-1931 |
2.49e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1452 EKQKHNIQRELQELKTLSEQEIKAKSQQVEEAllsrTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNA 1531
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1532 AQ--EEAEKLRKQVAEETQKKRKAEEELKRKSeaekdaakekkkaledlekfklQAEEAERHLKQAELEKQRQIqvveev 1609
Cdd:COG4717 128 LPlyQELEALEAELAELPERLEELEERLEELR----------------------ELEEELEELEAELAELQEEL------ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1610 akktaATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEK-ELETWRQKANEALR-------- 1680
Cdd:COG4717 180 -----EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQlENELEAAALEERLKearlllli 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1681 ----------LRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQ 1750
Cdd:COG4717 255 aaallallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1751 ELIRLRADFEHAEQQRTvLDDELQRLKNDVNSAVkQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQL---LE 1827
Cdd:COG4717 335 SPEELLELLDRIEELQE-LLREAEELEEELQLEE-LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELeeqLE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1828 SEAAKMRELAEEATKlrsvaEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKA 1907
Cdd:COG4717 413 ELLGELEELLEALDE-----EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
490 500
....*....|....*....|....*
gi 1207141765 1908 EEEGYQRKVLEDQA-AQHKQAIEEK 1931
Cdd:COG4717 488 LAEEWAALKLALELlEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1403-1629 |
2.66e-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: 50.15 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1403 AEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELktlsEQEIKAKSQQVEE 1482
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL----EAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1483 AllsRTRIEEEIHIIRLQLETTMKQKNTAETELL------------------QLRAKAVDADKLRnAAQEEAEKLRKQVA 1544
Cdd:COG4942 95 L---RAELEAQKEELAELLRALYRLGRQPPLALLlspedfldavrrlqylkyLAPARREQAEELR-ADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1545 EETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVA 1624
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 1207141765 1625 LTARL 1629
Cdd:COG4942 251 LKGKL 255
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2287-2521 |
2.90e-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: 50.72 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2287 KDNTKKLLEEEAENMKKLAEEAARLNIEAQEAAR----LRQ-IAESDLAKQR-----ELAEKMLEE--KKQAIQEAAKLK 2354
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEevleLEQkLSVADAARRQfekayELVCKIAGEveRSQAWQTARELL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2355 AEAEKLQKQKDQAQVEAQKLLEAKKEM--QQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAK 2432
Cdd:COG3096 502 RRYRSQQALAQRLQQLRAQLAELEQRLrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2433 KFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQeadglhkAIADLEKEKEKLKKEAADL--QKQSKEMANVQQE 2510
Cdd:COG3096 582 ELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGE-------ALADSQEVTAAMQQLLEREreATVERDELAARKQ 654
|
250
....*....|.
gi 1207141765 2511 QLQQEKTILQQ 2521
Cdd:COG3096 655 ALESQIERLSQ 665
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2054-2472 |
3.03e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2054 LAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNA---EK 2130
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAddlEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2131 EAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYK-KLAEKTLKQK 2209
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELReREAELEATLR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2210 SsVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLklklkiekenqelmkkdkdn 2289
Cdd:PRK02224 437 T-ARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVE-------------------- 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2290 tKKLleEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEekkqaiqEAAKLKAEAEKLQKQKDQAQV 2369
Cdd:PRK02224 496 -ERL--ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE-------RAAELEAEAEEKREAAAEAEE 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2370 EAQKLLEAKKEMQQRLdqetegfqksleAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETE 2449
Cdd:PRK02224 566 EAEEAREEVAELNSKL------------AELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR 633
|
410 420
....*....|....*....|...
gi 1207141765 2450 KHTSEKHTVVEKLEVQRLQSKQE 2472
Cdd:PRK02224 634 ERKRELEAEFDEARIEEAREDKE 656
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3090-3125 |
3.05e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 3.05e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1207141765 3090 LNLLEAQAGTGFIIDPVKNQKLTVDEAVKSGVVGPE 3125
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2221-2388 |
3.06e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2221 VQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLE----E 2296
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2297 EAENMKKlAEEAARLNIEAQEAARLrqiaesDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAEKLQKQKDQAQVEAQKLL 2375
Cdd:COG1579 90 EYEALQK-EIESLKRRISDLEDEIL------ELMERIEELEEELAELEAELAELeAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|...
gi 1207141765 2376 EAKKEMQQRLDQE 2388
Cdd:COG1579 163 AEREELAAKIPPE 175
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
838-883 |
3.09e-05 |
|
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: 44.19 E-value: 3.09e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1207141765 838 VQAVCDFKQME---ITVHKGDECALVNNSQPYKWKVRDSSGNEAVVPSI 883
Cdd:cd11768 2 VVALYDFQPIEpgdLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPSN 50
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1540-1748 |
3.11e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.87 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1540 RKQVAEETQKKRKAEEELKRKSeaekdaakekkkaledlekfKLQAEEAERHLKQAELEKQRQIQVVEeVAKKTAATQLE 1619
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERET--------------------EIAIAQANREAEEAELEQEREIETAR-IAEAEAELAKK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1620 skqvaltarleeslkneqvmviqlQEEAEhlkkqqAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEA 1699
Cdd:COG2268 250 ------------------------KAEER------REAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEA 299
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207141765 1700 EKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAA 1748
Cdd:COG2268 300 EREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAE 348
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1142-1948 |
3.15e-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: 50.56 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1142 EDILNKYENQLREVNKVPVN-EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEvnkRMSQLHSERDVELEHYRQL 1220
Cdd:pfam01576 193 EERLKKEEKGRQELEKAKRKlEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALA---RLEEETAQKNNALKKIREL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1221 VGNLRE------RWQAVFAQIELRQREldlLNRQMQAYR-ESYDWLirwiaDAKQRQDKLHavpiggSKGLQEqLTQEKK 1293
Cdd:pfam01576 270 EAQISElqedleSERAARNKAEKQRRD---LGEELEALKtELEDTL-----DTTAAQQELR------SKREQE-VTELKK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1294 LLEEIEKNKD-KVEDCQKFAKGYIDAIKDYELQLVTYKALVEPiasplKKAKMESASDDIIQEYVTLRTRYSELMTLSSQ 1372
Cdd:pfam01576 335 ALEEETRSHEaQLQEMRQKHTQALEELTEQLEQAKRNKANLEK-----AKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1373 YIKFIIETQRRLQDEEKAaeklKEEERKKMAEMQAELEK---------------QKQLA---------------ETHAK- 1421
Cdd:pfam01576 410 LEGQLQELQARLSESERQ----RAELAEKLSKLQSELESvssllneaegkniklSKDVSslesqlqdtqellqeETRQKl 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1422 ----AIAKAEQEANELKTKMKDEVSKRQDVavdsEKQKHNIQRELQELKTLSEQEikakSQQVEEALLSRTRIEEEIHII 1497
Cdd:pfam01576 486 nlstRLRQLEDERNSLQEQLEEEEEAKRNV----ERQLSTLQAQLSDMKKKLEED----AGTLEALEEGKKRLQRELEAL 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1498 RLQLETTM-------KQKNTAETELLQLrakAVDADKLR---NAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDA 1567
Cdd:pfam01576 558 TQQLEEKAaaydkleKTKNRLQQELDDL---LVDLDHQRqlvSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREK 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1568 AKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKtaATQLESKQVALTARLEEslkneqvMVIQLQEEA 1647
Cdd:pfam01576 635 ETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKN--VHELERSKRALEQQVEE-------MKTQLEELE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1648 EHLkkqqaeadKAREQAEKELETWRQKANEALRLRLQAEEEANkktaaqeeaekqkeeakrEAKKRakaeeAALKQKEAA 1727
Cdd:pfam01576 706 DEL--------QATEDAKLRLEVNMQALKAQFERDLQARDEQG------------------EEKRR-----QLVKQVREL 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1728 EMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRtvlDDELQRLKNdvnsAVKQKKELEEELIKVRKEM-EILLQ 1806
Cdd:pfam01576 755 EAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGR---EEAVKQLKK----LQAQMKDLQRELEEARASRdEILAQ 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1807 QKskaeketmsNTEKSKQLLESEAAKMRELAeeatklrSVAEEAKKQRQIAEEEAARQRAEAekiLKEKLTAINEATRLk 1886
Cdd:pfam01576 828 SK---------ESEKKLKNLEAELLQLQEDL-------AASERARRQAQQERDELADEIASG---ASGKSALQDEKRRL- 887
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 1887 tEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKK 1948
Cdd:pfam01576 888 -EARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNK 948
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2305-2510 |
3.19e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2305 AEEAARLNIEAQEAARLRQIAESDLAKQ-RELAEKMLEEKkQAIQEAAKLKAEAEKLQKQKDQAqveAQKLLEAKKEMQQ 2383
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQaEELQQKQAAEQ-ERLKQLEKERLAAQEQKKQAEEA---AKQAALKQKQAEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2384 RLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQlSDAQSKAEEEAKkfKKQADEIKIRLQETEKHTSEKhtvvEKLE 2463
Cdd:PRK09510 137 AAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAE-AEAAKKAAAEAK--KKAEAEAAAKAAAEAKKKAEA----EAKK 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207141765 2464 VQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQE 2510
Cdd:PRK09510 210 KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1040-1622 |
3.29e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1040 ESRTVNRLRQMVDKEPLKACTQRATEQKKVqtelEGIKKDLDKVVEKSEAVLATSQQSS-SAPVLRSEIDITQKKMEHVY 1118
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKA----DEAKKKAEEAKKKADAAKKKAEEAKkAAEAAKAEAEAAADEAEAAE 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1119 GLSSVylDKLKTIDlvirSTQGAEDILNKYEnqlrEVNKVPVNEKEIEASQTQLQKLRSEAEGKQATfdrleEELQRATE 1198
Cdd:PTZ00121 1364 EKAEA--AEKKKEE----AKKKADAAKKKAE----EKKKADEAKKKAEEDKKKADELKKAAAAKKKA-----DEAKKKAE 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1199 VNKRMSQLHSERDvELEHYRQLVGNLRERWQAVFAQIELRQ-RELDLLNRQMQAYRESyDWLIRWIADAKQRQDKLHAVP 1277
Cdd:PTZ00121 1429 EKKKADEAKKKAE-EAKKADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAA 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1278 IGGSKGLQEQLTQEKKLLEEIEK--NKDKVEDCQKF--AKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMESASDDII 1353
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKaeEAKKADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1354 QEyvTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEerkkmaemqaelEKQKQLAETHAKAIAKAEQEANEL 1433
Cdd:PTZ00121 1587 KK--AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA------------EEEKKKVEQLKKKEAEEKKKAEEL 1652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1434 KTKMKDEVSKRQDVAVDSEKQKhniqRELQELKTLSEQEIKAKSQQVEEALLSRtRIEEeihiirlqlettMKQKNTAET 1513
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDK----KKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEE------------LKKKEAEEK 1715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1514 EllqlrakavDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSeaekdaakekkkaledlEKFKLQAEEAERHLK 1593
Cdd:PTZ00121 1716 K---------KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE-----------------EKKKIAHLKKEEEKK 1769
|
570 580
....*....|....*....|....*....
gi 1207141765 1594 QAELEKQRQIQVVEEVAKKTAATQLESKQ 1622
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2031-2209 |
3.32e-05 |
|
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: 49.46 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2031 QAAEEEAARQHK--AAQEEVGRLMKLAEEAKKQkeiAEKEAEKQvilVQEAAQKcSAAEQKAQnvlvqqnkdSMAQDKLK 2108
Cdd:TIGR02794 119 KQAEEAKAKQAAeaKAKAEAEAERKAKEEAAKQ---AEEEAKAK---AAAEAKK-KAEEAKKK---------AEAEAKAK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2109 EEFE---KAKKLAQEAEKAKDNAEKEAAllhKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEaeaaal 2185
Cdd:TIGR02794 183 AEAEakaKAEEAKAKAEAAKAKAAAEAA---AKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGAR------ 253
|
170 180
....*....|....*....|....
gi 1207141765 2186 klKQEADSEMAKYKKLAEKTLKQK 2209
Cdd:TIGR02794 254 --GAAAGSEVDKYAAIIQQAIQQN 275
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2427-2643 |
3.56e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2427 AEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMAN 2506
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2507 VQQEQLQQEKTIlqqsffaekETLLKKEkaieeekkklekQFEDEVKKAEALKAEQERQRKLMEE---ERKKLQSAMDAA 2583
Cdd:COG3883 94 ALYRSGGSVSYL---------DVLLGSE------------SFSDFLDRLSALSKIADADADLLEElkaDKAELEAKKAEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2584 IKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEI 2643
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1583-2450 |
3.62e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.43 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1583 LQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQvALTARlEESLKNEQVMVIQLQEEAEHLKKQQAEADKARE 1662
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRD-QITSK-EAQLESSREIVKSYENELDPLKNRLKEIEHNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1663 ---QAEKELETWRQKANEALRLRLQAEEEAnKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEaaeMELGNQRKMAE 1739
Cdd:TIGR00606 263 kimKLDNEIKALKSRKKQMEKDNSELELKM-EKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRE---LEKLNKERRLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1740 ETAKQKLAAEQELIRLRADFEH-------AEQQRTVLDDELQRLKND------VNSAVKQKKELEEELIKVRKEMEILLQ 1806
Cdd:TIGR00606 339 NQEKTELLVEQGRLQLQADRHQehirardSLIQSLATRLELDGFERGpfserqIKNFHTLVIERQEDEAKTAAQLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1807 QKSKAEKETMSNTE-KSKQLLESEAAKMRELAEEATKLRSVAEEAKK----QRQIAEEEAARQRAEAEKILKEKltaiNE 1881
Cdd:TIGR00606 419 SKERLKQEQADEIRdEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegsSDRILELDQELRKAERELSKAEK----NS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1882 ATRLKTEAEIALKEKEAENDRLKRKAEEEGYQR------KVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQ------KKI 1949
Cdd:TIGR00606 495 LTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnKKQ 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1950 VEETL----KQRKVVEEEIHILKLNFEKASSGKQELELelkklkgiaDETQKSKAKAEEEAEKFRklaleeekkrkeaea 2025
Cdd:TIGR00606 575 LEDWLhsksKEINQTRDRLAKLNKELASLEQNKNHINN---------ELESKEEQLSSYEDKLFD--------------- 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2026 kvkqiqaaeeeaARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSA----------AEQKAQNVLV 2095
Cdd:TIGR00606 631 ------------VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrvfqTEAELQEFIS 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2096 Q-QNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEkea 2174
Cdd:TIGR00606 699 DlQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG--- 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2175 srraeAEAAALKLKQEADSEMAKYKKLAEKTlkqkSSVEEELVKVKVQLDETDKQKSVLDV-ELKRLKQEVSDAIKQKAQ 2253
Cdd:TIGR00606 776 -----TIMPEEESAKVCLTDVTIMERFQMEL----KDVERKIAQQAAKLQGSDLDRTVQQVnQEKQEKQHELDTVVSKIE 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2254 VEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQR 2333
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2334 ELAEKMLEEKKQAIQEAAKLKAEAE--------------------KLQKQKDQAQVEAQklLEAKKEMQQRLDQETEGFQ 2393
Cdd:TIGR00606 927 ELISSKETSNKKAQDKVNDIKEKVKnihgymkdienkiqdgkddyLKQKETELNTVNAQ--LEECEKHQEKINEDMRLMR 1004
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 2394 KSLEAE-------------RKRQLEITAEAEKLK--------VKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEK 2450
Cdd:TIGR00606 1005 QDIDTQkiqerwlqdnltlRKRENELKEVEEELKqhlkemgqMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEK 1082
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1630-1795 |
3.76e-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: 50.00 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1630 EESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAE-EEANKKTAAQEEAEKQKEEAKR 1708
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADtSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1709 EAKKRAkaeEAALKQKEAAEMELGNQRKMAEETAKQKLaaeqelirlradfEHAEQQRTVLDDELQRLKNDVNSavkQKK 1788
Cdd:pfam05262 289 EIKKND---EEALKAKDHKAFDLKQESKASEKEAEDKE-------------LEAQKKREPVAEDLQKTKPQVEA---QPT 349
|
....*..
gi 1207141765 1789 ELEEELI 1795
Cdd:pfam05262 350 SLNEDAI 356
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1382-1590 |
4.00e-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: 49.38 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1382 RRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRE 1461
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1462 LQELKTLSEQ---EIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNtaetELLQLRAKAVDADKLRNAAQEEAEK 1538
Cdd:COG4942 110 LRALYRLGRQpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207141765 1539 LRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKF--KLQAEEAER 1590
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1157-1631 |
4.01e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1157 KVPVNEKEIEASQTQLQklrsEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGN--LRERWQAVFAQ 1234
Cdd:COG4717 65 KPELNLKELKELEEELK----EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1235 IELRQRELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKG 1314
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1315 YIDAIKDyELQLVTYKALVEPIASPLKKAKMESASDDIIqeyVTLRTRYSELMTLSSQYIKFIIetqrrlqdeekAAEKL 1394
Cdd:COG4717 221 ELEELEE-ELEQLENELEAAALEERLKEARLLLLIAAAL---LALLGLGGSLLSLILTIAGVLF-----------LVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1395 KEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIK 1474
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1475 AKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAE 1554
Cdd:COG4717 366 EELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE 445
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 1555 EELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQ-IQVVEEVAKKTAATQLESKQVALTARLEE 1631
Cdd:COG4717 446 EELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAaLKLALELLEEAREEYREERLPPVLERASE 523
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1472-1750 |
4.74e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1472 EIKAKSQQVEEALLSRTRIEEEIhiIRLQLETtmkqkntAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKR 1551
Cdd:PRK05035 437 EIRAIEQEKKKAEEAKARFEARQ--ARLEREK-------AAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1552 KAEEELKRKSEAEKDAakekkkaleDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQvalTARLEE 1631
Cdd:PRK05035 508 IKAGARPDNSAVIAAR---------EARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANA---EAEEEV 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1632 SLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELetwRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAK 1711
Cdd:PRK05035 576 DPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDP---KKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAI 652
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1207141765 1712 KRAKAEEAALKQKEAAEMELGNQRKMAEETA----KQKLAAEQ 1750
Cdd:PRK05035 653 ARAKARKAAQQQANAEPEEAEDPKKAAVAAAiaraKAKKAAQQ 695
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1764-2420 |
4.97e-05 |
|
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: 49.75 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1764 QQRTVLDDELQRLKndvnsavkqkkELEEElikVRKEMEILLQQKSKAEKETMSntekskqlLESEAAKMRELAEEATKL 1843
Cdd:pfam07111 63 QQAELISRQLQELR-----------RLEEE---VRLLRETSLQQKMRLEAQAME--------LDALAVAEKAGQAEAEGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1844 RSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEAtrlkteAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQ 1923
Cdd:pfam07111 121 RAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQA------HEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1924 HKQAIEEKIGQLKKSSDtELDRQKKIVEETlkqRKVVEE----EIHILKLNFEKassgKQELELELKKLKGIADETQKSK 1999
Cdd:pfam07111 195 AQKEAELLRKQLSKTQE-ELEAQVTLVESL---RKYVGEqvppEVHSQTWELER----QELLDTMQHLQEDRADLQATVE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2000 AKAEEEAEKFRKLALEEEKKRKEaeakVKQIQAAEEEAARQHKAA----QEEVGRLMKLAEEAKKQKEIAEKEAEKQVIL 2075
Cdd:pfam07111 267 LLQVRVQSLTHMLALQEEELTRK----IQPSDSLEPEFPKKCRSLlnrwREKVFALMVQLKAQDLEHRDSVKQLRGQVAE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2076 VQEAAqkcsAAEQKAQNVLVQQNKDSMAQdkLKEEFEKAKKLAQEAEKAKDNAEKEaallHKKAEEAERQKKAAEAEAAK 2155
Cdd:pfam07111 343 LQEQV----TSQSQEQAILQRALQDKAAE--VEVERMSAKGLQMELSRAQEARRRQ----QQQTASAEEQLKFVVNAMSS 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2156 QAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKykKLAEKTLKQKSSVEEELV-----KVKVQLDETDKQK 2230
Cdd:pfam07111 413 TQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMAR--KVALAQLRQESCPPPPPAppvdaDLSLELEQLREER 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2231 SVLDVELKR----LKQEVSDAIKQKAQVEDELSKVKIQMEdllklklkiekenQELMKKdkdntkkllEEEAENMKKLAE 2306
Cdd:pfam07111 491 NRLDAELQLsahlIQQEVGRAREQGEAERQQLSEVAQQLE-------------QELQRA---------QESLASVGQQLE 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2307 EAARLNIEA-QEAARLRQiaesDLAKQRELAEKMLEEKKQAIQeaAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRL 2385
Cdd:pfam07111 549 VARQGQQEStEEAASLRQ----ELTQQQEIYGQALQEKVAEVE--TRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRA 622
|
650 660 670
....*....|....*....|....*....|....*
gi 1207141765 2386 DQETEgfqKSLEAERKRQLEITAEAEKLKVKVTQL 2420
Cdd:pfam07111 623 TQEKE---RNQELRRLQDEARKEEGQRLARRVQEL 654
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2028-2436 |
5.13e-05 |
|
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: 49.37 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2028 KQIQAAEEEAARQHKAAQEEVgrlmKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAaeqKAQNVLVQQNKDSMAQDKl 2107
Cdd:pfam09731 89 VKIPRQSGVSSEVAEEEKEAT----KDAAEAKAQLPKSEQEKEKALEEVLKEAISKAE---SATAVAKEAKDDAIQAVK- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2108 keefEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAerqkkaaeaeaakqakaqedAEKLRKEAEKEASRRAEAEAAALKL 2187
Cdd:pfam09731 161 ----AHTDSLKEASDTAEISREKATDSALQKAEAL--------------------AEKLKEVINLAKQSEEEAAPPLLDA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2188 KQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVqLDETDKQksVLDVELKRLKQEVSDAIKQK-AQVEDELSKVkiqME 2266
Cdd:pfam09731 217 APETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKE-LVASERI--VFQQELVSIFPDIIPVLKEDnLLSNDDLNSL---IA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2267 DLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARlNIEAQEAARLRQIAESdlakqrelaekmLEEKKQA 2346
Cdd:pfam09731 291 HAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSA-RLEEVRAADEAQLRLE------------FEREREE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2347 IQEAAKLKAEAEklqkQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKS-LEAERKRQLEITAEAeKLKVK-VTQLSDAQ 2424
Cdd:pfam09731 358 IRESYEEKLRTE----LERQAEAHEEHLKDVLVEQEIELQREFLQDIKEkVEEERAGRLLKLNEL-LANLKgLEKATSSH 432
|
410
....*....|..
gi 1207141765 2425 SKAEEEAKKFKK 2436
Cdd:pfam09731 433 SEVEDENRKAQQ 444
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2321-2767 |
5.66e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.72 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2321 LRQIAES-DLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQK----------QKDQAQVEAQKLLEAKKEMQQRLDQET 2389
Cdd:pfam05483 50 LEQVANSgDCHYQEGLKDSDFENSEGLSRLYSKLYKEAEKIKKwkvsieaelkQKENKLQENRKIIEAQRKAIQELQFEN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2390 EGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQS 2469
Cdd:pfam05483 130 EKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2470 KQEadgLHKAIADLEKEKEKlkkeaadLQKQSKEMANVQQEQLQqekTILQQSffAEKETLLKKEKAIEEEKKKLEKQFE 2549
Cdd:pfam05483 210 RLE---MHFKLKEDHEKIQH-------LEEEYKKEINDKEKQVS---LLLIQI--TEKENKMKDLTFLLEESRDKANQLE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2550 DEVK-KAEALKAEQERQRKLMEEeRKKLQSAMDAAIKKQKEAEEEMN-----------GKQKEMQDLEKKRIEQEKLLAE 2617
Cdd:pfam05483 275 EKTKlQDENLKELIEKKDHLTKE-LEDIKMSLQRSMSTQKALEEDLQiatkticqlteEKEAQMEELNKAKAAHSFVVTE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2618 ENKN-------LREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMT-----MVETTKKVLNGSTEVDGVKKDvplaFDG 2685
Cdd:pfam05483 354 FEATtcsleelLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKnnkevELEELKKILAEDEKLLDEKKQ----FEK 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2686 IREKVPASRLHEIGVLSKKEYD------KLKKGKTTVQELSKNDKVKMCLKGKDCIGGVIVEPNQKMsiyQALKDKMITQ 2759
Cdd:pfam05483 430 IAEELKGKEQELIFLLQAREKEihdleiQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK---LLLENKELTQ 506
|
....*...
gi 1207141765 2760 STAIMLLE 2767
Cdd:pfam05483 507 EASDMTLE 514
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1405-1560 |
5.80e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1405 MQAELEKQKQLAETHAKaIAKAEQEANELK---TKMKDEVSKRQDVAVDSEKQKHNIQRELQELktlsEQEIKAKSQQVE 1481
Cdd:COG1579 2 MPEDLRALLDLQELDSE-LDRLEHRLKELPaelAELEDELAALEARLEAAKTELEDLEKEIKRL----ELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1482 --EALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKR 1559
Cdd:COG1579 77 kyEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
.
gi 1207141765 1560 K 1560
Cdd:COG1579 157 E 157
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
72-159 |
5.95e-05 |
|
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: 45.52 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 72 LYEDLRDGHNLISLLEVLSGETLPrerDVVRNSRLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLT 151
Cdd:cd21294 38 LFDECKDGLVLSKLINDSVPDTID---ERVLNKPPRKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLI 114
|
....*...
gi 1207141765 152 LGLIWTII 159
Cdd:cd21294 115 LGLIWQII 122
|
|
| F-BAR_PSTPIP |
cd07647 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ... |
2234-2468 |
6.50e-05 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153331 [Multi-domain] Cd Length: 239 Bit Score: 47.86 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2234 DVELKRLK------QEVSDAIKQKAQVEDELSKVKIQMEDLLKLklkiekenqelmkKDKDNTkklLEEEAENMKKLAEE 2307
Cdd:cd07647 8 DTLLQRLKegkkmcKELEDFLKQRAKAEEDYGKALLKLSKSAGP-------------GDEIGT---LKSSWDSLRKETEN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2308 AARLNIEaqeaarlrqiaesdLAKQ-RELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKdqaQVEAQKLLEAKKEMQQRLd 2386
Cdd:cd07647 72 VANAHIQ--------------LAQSlREEAEKLEEFREKQKEERKKTEDIMKRSQKNK---KELYKKTMKAKKSYEQKC- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2387 QETEGFQKSleAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEKLEVQR 2466
Cdd:cd07647 134 REKDKAEQA--YEKSSSGAQPKEAEKLKKKAAQCKTSAEEADSAYKSSIGCLEDAR---VEWESEHATACQVFQNMEEER 208
|
..
gi 1207141765 2467 LQ 2468
Cdd:cd07647 209 IK 210
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1644-1872 |
6.71e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1644 QEEAEHLKKQQAEADKAREQAEKELETWRQKANEalRLRLQAEEEANKKtaaqeeaekqkEEAKREAKKRAK-AEEAALK 1722
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLE--KERLAAQEQKKQA-----------EEAAKQAALKQKqAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1723 QKEAAemelgnqrkmaeetakqKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKndvnSAVKQKKELEEElikVRKEME 1802
Cdd:PRK09510 141 AAAAA-----------------KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKK----AAAEAKKKAEAE---AAAKAA 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1803 ILLQQKSKAEKETMSNTEkSKQLLESEAAKMRELAEEATKlrSVAEEAKKQRQIAEEEAARQRAEAEKIL 1872
Cdd:PRK09510 197 AEAKKKAEAEAKKKAAAE-AKKKAAAEAKAAAAKAAAEAK--AAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2286-2447 |
7.26e-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: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2286 DKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKmleekkqAIQEAAKLKAEAEKLQKQKD 2365
Cdd:pfam05262 179 DKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADK-------AQQKADFAQDNADKQRDEVR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2366 QAQVEAQKLLEAKKEMQQRLDQETEGFQKSlEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRL 2445
Cdd:pfam05262 252 QKQQEAKNLPKPADTSSPKEDKQVAENQKR-EIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKR 330
|
..
gi 1207141765 2446 QE 2447
Cdd:pfam05262 331 EP 332
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1709-1957 |
7.36e-05 |
|
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: 48.30 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1709 EAKKRAKAEEAALKQKEAAEMELGNQrkmAEETAKQKLAAEQELIRLRADFEHAEQQRTVlddELQRLKndvnsAVKQKK 1788
Cdd:TIGR02794 51 QANRIQQQKKPAAKKEQERQKKLEQQ---AEEAEKQRAAEQARQKELEQRAAAEKAAKQA---EQAAKQ-----AEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1789 ELEEELIKVRKEmeillqQKSKAEKEtmsntekSKQLLESEAAKMRElaEEATKlrSVAEEAKKQRQIAE---EEAARQR 1865
Cdd:TIGR02794 120 QAEEAKAKQAAE------AKAKAEAE-------AERKAKEEAAKQAE--EEAKA--KAAAEAKKKAEEAKkkaEAEAKAK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1866 AEAE-KILKEKLTAINEATRLKTEAEiALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQ-LKKSSDTEL 1943
Cdd:TIGR02794 183 AEAEaKAKAEEAKAKAEAAKAKAAAE-AAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGaRGAAAGSEV 261
|
250
....*....|....
gi 1207141765 1944 DRQKKIVEETLKQR 1957
Cdd:TIGR02794 262 DKYAAIIQQAIQQN 275
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2028-2166 |
7.98e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2028 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQkeiAEKEAEKQVilvQEAAQKCSAAEQKAQNVLVQQNKdSMAQDKL 2107
Cdd:PRK09510 129 LKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK---AAAEAKKKA---EAEAAKKAAAEAKKKAEAEAAAK-AAAEAKK 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141765 2108 KEEFEKAKKLAQEAEK-----AKDNAEKEAAllhKKAEEAERQKKAAEAEAAKQAKAQEDAEKL 2166
Cdd:PRK09510 202 KAEAEAKKKAAAEAKKkaaaeAKAAAAKAAA---EAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
37-158 |
8.10e-05 |
|
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: 45.34 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 37 RKDERDRVQKKTFTKWVNKHLVKhwkAEAQRHITDLYEDLRDGHNLISLLEVLSGETLpreRDVvrnSRLPREKGRMrfh 116
Cdd:cd21285 3 SWEAENGFDKQIYTDWANHYLAK---SGHKRLIKDLQQDVTDGVLLAEIIQVVANEKI---EDI---NGCPKNRSQM--- 70
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207141765 117 kLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTI 158
Cdd:cd21285 71 -IENIDACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1749-1909 |
8.35e-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: 47.23 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1749 EQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtMSNTEKSKQLles 1828
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRNNKEY--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1829 eAAKMRELaEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEatrLKTEAEIALKEKEAENDRLKRKAE 1908
Cdd:COG1579 92 -EALQKEI-ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAERE 166
|
.
gi 1207141765 1909 E 1909
Cdd:COG1579 167 E 167
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1624-2056 |
8.44e-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: 49.18 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1624 ALTARLE-----ESLKNEQVMVIQLQEEAEHLkkqqaeadkarEQAEKELETWRQKANEALRLRLQAEEEANKKtaaqee 1698
Cdd:COG3096 287 ALELRRElfgarRQLAEEQYRLVEMARELEEL-----------SARESDLEQDYQAASDHLNLVQTALRQQEKI------ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1699 aekqkeeakreAKKRAKAEEAALKQKEAAEM--ELGNQRKMAEEtakQKLAAEQELIRLR---ADFEHA--EQQRTVLD- 1770
Cdd:COG3096 350 -----------ERYQEDLEELTERLEEQEEVveEAAEQLAEAEA---RLEAAEEEVDSLKsqlADYQQAldVQQTRAIQy 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1771 -DELQRLKN----------DVNSAVKQKKELEEELIKVRKEMeILLQQKSKAEKETMSNTEKSKQLLESEAA-------- 1831
Cdd:COG3096 416 qQAVQALEKaralcglpdlTPENAEDYLAAFRAKEQQATEEV-LELEQKLSVADAARRQFEKAYELVCKIAGeversqaw 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1832 -KMRELAEEATKLRSVAEEAKK-QRQIAE-EEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAE 1908
Cdd:COG3096 495 qTARELLRRYRSQQALAQRLQQlRAQLAElEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1909 EEGYQRKVLEdqaaQHKQAIEEKIGQLKKS------SDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKqele 1982
Cdd:COG3096 575 EAVEQRSELR----QQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVER---- 646
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141765 1983 lelkklkgiaDETQkskakaeeeaekFRKLALeeekkrkeaeakvkqiqaaEEEAARQHKAAQEEVGRLMKLAE 2056
Cdd:COG3096 647 ----------DELA------------ARKQAL-------------------ESQIERLSQPGGAEDPRLLALAE 679
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1282-1940 |
8.60e-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: 48.86 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1282 KGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKAlvepiasplKKAKMESASDDIIQEYVTLRT 1361
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEK---------EKLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1362 RYSELMTLssqyikfiIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQlaethakAIAKAEQEANELK---TKMK 1438
Cdd:TIGR04523 202 LLSNLKKK--------IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT-------EISNTQTQLNQLKdeqNKIK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1439 DEVSKRQDVAVDSEKQKHNIQRELQELKTlseqEIKAKSQQVEEALLSRtrieeeihiIRLQLETTMKQKNTAETELLQl 1518
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKS----EISDLNNQKEQDWNKE---------LKSELKNQEKKLEEIQNQISQ- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1519 rakavdADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHL-KQAEL 1597
Cdd:TIGR04523 333 ------NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIqNQEKL 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1598 EKQRQIQVveevakKTAATQLESKQVALTARLEESLKNEQvMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANE 1677
Cdd:TIGR04523 407 NQQKDEQI------KKLQQEKELLEKEIERLKETIIKNNS-EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1678 ALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKrAKAEEAALKQKEaaemelgnqrkmaEETAKQKLAAEQELIRLRA 1757
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD-LTKKISSLKEKI-------------EKLESEKKEKESKISDLED 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1758 DFEHAEQQRTvlDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELA 1837
Cdd:TIGR04523 546 ELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1838 EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAE--IALKEKEAENDRLKRKAEEEGYQRK 1915
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDdiIELMKDWLKELSLHYKKYITRMIRI 703
|
650 660
....*....|....*....|....*
gi 1207141765 1916 VLEDQAAQHKQAIEEKIGQLKKSSD 1940
Cdd:TIGR04523 704 KDLPKLEEKYKEIEKELKKLDEFSK 728
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1410-1844 |
8.66e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.05 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1410 EKQKQLaethakaiakaeQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQelkTLSEQeIKAKSQQVEEAllsRTR 1489
Cdd:pfam10174 363 KKTKQL------------QDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE---NLQEQ-LRDKDKQLAGL---KER 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1490 IEEeihiirLQLETTmkqknTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAK 1569
Cdd:pfam10174 424 VKS------LQTDSS-----NTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELT 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1570 EKKKALEDL-EKFKLQAEEA---ERHLKQAELEkqrqIQVVEEVAKKTAATQLESKQVALTARLEESLKNE-QVMVIQLQ 1644
Cdd:pfam10174 493 EKESSLIDLkEHASSLASSGlkkDSKLKSLEIA----VEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRiRLLEQEVA 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1645 EEAEHLKKQQAEADK---AREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQeeaekqkeeakreakkraKAEEAAL 1721
Cdd:pfam10174 569 RYKEESGKAQAEVERllgILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANI------------------KHGQQEM 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1722 KQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLradfehaEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM 1801
Cdd:pfam10174 631 KKKGAQLLEEARRREDNLADNSQQLQLEELMGAL-------EKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQL 703
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1207141765 1802 EILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLR 1844
Cdd:pfam10174 704 EEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALK 746
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2330-2597 |
9.94e-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: 48.22 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2330 AKQRELAEKMLEEKKQAIQEaakLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLdQETEGFQKSLEAErkrqleitae 2409
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAE---LEKELAALKKEEKALLKQLAALERRIAALARRI-RALEQELAALEAE---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2410 aeklkvkvtqLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVeklevqrLQSKQEADGLHKAIADLEKEKEK 2489
Cdd:COG4942 85 ----------LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL-------LLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2490 LKKEAADLQKQSKEMANVQQEQLQQEKtilqqsffaEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLM 2569
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERA---------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
250 260
....*....|....*....|....*...
gi 1207141765 2570 EEERKKLQSAMDAAIKKQKEAEEEMNGK 2597
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2521-2643 |
1.04e-04 |
|
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: 47.67 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2521 QSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRklmeEERKKLQSAMDAAIKKQKEAEEEMngKQKE 2600
Cdd:pfam02841 179 QEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLR----EKQKEEEQMMEAQERSYQEHVKQL--IEKM 252
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207141765 2601 MQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEI 2643
Cdd:pfam02841 253 EAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQD 295
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1360-1776 |
1.12e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 48.36 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1360 RTRYSELMTLSSQYIKF---IIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTK 1436
Cdd:COG5278 106 QARLDELEALIDQWLAEleqVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1437 MKDEVSKRQDVAVDSEKQKHNIQRELQELkTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELL 1516
Cdd:COG5278 186 LALAELLLLALARALAALLLLLLLEAELA-AAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1517 QLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAE 1596
Cdd:COG5278 265 AALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1597 LEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKAN 1676
Cdd:COG5278 345 ALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1677 EALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLR 1756
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
410 420
....*....|....*....|
gi 1207141765 1757 ADFEHAEQQRTVLDDELQRL 1776
Cdd:COG5278 505 LAALLLAAAEAALAAALAAA 524
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1457-1796 |
1.18e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1457 NIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEA 1536
Cdd:COG4372 32 QLRKALFELDKL-QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1537 EKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAT 1616
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1617 QLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQ 1696
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1697 EEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRL 1776
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
330 340
....*....|....*....|
gi 1207141765 1777 KNDVNSAVKQKKELEEELIK 1796
Cdd:COG4372 351 LDNDVLELLSKGAEAGVADG 370
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3750-3786 |
1.20e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.20e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1207141765 3750 IDLLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPEF 3786
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2299-2520 |
1.24e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.51 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2299 ENMKKLAEE-AARLNIEAQEAARLRQIAESDLAKQREL--AEKMLEEKKQAIQEAAKLKAEAEKLQkQKDQAQVEAQKLL 2375
Cdd:PRK10929 75 DNFPKLSAElRQQLNNERDEPRSVPPNMSTDALEQEILqvSSQLLEKSRQAQQEQDRAREISDSLS-QLPQQQTEARRQL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2376 eakKEMQQRLdqETEGFQKSLEAERKRQLeITAEAEKLKVKVTQLSDAQSKAEE-------EAKKFKKQADEIKIRLQET 2448
Cdd:PRK10929 154 ---NEIERRL--QTLGTPNTPLAQAQLTA-LQAESAALKALVDELELAQLSANNrqelarlRSELAKKRSQQLDAYLQAL 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141765 2449 EKH-TSEKHTVVEK-LEVQRLQSKQEADgLHKAIADLEKEKEKLkkeAADLQKQSKEMANVQQEQLQQEKTILQ 2520
Cdd:PRK10929 228 RNQlNSQRQREAERaLESTELLAEQSGD-LPKSIVAQFKINREL---SQALNQQAQRMDLIASQQRQAASQTLQ 297
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2549-2641 |
1.25e-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: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2549 EDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQ 2628
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90
....*....|...
gi 1207141765 2629 LQSSQKASYTKEI 2641
Cdd:COG4942 113 LYRLGRQPPLALL 125
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2043-2256 |
1.26e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2043 AAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVilvQEAAQKCSAAEQKAQnvlvQQNKDSMAQDKLKEEFEKAKKLAQEAE 2122
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQA---EELQQKQAAEQERLK----QLEKERLAAQEQKKQAEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2123 KAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAAlKLKQEADSEM-AKYKKL 2201
Cdd:PRK09510 132 KQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAA-KAAAEAKKKAeAEAKKK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141765 2202 AEKTLKQKSSVEEELVKVKvqldETDKQKSVLDVELKRLKQEVSDAIKQKAQVED 2256
Cdd:PRK09510 211 AAAEAKKKAAAEAKAAAAK----AAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
45-169 |
1.28e-04 |
|
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: 45.03 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 45 QKKTFTKWVNKHLVKHWKAeaqRHIT-------DLYEDLRDGHNLISLLEVLSGETLPrERDVVRNSRLPrekgrmrFHK 117
Cdd:cd21323 25 EKVAFVNWINKALEGDPDC---KHVVpmnptdeSLFKSLADGILLCKMINLSQPDTID-ERAINKKKLTP-------FTI 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 118 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 169
Cdd:cd21323 94 SENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2294-2505 |
1.34e-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: 48.02 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2294 LEEEAENMKKLAEEAARLNIEAQEAARLRQIAESdlAKQRELAekmLEEKKQAIQEAAKLKAEA-EKLQKQKDQAQVEAQ 2372
Cdd:pfam15709 309 MESEEERSEEDPSKALLEKREQEKASRDRLRAER--AEMRRLE---VERKRREQEEQRRLQQEQlERAEKMREELELEQQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2373 KLLEAKKEMQQRLDQETegfQKSLEAERKRQLEITAEAEK-------LKVKVTQLS-DAQSKAEEEAKKFKKQADEIKIR 2444
Cdd:pfam15709 384 RRFEEIRLRKQRLEEER---QRQEEEERKQRLQLQAAQERarqqqeeFRRKLQELQrKKQQEEAERAEAEKQRQKELEMQ 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141765 2445 LQETEKHTSEKhTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMA 2505
Cdd:pfam15709 461 LAEEQKRLMEM-AEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQA 520
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1757-2130 |
1.39e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1757 ADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKetmsntekskqllESEAAKMR-E 1835
Cdd:PRK04863 272 ADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQ-------------DYQAASDHlN 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1836 LAEEAtklrsVAEEAKKQRQIAEEEAARQRAEAEKILKEkltainEATRLKTEAEIALKEKEAENDRLkrKAEEEGYQRK 1915
Cdd:PRK04863 339 LVQTA-----LRQQEKIERYQADLEELEERLEEQNEVVE------EADEQQEENEARAEAAEEEVDEL--KSQLADYQQA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1916 --VLEDQAAQHKQAIE--EKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGI 1991
Cdd:PRK04863 406 ldVQQTRAIQYQQAVQalERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1992 ADETQKSkakaeEEAEKFRKLaLEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQeevgRLMKLAEEAKKQKEIAEKEAEK 2071
Cdd:PRK04863 486 AGEVSRS-----EAWDVAREL-LRRLREQRHLAEQLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDE 555
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141765 2072 QVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEK 2130
Cdd:PRK04863 556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALAR 614
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1500-1923 |
1.41e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.98 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1500 QLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLE 1579
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1580 KFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADK 1659
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1660 AREQAEKELETWRQKANEALRLRLQAEEEAnkktaAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAE 1739
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALA-----ELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1740 ETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNT 1819
Cdd:COG5278 346 LLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELA 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1820 EKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE 1899
Cdd:COG5278 426 EALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALAL 505
|
410 420
....*....|....*....|....
gi 1207141765 1900 NDRLKRKAEEEGYQRKVLEDQAAQ 1923
Cdd:COG5278 506 AALLLAAAEAALAAALAAALASAE 529
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
40-165 |
1.50e-04 |
|
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: 44.60 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 40 ERDRVQKKTFTKWVNKHLVkhwkaeaQRHITDLYEDLRDGHNLISLLEVLSgetLPRERDVVRNSRLPREKGRMRfhKLQ 119
Cdd:cd21330 9 EGETREERTFRNWMNSLGV-------NPRVNHLYSDLSDALVIFQLYEKIK---VPVDWNRVNKPPYPKLGENMK--KLE 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207141765 120 NVQIALDFLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 165
Cdd:cd21330 77 NCNYAVELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1577-1877 |
1.53e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1577 DLEKFKLQAEEAERHLKQAELEKQRQIQvveevakktAATQLEsKQVALTARLEEslkneQVMVIQ---LQEEAEHLKKQ 1653
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQEQQQRS---------QLEQAK-EGLSALNRLLP-----RLNLLAdetLADRVEEIREQ 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1654 QAEADKAR----------EQAEKELETWRQKANEALRLRLQAEEeankktaaqeeaekqkeeakreakkrAKAEEAALKQ 1723
Cdd:PRK04863 903 LDEAEEAKrfvqqhgnalAQLEPIVSVLQSDPEQFEQLKQDYQQ--------------------------AQQTQRDAKQ 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1724 KEAAEMELgNQRK--MAEETAKQKLAAEQEL-IRLRADFEHAEQQRTVLDDEL--------------QRLKNDVNSAVKQ 1786
Cdd:PRK04863 957 QAFALTEV-VQRRahFSYEDAAEMLAKNSDLnEKLRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQM 1035
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1787 KKELEEEL--IKVR--KEMEILLQQKSKAEKETMSNT-------EKSKQLLESE----AAKMRELAEEATKLRSVAEEAK 1851
Cdd:PRK04863 1036 LQELKQELqdLGVPadSGAEERARARRDELHARLSANrsrrnqlEKQLTFCEAEmdnlTKKLRKLERDYHEMREQVVNAK 1115
|
330 340
....*....|....*....|....*.
gi 1207141765 1852 KqRQIAEEEAARQRAEAEKILKEKLT 1877
Cdd:PRK04863 1116 A-GWCAVLRLVKDNGVERRLHRRELA 1140
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1631-1915 |
1.56e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1631 ESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEaLRLRLQAEEEANKKTAAQEEAEKQKEEAKREA 1710
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDE-LNAQVKELREEAQELREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1711 KKRAKAEEAALKQKEAaemELGNQRKMAEETAKQKLAAEQELIRLRAdfehaEQQRTVLD--------DELQRLKNDVNs 1782
Cdd:COG1340 80 RDELNEKLNELREELD---ELRKELAELNKAGGSIDKLRKEIERLEW-----RQQTEVLSpeeekelvEKIKELEKELE- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1783 AVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEEAKKQRQIAEEEAA 1862
Cdd:COG1340 151 KAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHE----EMIELYKEADELRKEADELHKEIVEAQEKAD 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1207141765 1863 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRK 1915
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKG 279
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4415-4452 |
1.60e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.60e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1207141765 4415 QRFLEVQYLTGGLIEPDVTGRVSLDEAVRKGSLDARTA 4452
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1598-1915 |
1.75e-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: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1598 EKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKK------QQAEADKAREQAEKELETW 1671
Cdd:pfam15558 4 ERDRKIAALMLARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQsqeqwqAEKEQRKARLGREERRRAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1672 RQKANEAL---RLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALkQKEAAEMELGNQRKMAE--------- 1739
Cdd:pfam15558 84 RREKQVIEkesRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL-QALREQNSLQLQERLEEachkrqlke 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1740 --------ETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKA 1811
Cdd:pfam15558 163 reeqkkvqENNLSELLNHQARKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1812 EKETMSNTEKSKQLLESEAAKMRelaeeatKLRSVAEEAKKQR--QIAEEEAARQRaeAEKILKEKLTAINEATRLKTEA 1889
Cdd:pfam15558 243 EEKEEERQEHKEALAELADRKIQ-------QARQVAHKTVQDKaqRARELNLEREK--NHHILKLKVEKEEKCHREGIKE 313
|
330 340
....*....|....*....|....*.
gi 1207141765 1890 EIALKEKEAENDRLKRKAEEEGYQRK 1915
Cdd:pfam15558 314 AIKKKEQRSEQISREKEATLEEARKT 339
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2232-2602 |
1.78e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2232 VLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARL 2311
Cdd:pfam07888 31 LLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2312 NIEAQEAARLRQIAESDLAKQRELAE--KMLEEKKQAIQ-EAAKLKAEAEKLQKQKDQAQVEaQKLLEAKKEMQQrldQE 2388
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEdiKTLTQRVLEREtELERMKERAKKAGAQRKEEEAE-RKQLQAKLQQTE---EE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2389 TEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKA---EEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQ 2465
Cdd:pfam07888 187 LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAhrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2466 RLQSKQEadgLHKAiadlekekeklKKEAADLQKQSKEMANVQQE---QLQQEKTILQQSFFAEKETLLKKEKAIEEEKK 2542
Cdd:pfam07888 267 RDRTQAE---LHQA-----------RLQAAQLTLQLADASLALREgraRWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2543 KLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQ 2602
Cdd:pfam07888 333 RLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1722-1927 |
1.85e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1722 KQKEAAEMElgNQRKMAEETAKQKLAAEQElirlradfehAEQQRtVLDDELQRLKndvnsAVKQKKELEEElikvrkEM 1801
Cdd:PRK09510 70 QQKSAKRAE--EQRKKKEQQQAEELQQKQA----------AEQER-LKQLEKERLA-----AQEQKKQAEEA------AK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1802 EILLQQKsKAEKETMSNTEKSKqlLESEAAKMReLAEEATKlrsvAEEAKKQRQIAE-----EEAARQRAEAEKILKEKL 1876
Cdd:PRK09510 126 QAALKQK-QAEEAAAKAAAAAK--AKAEAEAKR-AAAAAKK----AAAEAKKKAEAEaakkaAAEAKKKAEAEAAAKAAA 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207141765 1877 TAINEATRLKTEAEIALKEKEAENDRlKRKAEEEGYQRKVLEDQAAQHKQA 1927
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKKKAAAEA-KAAAAKAAAEAKAAAEKAAAAKAA 247
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2307-2443 |
1.90e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2307 EAARLNIeAQEAARLRQIAESDLAKQRELAEKmLEEKKQAIQEAAKLKaeaEKLQKQKDQAQ-VEAQKLLEAKKEMQQRL 2385
Cdd:PRK00409 505 EEAKKLI-GEDKEKLNELIASLEELERELEQK-AEEAEALLKEAEKLK---EELEEKKEKLQeEEDKLLEEAEKEAQQAI 579
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141765 2386 DQETEgfqkslEAERK-RQLEITAEAEKLKVKVTQLSDAQS-------KAEEEAKKFKKQADEIKI 2443
Cdd:PRK00409 580 KEAKK------EADEIiKELRQLQKGGYASVKAHELIEARKrlnkaneKKEKKKKKQKEKQEELKV 639
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2554-2655 |
1.99e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2554 KAEALKAEQERQRKLMEEER-------KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKL 2626
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKeaeaikkEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100
....*....|....*....|....*....
gi 1207141765 2627 QQLQSSQKASYTKEIEIQTDKVPEEELVQ 2655
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIE 138
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1801-2258 |
2.01e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1801 MEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEE-AKKQRQIAEEEAARQRAEAEKILKEKLTAI 1879
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1880 NEATRLKTEAEIALKEKEAENDRLKRKAEE-EGYQRKV--LEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQ 1956
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEElRELEEELeeLEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1957 RKVVEEEIHILKlnfEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAeee 2036
Cdd:COG4717 208 LAELEEELEEAQ---EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL--- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2037 aarqhkaaqeEVGRLMKLAEEAKKQKEIAEKEAEKqvilVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKK 2116
Cdd:COG4717 282 ----------VLGLLALLFLLLAREKASLGKEAEE----LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2117 LAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEaeaaalkLKQEADSEMA 2196
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQ-------LEELLGELEE 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141765 2197 KYKKLAEKTLKQK-SSVEEELVKVKVQLDETDKQKSVLDVELKRLK--QEVSDAIKQKAQVEDEL 2258
Cdd:COG4717 421 LLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAEL 485
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2306-2599 |
2.08e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.55 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2306 EEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRL 2385
Cdd:pfam02029 60 EEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2386 DQETEGFQKSLEAERKrqleitAEAEKLKVKVTQLSDAQSKAEEE-----AKKFKKQADEIKIRLQETEKHTSEKHTVVE 2460
Cdd:pfam02029 140 YQENKWSTEVRQAEEE------GEEEEDKSEEAEEVPTENFAKEEvkdekIKKEKKVKYESKVFLDQKRGHPEVKSQNGE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2461 KlEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAA----DLQKQSKEMANVQQEQLQQEktilQQSFFAEKETLLKKEKA 2536
Cdd:pfam02029 214 E-EVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEqkleELRRRRQEKESEEFEKLRQK----QQEAELELEELKKKREE 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141765 2537 IEEEKKKLEKQFEDEvkKAEALKAEQERQRKLMEE-ERKKlqsaMDAAIKKQKEAEEEMNGKQK 2599
Cdd:pfam02029 289 RRKLLEEEEQRRKQE--EAERKLREEEEKRRMKEEiERRR----AEAAEKRQKLPEDSSSEGKK 346
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1773-1942 |
2.14e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1773 LQRLKNDVNSAVKQKKELEEElikvrKEMEilLQQKSKAEKETMSNTEKSKQllesEAAKMRELAEEATKLRSVAEEAKK 1852
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ-----QAEE--LQQKQAAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1853 QRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENdrlKRKAEEEGYQRKVLEDQAAQHKQAIEEKI 1932
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEA---KKKAEAEAAAKAAAEAKKKAEAEAKKKAA 212
|
170
....*....|
gi 1207141765 1933 GQLKKSSDTE 1942
Cdd:PRK09510 213 AEAKKKAAAE 222
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2039-2628 |
2.28e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.53 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2039 RQHKAA-QEEVGRLMKLAEEAKkQKEIAE------KEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ--DKLKE 2109
Cdd:pfam12128 230 IQAIAGiMKIRPEFTKLQQEFN-TLESAElrlshlHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEkrDELNG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2110 EfekakKLAQEAEKAKDNAEKEAALLHKKAEEAErqkkaaeaeaakqakaqeDAEKLRKEAEKEASRRAEAEAaalkLKQ 2189
Cdd:pfam12128 309 E-----LSAADAAVAKDRSELEALEDQHGAFLDA------------------DIETAAADQEQLPSWQSELEN----LEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2190 EADSEMAKYKKLAEKTLKQKSSVEEELV-KVKVQLDETDKQKSVLDvelkrlkqevsdaiKQKAQVEDELSKVKIQMEDL 2268
Cdd:pfam12128 362 RLKALTGKHQDVTAKYNRRRSKIKEQNNrDIAGIKDKLAKIREARD--------------RQLAVAEDDLQALESELREQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2269 LklklkiekenqELMKKDKDNTKKLLEEEAENMKklaeeaARLNIEAQEAARLRQIAESDlakqrELAEKMLEEKKQAIQ 2348
Cdd:pfam12128 428 L-----------EAGKLEFNEEEYRLKSRLGELK------LRLNQATATPELLLQLENFD-----ERIERAREEQEAANA 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2349 EAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ-ETEGFQKS------LEAE----RKRQLEITAEAEKLKVKV 2417
Cdd:pfam12128 486 EVERLQSELRQARKRRDQASEALRQASRRLEERQSALDElELQLFPQAgtllhfLRKEapdwEQSIGKVISPELLHRTDL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2418 TQLSDAQSKAEE-------------EAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLE 2484
Cdd:pfam12128 566 DPEVWDGSVGGElnlygvkldlkriDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFAR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2485 KEKEKLKKeaaDLQKQSKEManvQQEQLQQEKTILQQSFFAEKEtlLKKEKAIEEEKKKLEKQFEDEVKKaEALKAEQER 2564
Cdd:pfam12128 646 TALKNARL---DLRRLFDEK---QSEKDKKNKALAERKDSANER--LNSLEAQLKQLDKKHQAWLEEQKE-QKREARTEK 716
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2565 Q--RKLMEEERKKLQSAMDAAI-KKQKEAEEEMNGKQKEM-QDLEKKRIEQEKL--LAEENKNLREKLQQ 2628
Cdd:pfam12128 717 QayWQVVEGALDAQLALLKAAIaARRSGAKAELKALETWYkRDLASLGVDPDVIakLKREIRTLERKIER 786
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1586-1962 |
2.83e-04 |
|
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: 47.06 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1586 EEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESlkneqvmviqlqeeaEHLKKQQAEADKAREQAE 1665
Cdd:pfam09731 52 GEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVS---------------SEVAEEEKEATKDAAEAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1666 KELETWRQKANEALRLRLQ-AEEEANKKTAAQEEAekqkeeakrEAKKRAKAEEAALKQKEAAEMELGNQRKMaEETAKQ 1744
Cdd:pfam09731 117 AQLPKSEQEKEKALEEVLKeAISKAESATAVAKEA---------KDDAIQAVKAHTDSLKEASDTAEISREKA-TDSALQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1745 KLAAEQELIRLRADFEHAEQQrTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQ 1824
Cdd:pfam09731 187 KAEALAEKLKEVINLAKQSEE-EAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1825 LLESEAAKMREL-AEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRL 1903
Cdd:pfam09731 266 IFPDIIPVLKEDnLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEA 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141765 1904 KRKAEeegYQRKVLEDQaaqhkQAIEEKIgqlkkssDTELDRQKKIVEETLKQRKVVEE 1962
Cdd:pfam09731 346 QLRLE---FEREREEIR-----ESYEEKL-------RTELERQAEAHEEHLKDVLVEQE 389
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2801-2838 |
2.89e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.89e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1207141765 2801 TKLLSAERAVTGFKDPFTGDTISVFEAMKKGLITEDQA 2838
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2321-2480 |
2.99e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2321 LRQIAESDLAKQRELAEKMLEE--------KKQAIQEA----AKLKAEAEKLQKQKDQaqvEAQKLLEAKKEMQQRLDQE 2388
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEakkeaeaiKKEALLEAkeeiHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2389 TEGFQK---SLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFkkQADEIK-IRLQETEKHTSEK--HTVVEKL 2462
Cdd:PRK12704 102 LELLEKreeELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL--TAEEAKeILLEKVEEEARHEaaVLIKEIE 179
|
170
....*....|....*...
gi 1207141765 2463 EvqrlQSKQEADGLHKAI 2480
Cdd:PRK12704 180 E----EAKEEADKKAKEI 193
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
995-1360 |
3.29e-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: 47.37 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 995 DNLLRSVEQEPALIQKDSTSGEQDESVCKSYITQIKDLRLRLEGCESRTVNRLRQMVDKepLKACTQRATEQKKVQTELE 1074
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED--LSSLEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1075 GIKKDLDKVVEKSEAVLATSQQSSSapvlRSEIDITQKKMEHVYglssvylDKLKTIDLVIRSTQG-----------AED 1143
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLS----HSRIPEIQAELSKLE-------EEVSRIEARLREIEQklnrltlekeyLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1144 ILNKYENQLREV-NKVPVNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELqratevnkrmSQLHSERDVELEHYRQlvg 1222
Cdd:TIGR02169 834 EIQELQEQRIDLkEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----------GDLKKERDELEAQLRE--- 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1223 nLRERWQAVFAQIELRQRELDLLNRQMQAyresydwlirwiadAKQRQDKlhavpIGGSKGLQEQLTQEKKLLEEIEKNK 1302
Cdd:TIGR02169 901 -LERKIEELEAQIEKKRKRLSELKAKLEA--------------LEEELSE-----IEDPKGEDEEIPEEELSLEDVQAEL 960
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 1303 DKVE-DCQKFAKGYIDAIKDYELQLVTYKALVEpiasplKKAKMESASDDI---IQEYVTLR 1360
Cdd:TIGR02169 961 QRVEeEIRALEPVNMLAIQEYEEVLKRLDELKE------KRAKLEEERKAIlerIEEYEKKK 1016
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3167-3202 |
3.45e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.45e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1207141765 3167 RLLEAQLATGGIIDPEKSYRITPDIAYKRGHLNEEM 3202
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2318-2522 |
3.51e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2318 AARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLE 2397
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2398 AERKRQ-----LEITAEAEKLK------VKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKL--EV 2464
Cdd:COG3883 94 ALYRSGgsvsyLDVLLGSESFSdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAkaEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 2465 QRLQSKQEADgLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQS 2522
Cdd:COG3883 174 EAQQAEQEAL-LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2189-2422 |
3.52e-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: 46.94 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2189 QEADSEMAKYKKLAEKTLKQKSsvEEELVKVKVQLDETDKQKSVLDVELKRLKQEVsdaikqkAQVEDELSKVKIQMEdl 2268
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQR--EEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNE-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2269 lklklkIEKENQELMKKdkdnTKKLLEEEAENMKKL----AEEAARL-NIEAQ-EAARlrqiaESDLAKQRELAEKMLEE 2342
Cdd:pfam05667 381 ------ELEKQYKVKKK----TLDLLPDAEENIAKLqalvDASAQRLvELAGQwEKHR-----VPLIEEYRALKEAKSNK 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2343 KKqaiqEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSleAERKRQLEITAEAEKLKVKVTQ-LS 2421
Cdd:pfam05667 446 ED----ESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRS--AYTRRILEIVKNIKKQKEEITKiLS 519
|
.
gi 1207141765 2422 D 2422
Cdd:pfam05667 520 D 520
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1006-1979 |
3.60e-04 |
|
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: 47.35 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1006 ALIQKDSTSGEQDESVCKSYITQIKDLRLRLEGCESRTVNRLRQMVDKEPLKACTQRATEQKKVQTElegIKKDLDKVVE 1085
Cdd:TIGR01612 682 SIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGE---INKDLNKILE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1086 KSEAvlATSQQSSSAPVLRSEIDITQKKMEHVYGLSSVYLDKLkTIDlvirsTQGAEDILNKYENQLREVNKVPVNEKEI 1165
Cdd:TIGR01612 759 DFKN--KEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQI-NID-----NIKDEDAKQNYDKSKEYIKTISIKEDEI 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1166 EASQTQLQKLRSEAEGKQATFDRLE---------EELQRATEVNKRMSQLHSERdveLEHYRQLVGNLRERWQAVFAQIE 1236
Cdd:TIGR01612 831 FKIINEMKFMKDDFLNKVDKFINFEnnckekidsEHEQFAELTNKIKAEISDDK---LNDYEKKFNDSKSLINEINKSIE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1237 LRQRELDLLNRqmqayresYDWLIRWIADAKQRQDKLHavpiggskglqeqlTQEKKLLEEIEKNKDKVEDCQKFAKGYI 1316
Cdd:TIGR01612 908 EEYQNINTLKK--------VDEYIKICENTKESIEKFH--------------NKQNILKEILNKNIDTIKESNLIEKSYK 965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1317 DaikDYELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRY--SELMTLSSQYI---KFIIETQRRLQDEEKAA 1391
Cdd:TIGR01612 966 D---KFDNTLIDKINELDKAFKDASLNDYEAKNNELIKYFNDLKANLgkNKENMLYHQFDekeKATNDIEQKIEDANKNI 1042
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1392 EKLKEEERKKMAEMQAELEKQ--KQLAETHAKAIAKAEQEA---NELKTKMK----------------DEVSK-RQDVAV 1449
Cdd:TIGR01612 1043 PNIEIAIHTSIYNIIDEIEKEigKNIELLNKEILEEAEINItnfNEIKEKLKhynfddfgkeenikyaDEINKiKDDIKN 1122
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1450 DSEKQKHNIqRELQELKTLSEQ---EIKAKSQQVEEaLLSRTRIEEEIHIIRLQLETTM----KQKNTAE------TELL 1516
Cdd:TIGR01612 1123 LDQKIDHHI-KALEEIKKKSENyidEIKAQINDLED-VADKAISNDDPEEIEKKIENIVtkidKKKNIYDeikkllNEIA 1200
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1517 QLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEE--------------ELKRKSEAEKDAAKEKKKALEDLEKFK 1582
Cdd:TIGR01612 1201 EIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEhmikameayiedldEIKEKSPEIENEMGIEMDIKAEMETFN 1280
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1583 LQAEE-------AERHLKQAELEKQRQIQVVEEVAKKTAATQLESKqvaLTARLEESLKNEQVMVIQLQEEAE-----HL 1650
Cdd:TIGR01612 1281 ISHDDdkdhhiiSKKHDENISDIREKSLKIIEDFSEESDINDIKKE---LQKNLLDAQKHNSDINLYLNEIANiynilKL 1357
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1651 KKQQAEADKAREQAeKELETWRQKANEAL----RLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAK-------AEEA 1719
Cdd:TIGR01612 1358 NKIKKIIDEVKEYT-KEIEENNKNIKDELdkseKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKelknhilSEES 1436
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1720 ALKQ--KEAAEME-----LGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVldDELQRLKNDVNSAVKQKKELEE 1792
Cdd:TIGR01612 1437 NIDTyfKNADENNenvllLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHI--DKSKGCKDEADKNAKAIEKNKE 1514
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1793 ELIKVRKEMEILLQQKSKAE-KETMSNTEK-SKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEK 1870
Cdd:TIGR01612 1515 LFEQYKKDVTELLNKYSALAiKNKFAKTKKdSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKA 1594
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1871 ILKEKLTAINEATRL------KTEAEIALKEKEA------------ENDRLKRKAEEEGYQRKVLEDQAAQhKQAIEEKi 1932
Cdd:TIGR01612 1595 AIDIQLSLENFENKFlkisdiKKKINDCLKETESiekkissfsidsQDTELKENGDNLNSLQEFLESLKDQ-KKNIEDK- 1672
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|...
gi 1207141765 1933 gqlKKSSDtELDRQKKIVEETLKQRK------VVEEEIHILKLNFEKASSGKQ 1979
Cdd:TIGR01612 1673 ---KKELD-ELDSEIEKIEIDVDQHKknyeigIIEKIKEIAIANKEEIESIKE 1721
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1461-1794 |
3.65e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1461 ELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKavdadklRNAAQEEAEKLR 1540
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE-------LEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1541 KQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLES 1620
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1621 KQVALTARLEESLKNEQVmVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAE 1700
Cdd:COG4372 167 AALEQELQALSEAEAEQA-LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1701 KQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDV 1780
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330
....*....|....
gi 1207141765 1781 NSAVKQKKELEEEL 1794
Cdd:COG4372 326 KKLELALAILLAEL 339
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2331-2644 |
3.65e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2331 KQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL---LEAKKEMQQRLDQETEGFQKSLEAERKRQLEIT 2407
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLeeeLEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2408 AEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIAdlEKEK 2487
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2488 EKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRK 2567
Cdd:COG4372 179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141765 2568 LMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQ 2644
Cdd:COG4372 259 EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1517-1678 |
3.79e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1517 QLRAKAVDADKLRN--AAQEEAEKLRKQVAE-----ETQKKRKAEEELKRKSEAEKDAAKEKKKALED-----LEKFKLQ 1584
Cdd:PRK09510 69 QQQKSAKRAEEQRKkkEQQQAEELQQKQAAEqerlkQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEaaakaAAAAKAK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1585 AEEAERHL----KQAELEKQRQIQvvEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKA 1660
Cdd:PRK09510 149 AEAEAKRAaaaaKKAAAEAKKKAE--AEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
170
....*....|....*...
gi 1207141765 1661 REQAEKELETWRQKANEA 1678
Cdd:PRK09510 227 AAKAAAEAKAAAEKAAAA 244
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4305-4338 |
3.81e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 3.81e-04
10 20 30
....*....|....*....|....*....|....
gi 1207141765 4305 EETGPVAGILDTDTLEKVSVTEAMHRNLVDNITG 4338
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2039-2363 |
4.37e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2039 RQHKAAQEEVGRLMKLAEEAK-----KQ----KEIAEKEAEKqvilvQEAAQKCSAAEQKAqnvlVQQNKDSMAQDKLKE 2109
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKarfeaRQarleREKAAREARH-----KKAAEARAAKDKDA----VAAALARVKAKKAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2110 EFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAErqkkaaeaeaakqaKAQEDAEKLRKEAekeasrraeaeaaalklkQ 2189
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQARARQAE--------------KQAAAAADPKKAA------------------V 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2190 EADSEMAKYKKLAEKTLKQKSSVEEELVKVKVqldetdkQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLL 2269
Cdd:PRK05035 551 AAAIARAKAKKAAQQAANAEAEEEVDPKKAAV-------AAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIAR 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2270 KLKLKIEKENQElmkkdkdntkklLEEEAENMKKLAEEAARlnieAQEAARLRQIAESDLAKQRElaekmLEEKKQAIqE 2349
Cdd:PRK05035 624 AKAKKAEQQANA------------EPEEPVDPRKAAVAAAI----ARAKARKAAQQQANAEPEEA-----EDPKKAAV-A 681
|
330
....*....|....
gi 1207141765 2350 AAKLKAEAEKLQKQ 2363
Cdd:PRK05035 682 AAIARAKAKKAAQQ 695
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1663-1975 |
4.42e-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: 46.44 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1663 QAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQ--RKMAEE 1740
Cdd:pfam15964 321 SSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKemKKEREE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1741 TAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQrlkndvnSAVKQKKELEEELIKVRKEMEILLQQkSKAEKEtmsntE 1820
Cdd:pfam15964 401 LGATMLALSQNVAQLEAQVEKVTREKNSLVSQLE-------EAQKQLASQEMDVTKVCGEMRYQLNQ-TKMKKD-----E 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1821 KSKQLLESEAAKMRELA---EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKIlkekltaineaTRLKTEAEIALKEKE 1897
Cdd:pfam15964 468 AEKEHREYRTKTGRQLEikdQEIEKLGLELSESKQRLEQAQQDAARAREECLKL-----------TELLGESEHQLHLTR 536
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 1898 AENDRLKRKAEEEGyqrKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKAS 1975
Cdd:pfam15964 537 LEKESIQQSFSNEA---KAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEIT 611
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2200-2477 |
4.56e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2200 KLAEKTLKQKSSVEEelvkVKVQLDETDKQKSVLDVELKRLKQEVSD-----------AIkQKAQVEDELSKVKIQMEDL 2268
Cdd:PRK04863 359 ELEERLEEQNEVVEE----ADEQQEENEARAEAAEEEVDELKSQLADyqqaldvqqtrAI-QYQQAVQALERAKQLCGLP 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2269 LKLKLKIEKENQELMKKDKDNTKKLLEEE-----AENMKKLAEEAARL------NIEAQEAARLRQIAESDLAKQRELAE 2337
Cdd:PRK04863 434 DLTADNAEDWLEEFQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLREQRHLAE 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2338 KM---------LEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITA 2408
Cdd:PRK04863 514 QLqqlrmrlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQA 593
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141765 2409 EAEKLKVKVTQLSDAQSKAEE------EAKKFKKQADEIKIRLQETEKHTSEkhtVVEKLEVQRLQSKQEADGLH 2477
Cdd:PRK04863 594 RIQRLAARAPAWLAAQDALARlreqsgEEFEDSQDVTEYMQQLLERERELTV---ERDELAARKQALDEEIERLS 665
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2228-2479 |
4.61e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2228 KQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLkiekenqelmkkdkdntkklLEEEAENMKKLAEE 2307
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE--------------------YSWDEIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2308 AARLNieaQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ 2387
Cdd:COG4913 670 IAELE---AELERLDA-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2388 ETEgfqKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEKL-EVQR 2466
Cdd:COG4913 746 ELR---ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFN---REWPAETADLDADLESLpEYLA 819
|
250
....*....|...
gi 1207141765 2467 LQSKQEADGLHKA 2479
Cdd:COG4913 820 LLDRLEEDGLPEY 832
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1469-1720 |
4.71e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1469 SEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELlqlrakavdadklrNAAQEEAEKLRKQVAEETQ 1548
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL--------------EALQAEIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1549 KKRKAEEELKRkseaeKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQ---RQIQVVEEVakKTAATQLESKQval 1625
Cdd:COG3883 80 EIEERREELGE-----RARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKiadADADLLEEL--KADKAELEAKK--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1626 tARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEE 1705
Cdd:COG3883 150 -AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
250
....*....|....*
gi 1207141765 1706 AKREAKKRAKAEEAA 1720
Cdd:COG3883 229 AAAAAAAAAAAAAAA 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1103-1307 |
5.11e-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: 45.91 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1103 LRSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQGAediLNKYENQLREVnkvpvnEKEIEASQTQLQKLRSEAEGK 1182
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR---IRALEQELAAL------EAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1183 QATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYDWLIRW 1262
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1207141765 1263 IADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVED 1307
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
45-170 |
5.24e-04 |
|
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: 43.51 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 45 QKKTFTKWVNKHLVKHWKAeaqRHIT-------DLYEDLRDGHNLISLLEVLSGETLPrERDVVRNSRLPrekgrmrFHK 117
Cdd:cd21325 25 EKYAFVNWINKALENDPDC---RHVIpmnpntdDLFKAVGDGIVLCKMINLSVPDTID-ERAINKKKLTP-------FII 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1207141765 118 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVN 170
Cdd:cd21325 94 QENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2301-2440 |
5.87e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.86 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2301 MKKLAEEAARLNIEAQEAARlRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL--LEAK 2378
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAE-EKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLdnLENQ 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 2379 KEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2440
Cdd:PRK12705 107 LEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEE 168
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1585-1910 |
6.25e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.01 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1585 AEEAERHLKQAELEKQRQIQVVEEVAK------KTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEAd 1658
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGqvtesvEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1659 karEQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKeeakreaKKRAKAEEAALKQKEAAEMELGNQRKMA 1738
Cdd:pfam02029 83 ---LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSR-------LGRYKEEETEIREKEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1739 EETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSN 1818
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1819 T----EKSKQLLESEAaKMRELAEEATKLRSVAEEAKKQRQiaeEEAARQRAEAEKILKEKlTAINEATRLKTEAEIALK 1894
Cdd:pfam02029 233 SqereEEAEVFLEAEQ-KLEELRRRRQEKESEEFEKLRQKQ---QEAELELEELKKKREER-RKLLEEEEQRRKQEEAER 307
|
330
....*....|....*.
gi 1207141765 1895 EKEAENDRLKRKAEEE 1910
Cdd:pfam02029 308 KLREEEEKRRMKEEIE 323
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2553-2642 |
6.45e-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: 45.26 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2553 KKAEALKAEQ-ERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMngKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQS 2631
Cdd:cd16269 200 IEAERAKAEAaEQERKLLEEQQRELEQKLEDQERSYEEHLRQL--KEKMEEERENLLKEQERALESKLKEQEALLEEGFK 277
|
90
....*....|.
gi 1207141765 2632 SQKASYTKEIE 2642
Cdd:cd16269 278 EQAELLQEEIR 288
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2312-2591 |
6.47e-04 |
|
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: 46.37 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2312 NIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAiqEAAKLKAEAEKlQKQKDqAQVEAQKLLEAKKemQQRLDQETEG 2391
Cdd:NF012221 1533 NVVATSESSQQADAVSKHAKQDDAAQNALADKERA--EADRQRLEQEK-QQQLA-AISGSQSQLESTD--QNALETNGQA 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2392 FQKSLEAERKrqlEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQ-ADEIKIRLQEteKHTSEKHTVVEKLEVQRLQSK 2470
Cdd:NF012221 1607 QRDAILEESR---AVTKELTTLAQGLDALDSQATYAGESGDQWRNPfAGGLLDRVQE--QLDDAKKISGKQLADAKQRHV 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2471 QEADGLHKAIADLEkekeklkkeaADLQKQSKEMANVQQEqLQQEKTilqQSFFAEKETLLKKEKAIEEEkkklekqfed 2550
Cdd:NF012221 1682 DNQQKVKDAVAKSE----------AGVAQGEQNQANAEQD-IDDAKA---DAEKRKDDALAKQNEAQQAE---------- 1737
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1207141765 2551 evKKAEAL--KAEQERQRKLMEEERKKLQSAMDAAIKKQKEAE 2591
Cdd:NF012221 1738 --SDANAAanDAQSRGEQDASAAENKANQAQADAKGAKQDESD 1778
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2220-2462 |
6.99e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2220 KVQLDETDKQKSVLDVELKRLKQEVsdAIKQKAQVE-DELSKVKIQ----MEDLLKLKLKIEKENQELMKKDKDNTKKLL 2294
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQI--KTYNKNIEEqRKKNGENIArkqnKYDELVEEAKTIKAEIEELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2295 EEEAENMKKLAEEAARLNIEAQEAARLrqiaesdlakqrelaEKMLEEK------KQAIQEAAKLkaeAEKLQKQKDQAQ 2368
Cdd:PHA02562 251 EDPSAALNKLNTAAAKIKSKIEQFQKV---------------IKMYEKGgvcptcTQQISEGPDR---ITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2369 VEAQKLLEAKKEMQQRLDQETE------GFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2442
Cdd:PHA02562 313 HSLEKLDTAIDELEEIMDEFNEqskkllELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
|
250 260
....*....|....*....|
gi 1207141765 2443 IRLQETEKHTSEKHTVVEKL 2462
Cdd:PHA02562 393 KTKSELVKEKYHRGIVTDLL 412
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2096-2442 |
7.55e-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: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2096 QQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKA----EEAERQKKAAEAEAAKQAKAQEDAEKLRKEAE 2171
Cdd:NF033838 112 EAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAkdqkEEDRRNYPTNTYKTLELEIAESDVEVKKAELE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2172 --KEASRRAEAEAAALKLKQEADSEMAKYKKLaEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIK 2249
Cdd:NF033838 192 lvKEEAKEPRDEEKIKQAKAKVESKKAEATRL-EKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2250 QKAQVEDElSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLleEEAENMKKLAEEAARLNIEAQEAARLR-QIAESD 2328
Cdd:NF033838 271 GEPATPDK-KENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKV--EEAKKKAKDQKEEDRRNYPTNTYKTLElEIAESD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2329 LAKQRELAEKMLEEKKQAIQEAAKLKAEAEklqkqkdqaqveaqklLEAKKEMQQRLDQ-ETEGFQKSLEAERKrqleiT 2407
Cdd:NF033838 348 VKVKEAELELVKEEAKEPRNEEKIKQAKAK----------------VESKKAEATRLEKiKTDRKKAEEEAKRK-----A 406
|
330 340 350
....*....|....*....|....*....|....*..
gi 1207141765 2408 AEAEKLKVKVTQLSDAQS--KAEEEAKKFKKQADEIK 2442
Cdd:NF033838 407 AEEDKVKEKPAEQPQPAPapQPEKPAPKPEKPAEQPK 443
|
|
| DUF2968 |
pfam11180 |
Protein of unknown function (DUF2968); This family of proteins has no known function. |
2298-2374 |
7.94e-04 |
|
Protein of unknown function (DUF2968); This family of proteins has no known function.
Pssm-ID: 431707 [Multi-domain] Cd Length: 180 Bit Score: 43.52 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2298 AENMKKLAE-EAARLNIEAQEAARLRQIAES---------DLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQA 2367
Cdd:pfam11180 88 ARQTAQLADvEIRRAQLEAQKAQTERQIAASearaarlqaDLQVARQQEQQVASRQKQTRQEAAALEAQRQAAQAQLRAL 167
|
....*..
gi 1207141765 2368 QVEAQKL 2374
Cdd:pfam11180 168 QRQIRQL 174
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1758-2642 |
8.12e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1758 DFEHAEQQRTVLDDELQRLKNDVNSAVK-QKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQ-LLESEAAKMRE 1835
Cdd:TIGR00606 55 DFPPGTKGNTFVHDPKVAQETDVRAQIRlQFRDVNGEECAVVRSMVCTQKTKKTEFKTLEGVITRYKHgEKVSLSSKCAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1836 LAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATR----LKTEAEIAL------KEKEAENDRLKR 1905
Cdd:TIGR00606 135 IDREMISHLGVSKAVLNNVIFCHQEDSNWPLSEGKALKQKFDEIFSATRyikaLETLRQVRQtqgqkvQEHQMELKYLKQ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1906 KAEEEGYQRKVLEDQAAQhkQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKlnfekasSGKQELELEL 1985
Cdd:TIGR00606 215 YKEKACEIRDQITSKEAQ--LESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALK-------SRKKQMEKDN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1986 KKLKGIADETQKSKAKAEEEAEKFRKlaleeekkrkeaeakvKQIQAAEEEAARQHKaaqeEVGRLMKLAEEAKKQKEIA 2065
Cdd:TIGR00606 286 SELELKMEKVFQGTDEQLNDLYHNHQ----------------RTVREKERELVDCQR----ELEKLNKERRLLNQEKTEL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2066 EKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKE-EFEKAKKLAQE--AEKAKDNAEKEAALLHKKAEEA 2142
Cdd:TIGR00606 346 LVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSErQIKNFHTLVIErqEDEAKTAAQLCADLQSKERLKQ 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2143 ERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQ 2222
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKS 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2223 LDEtdkQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKD--NTKKL---LEEE 2297
Cdd:TIGR00606 506 LQN---EKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpNKKQLedwLHSK 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2298 AENMKKLAEEAARLNIEAQEAARLRQIAESDLaKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEA 2377
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNEL-ESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGA 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2378 KKEMQQRLDQETEGFQKSL---EAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEI----KIRLQETEK 2450
Cdd:TIGR00606 662 TAVYSQFITQLTDENQSCCpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglaPGRQSIIDL 741
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2451 HTSEKHTVVEKLEVQRLQSKQEADGLHKAiADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETL 2530
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQ-ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDL 820
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2531 LKKEKAIEEEKKKLEKQFEDEVKKAEALK---------------------------AEQERQRKLMEEERKKLQSAMDAA 2583
Cdd:TIGR00606 821 DRTVQQVNQEKQEKQHELDTVVSKIELNRkliqdqqeqiqhlksktnelkseklqiGTNLQRRQQFEEQLVELSTEVQSL 900
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141765 2584 IKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSS--QKASYTKEIE 2642
Cdd:TIGR00606 901 IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKvkNIHGYMKDIE 961
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2765-2798 |
8.53e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 8.53e-04
10 20 30
....*....|....*....|....*....|....
gi 1207141765 2765 LLEAQAASGYIIDPIKNRRLSVSESVKDGLIGPE 2798
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3419-3452 |
8.53e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 8.53e-04
10 20 30
....*....|....*....|....*....|....
gi 1207141765 3419 LLEAQAATGYIIDPIRNEMFTVDDAVKAGIVGPE 3452
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
551-645 |
8.67e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.55 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 551 LKYIQDLLSWVEENQRRIEGAEWGEDLPSVESQLGSHRGLHQSIEEFKYKIDRARADENQLT---PVSKGAYREYLGKLD 627
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIeegHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1207141765 628 LQYAKLLTSSKTRLRSLD 645
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2189-2393 |
8.78e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2189 QEADSEMAKYKK---------LAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKA--QVEDE 2257
Cdd:COG3206 192 EEAEAALEEFRQknglvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2258 LSKVKIQMedllklklkiekenQELMKKDKDNT---KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQre 2334
Cdd:COG3206 272 LAELEAEL--------------AELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQ-- 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141765 2335 laekmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQ 2393
Cdd:COG3206 336 -----LAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1510-1742 |
9.00e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1510 TAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaLEDLEKFKLQAEEAe 1589
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL--------------QAEIDKLQAEIAEA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1590 rhlkQAELEKQRqiqvvEEVAKKTAATQLESKQVALTARLEES----------------LKNEQVMVIQLQEEAEHLKKQ 1653
Cdd:COG3883 78 ----EAEIEERR-----EELGERARALYRSGGSVSYLDVLLGSesfsdfldrlsalskiADADADLLEELKADKAELEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1654 QAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGN 1733
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
....*....
gi 1207141765 1734 QRKMAEETA 1742
Cdd:COG3883 229 AAAAAAAAA 237
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
45-169 |
1.19e-03 |
|
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: 42.30 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 45 QKKTFTKWVNKHLVKHWKAeaqRHIT-------DLYEDLRDGHNLISLLEVLSGETLPrERDVVRNSRLPrekgrmrFHK 117
Cdd:cd21324 25 EKYAFVNWINKALENDPDC---KHVIpmnpntdDLFKAVGDGIVLCKMINFSVPDTID-ERTINKKKLTP-------FTI 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 118 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 169
Cdd:cd21324 94 QENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1758-1927 |
1.19e-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: 45.31 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1758 DFEHAEQQRTVLDDELQRL---------KNDVNSAVKQKKELEEELIkvrkemeillqQKSKAEKetmsnTEKSKQLLES 1828
Cdd:pfam04147 126 DDDSEEEEDGQLDLKRVRRahfgggeddEEEEPERKKSKKEVMEEVI-----------AKSKLHK-----YERQKAKEED 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1829 EAakMRE-----LAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAE--KILKEkLTAINEAT---RLKTEAEIALKEKE- 1897
Cdd:pfam04147 190 EE--LREeldkeLKDLRSLLSGSKRPKPEQAKKPEEKPDRKKPDDDydKLVRE-LAFDKRAKpsdRTKTEEELAEEEKEr 266
|
170 180 190
....*....|....*....|....*....|....
gi 1207141765 1898 ---AENDRLKR-KAEEEGYQRKvlEDQAAQHKQA 1927
Cdd:pfam04147 267 lekLEEERLRRmRGEEDEEEED--GKKKKKHKSA 298
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2198-2413 |
1.21e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2198 YKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiek 2277
Cdd:PRK09510 64 YNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQA--------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2278 enQELMKKDKDNTKKLLEEEAenmKKLAEEAARlnieAQEAARLRQIAESDlAKQRELAEKMLEEKKQAiQEAAKLKAEA 2357
Cdd:PRK09510 135 --EEAAAKAAAAAKAKAEAEA---KRAAAAAKK----AAAEAKKKAEAEAA-KKAAAEAKKKAEAEAAA-KAAAEAKKKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141765 2358 EKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKL 2413
Cdd:PRK09510 204 EAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1718-1961 |
1.25e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1718 EAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKV 1797
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1798 RKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLT 1877
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1878 AINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQR 1957
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
....
gi 1207141765 1958 KVVE 1961
Cdd:COG4372 288 LEEA 291
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1636-1802 |
1.25e-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: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1636 EQVMVIQLQE---EAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKtaaqeeAEKQKEEAKREAKK 1712
Cdd:COG1579 5 DLRALLDLQEldsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL------ELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1713 RAKAEEAA-LKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELE 1791
Cdd:COG1579 79 EEQLGNVRnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|.
gi 1207141765 1792 EELIKVRKEME 1802
Cdd:COG1579 159 EELEAEREELA 169
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1771-2444 |
1.26e-03 |
|
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: 45.43 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1771 DELQRLKNDVNSaVKQK-----KELEEELIKVRKEMEILLQQKSKAEK---ETMSN-----TEKSKQLLESEAAKMRELA 1837
Cdd:TIGR01612 1111 DEINKIKDDIKN-LDQKidhhiKALEEIKKKSENYIDEIKAQINDLEDvadKAISNddpeeIEKKIENIVTKIDKKKNIY 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1838 EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRlKTEAEIALKEKEAEN-DRLKRKAEEEGYQRKV 1916
Cdd:TIGR01612 1190 DEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKK-KSEHMIKAMEAYIEDlDEIKEKSPEIENEMGI 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1917 LEDQAAQ--------------------HKQAI----------------EEKIGQLKKSSDTELDRQKKIVEETLKQRKVV 1960
Cdd:TIGR01612 1269 EMDIKAEmetfnishdddkdhhiiskkHDENIsdirekslkiiedfseESDINDIKKELQKNLLDAQKHNSDINLYLNEI 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1961 EEEIHILKLNFEKA--SSGKQELELELKKLKGIADETQKSKAKAEEEAEkfrKLALEEEKKRKEAEAKVKQIqaaeEEAA 2038
Cdd:TIGR01612 1349 ANIYNILKLNKIKKiiDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD---DINLEECKSKIESTLDDKDI----DECI 1421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2039 RQHKAAQEEVgrlmkLAEEAKKQKEIAE-KEAEKQVILVqeaAQKCSAAEQKAQNVLVQQnKDSMAQD------KLKEEF 2111
Cdd:TIGR01612 1422 KKIKELKNHI-----LSEESNIDTYFKNaDENNENVLLL---FKNIEMADNKSQHILKIK-KDNATNDhdfninELKEHI 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2112 EKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER--QKKAAEAEAAKQAKAQEDAEKLRKEAEKEASrraeaeaaalKLKQ 2189
Cdd:TIGR01612 1493 DKSKGCKDEADKNAKAIEKNKELFEQYKKDVTEllNKYSALAIKNKFAKTKKDSEIIIKEIKDAHK----------KFIL 1562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2190 EADSEMAKYKKLAektlKQKSSVEEELVKV-KVQLDETDKQKSVLDVELKRLK-----QEVSDAIKQKAQVEDELSKVKI 2263
Cdd:TIGR01612 1563 EAEKSEQKIKEIK----KEKFRIEDDAAKNdKSNKAAIDIQLSLENFENKFLKisdikKKINDCLKETESIEKKISSFSI 1638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2264 QMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEK-MLEE 2342
Cdd:TIGR01612 1639 DSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKeEIES 1718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2343 KKQAIQEAAKLKAEA------------EKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETegfQKSLEAERKRQLEITAEA 2410
Cdd:TIGR01612 1719 IKELIEPTIENLISSfntndlegidpnEKLEEYNTEIGDIYEEFIELYNIIAGCLETVS---KEPITYDEIKNTRINAQN 1795
|
730 740 750
....*....|....*....|....*....|....
gi 1207141765 2411 EKLKVKvtqlsdaqskaeEEAKKFKKQADEIKIR 2444
Cdd:TIGR01612 1796 EFLKII------------EIEKKSKSYLDDIEAK 1817
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3456-3492 |
1.29e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.29e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1207141765 3456 KLLSAEKAVTGYKDPYTGNKISLLQAMQKQLVLREHA 3492
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
2292-2522 |
1.37e-03 |
|
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: 44.04 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2292 KLLEEEAENMKKLAEEaarlniEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQ-KQKDQAQVE 2370
Cdd:pfam17045 38 DIREEELLSARNTLER------KHKEIGLLRQQLEELEKGKQELVAKYEQQLQKLQEELSKLKRSYEKLQrKQLKEAREE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2371 AQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITaeaeklkvKVTQLsDAQSKA-EEEAKKFKKQADEIKI--RLQE 2447
Cdd:pfam17045 112 AKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQ--------QVASL-EAQRKAlAEQSSLIQSAAYQVQLegRKQC 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 2448 TEKHTSEKHTVVEKLEVQR---LQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKeMANVQQEQLQQEKTILQQS 2522
Cdd:pfam17045 183 LEASQSEIQRLRSKLERAQdslCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELR-MSQRQLQVLQNELMELKAT 259
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1533-1748 |
1.46e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.59 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1533 QEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERhLKQAELEKQRQIQVVE----- 1607
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAK-AKAAALAKQKREGTEEvteee 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1608 -EVAKKTAATQLESKQVALTArleeslkneqvmviQLQEEAEHLKKQQAEADKAREQAEKeletwRQKANEALRLRLQAE 1686
Cdd:PRK07735 90 kAKAKAKAAAAAKAKAAALAK--------------QKREGTEEVTEEEKAAAKAKAAAAA-----KAKAAALAKQKREGT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 1687 EEAnkktaAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAA 1748
Cdd:PRK07735 151 EEV-----TEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKA 207
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2222-2455 |
1.55e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2222 QLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKL------LE 2295
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVkelkeeRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2296 EEAENMKKLAEEAARLNIEAQEAARLR-----------------QIAESDLAKQRELAEKM------LEEKKQAIQEAAK 2352
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGgsidklrkeierlewrqQTEVLSPEEEKELVEKIkelekeLEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2353 LKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKsLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAK 2432
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE-ADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260
....*....|....*....|...
gi 1207141765 2433 KFKKQADEIKIRLQETEKHTSEK 2455
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKE 263
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1338-1688 |
1.71e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1338 SPLKKA--KMESASD------DIIQEYVTLRTRYSELMTLSSQYIK---FIIETQRRLQDEEK--------AAEKLKEEE 1398
Cdd:PRK04863 226 SGVRKAfqDMEAALRenrmtlEAIRVTQSDRDLFKHLITESTNYVAadyMRHANERRVHLEEAlelrrelyTSRRQLAAE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1399 RKKMAEMQAELEKQK--------------------QLAETHAKAIAKAEQEANELKTKMKD--EVSKRQDVAVD-SEKQK 1455
Cdd:PRK04863 306 QYRLVEMARELAELNeaesdleqdyqaasdhlnlvQTALRQQEKIERYQADLEELEERLEEqnEVVEEADEQQEeNEARA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1456 HNIQRELQELKT--------LSEQEIKA-KSQQVEEAL-----------LSRTRIEEEIHIIRLQLEttmkqknTAETEL 1515
Cdd:PRK04863 386 EAAEEEVDELKSqladyqqaLDVQQTRAiQYQQAVQALerakqlcglpdLTADNAEDWLEEFQAKEQ-------EATEEL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1516 LQLRAKAVDADKLRNAAQEEAEKLRKQVAE--ETQKKRKAEEELK--RKSEAEKDAAKEKKKALEDLEKFKLQAEEAERH 1591
Cdd:PRK04863 459 LSLEQKLSVAQAAHSQFEQAYQLVRKIAGEvsRSEAWDVARELLRrlREQRHLAEQLQQLRMRLSELEQRLRQQQRAERL 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1592 LKQAElekQRQIQVVEevakktAATQLESKQVALTARLeESLKNEQVMVIQLQEEAEHlkkQQAEADKAREQAEKELETW 1671
Cdd:PRK04863 539 LAEFC---KRLGKNLD------DEDELEQLQEELEARL-ESLSESVSEARERRMALRQ---QLEQLQARIQRLAARAPAW 605
|
410
....*....|....*...
gi 1207141765 1672 RQkANEAL-RLRLQAEEE 1688
Cdd:PRK04863 606 LA-AQDALaRLREQSGEE 622
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
1708-1918 |
1.83e-03 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 44.70 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1708 REAKKRAKAEEAALkQKEAAemelgNQRKMAEETAKQKLAAEQE---------LIRLRADFEHAEQQRTVLD-------- 1770
Cdd:NF033875 66 SETPKTAVSEEATV-QKDTT-----SQPTKVEEVASEKNGAEQSsatpndttnAQQPTVGAEKSAQEQPVVSpettnepl 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1771 ---DELQRLKNDVNSAVKQKKELE-----EELIKVRKEMEILLQQKSKaekETMSNTEkSKQLleseAAKMRElaeeatk 1842
Cdd:NF033875 140 gqpTEVAPAENEANKSTSIPKEFEtpdvdKAVDEAKKDPNITVVEKPA---EDLGNVS-SKDL----AAKEKE------- 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141765 1843 lrsVAEEAKKQRQIAEEEAARQRAEAEKILKEKltaineatrlkteAEIALKEkeaendrlkrKAEEEGYQRKVLE 1918
Cdd:NF033875 205 ---VDQLQKEQAKKIAQQAAELKAKNEKIAKEN-------------AEIAAKN----------KAEKERYEKEVAE 254
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1531-1860 |
2.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1531 AAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVA 1610
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1611 KktAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEAN 1690
Cdd:COG4372 122 K--ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1691 KKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLD 1770
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1771 DELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEA 1850
Cdd:COG4372 280 IAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELL 359
|
330
....*....|
gi 1207141765 1851 KKQRQIAEEE 1860
Cdd:COG4372 360 SKGAEAGVAD 369
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1517-1808 |
2.15e-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: 43.75 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1517 QLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAE 1596
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1597 LEKQRQIQVVEEVAKKTAATQLESKQVALTAR----LEESLKNEQVMVIQLQ----EEAEHLKKQQAEADKAREQA---- 1664
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKelekEEEREEDERILEYLKEkaerEEEREAEREEIEEEKEREIArlra 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1665 EKELETWRQKANEALRLRLQAEE---EANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEET 1741
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEqerKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141765 1742 AKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQK 1808
Cdd:pfam13868 272 EDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4032-4063 |
2.21e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.21e-03
10 20 30
....*....|....*....|....*....|..
gi 1207141765 4032 KLLSAERAVTGYKDPYSGKVISLFQAMKKGLI 4063
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1647-1871 |
2.27e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1647 AEHLKKQQAEADKAREQAEKELETWRQKANEAlRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEeAALKQKEA 1726
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEA-EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAR-AELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1727 AEMELGNQRKMAEETAKQkLAAEQELIRLRADFEHAEQQRTVL-------DDELQRLKNDVNSAVKQ-KKELEEELIKVR 1798
Cdd:COG3206 241 RLAALRAQLGSGPDALPE-LLQSPVIQQLRAQLAELEAELAELsarytpnHPDVIALRAQIAALRAQlQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141765 1799 KEMEILLQQKSKAEKETMSNTEKSKQLLESEAaKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKI 1871
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEA-ELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVI 391
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1650-1969 |
2.27e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1650 LKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEM 1729
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1730 ELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKS 1809
Cdd:COG4372 88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1810 KAEKEtmsNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEA 1889
Cdd:COG4372 168 ALEQE---LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1890 EIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKL 1969
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1391-1627 |
2.31e-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: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1391 AEKLKEEERKKMAEMQAELEK-QKQLAETHAKaIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKT-L 1468
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAaQAELDALQAE-LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1469 SEQEIKAKSQQVEEALLSRTRIEEEIHiiRLQLETTMKQKNTAETELLQLRAKAVDADKlrNAAQEEAEKLRKQVAEETQ 1548
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFSDFLD--RLSALSKIADADADLLEELKADKAELEAKK--AELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141765 1549 KKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTA 1627
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1739-1869 |
2.39e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.17 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1739 EETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsN 1818
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQE---R 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141765 1819 TEKSKQLLEsEAAKMRELAEEAT------KLRSVAEEAKKQR----QIAEEEAARQRAEAE 1869
Cdd:PRK11448 215 KQKRKEITD-QAAKRLELSEEETrilidqQLRKAGWEADSKTlrfsKGARPEKGRNLAIAE 274
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3129-3165 |
2.52e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.52e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1207141765 3129 KLLSAERAVCGYKDPYTGKTVSLFEAMQKDLIKKEQG 3165
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1708-1964 |
2.56e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1708 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQK 1787
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1788 KELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEA---AKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQ 1864
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQdleQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1865 RAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELD 1944
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260
....*....|....*....|
gi 1207141765 1945 RQKKIVEETLKQRKVVEEEI 1964
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEE 262
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3957-3995 |
2.60e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.46 E-value: 2.60e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1207141765 3957 YLEGISSIAGVFVEATKDRLSVYQAMKKTMIRPGTAFEL 3995
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1184-1779 |
2.68e-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: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1184 ATFDRLEEELQRATE---VNKRMSQLHSERDVELEHYRQLVGnLRERWQAVFAQielrqRELDLLNRQMQAYRESYDWLI 1260
Cdd:COG4913 235 DDLERAHEALEDAREqieLLEPIRELAERYAAARERLAELEY-LRAALRLWFAQ-----RRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1261 RWIADAKQRQDKLHAVpiggSKGLQEQLTQ-----EKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVT----YKA 1331
Cdd:COG4913 309 AELERLEARLDALREE----LDELEAQIRGnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeeFAA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1332 LVEPIASplKKAKMESASDDIIQEYVTLRTRYSELMtlssqyikfiiETQRRLQDEEKAAEKLKEEERKKMAEMQAELEK 1411
Cdd:COG4913 385 LRAEAAA--LLEALEEELEALEEALAEAEAALRDLR-----------RELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1412 QKQLAETHAKAIA-----KAEQEA---------NELKTKM------KDEVSKrqdvAVDSEKQKHNIQ-------RELQE 1464
Cdd:COG4913 452 ALGLDEAELPFVGelievRPEEERwrgaiervlGGFALTLlvppehYAAALR----WVNRLHLRGRLVyervrtgLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1465 LKTLSEQ----EIKAKSQQVEEALlsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAV-----DADKLR------ 1529
Cdd:COG4913 528 RPRLDPDslagKLDFKPHPFRAWL--EAELGRRFDYVCVDSPEELRRHPRAITRAGQVKGNGTrhekdDRRRIRsryvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1530 --NAAQEEAekLRKQVAEETQKKRKAEEELKrkseaekdaakekkkaledlekfKLQAEEAERHLKQAELEKQRQIQvVE 1607
Cdd:COG4913 606 fdNRAKLAA--LEAELAELEEELAEAEERLE-----------------------ALEAELDALQERREALQRLAEYS-WD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1608 EVAKKTAATQLESKQVALtarleESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEE 1687
Cdd:COG4913 660 EIDVASAEREIAELEAEL-----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1688 EANKKTAAQEEAEKQkeeakrEAKKRAKAEEAALKQKEAAEmELGNQRKMAEETAKQklaAEQELIRLRADF------EH 1761
Cdd:COG4913 735 RLEAAEDLARLELRA------LLEERFAAALGDAVERELRE-NLEERIDALRARLNR---AEEELERAMRAFnrewpaET 804
|
650 660
....*....|....*....|...
gi 1207141765 1762 AEQQRTVLD-----DELQRLKND 1779
Cdd:COG4913 805 ADLDADLESlpeylALLDRLEED 827
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1826-1956 |
2.74e-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: 41.31 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1826 LESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAarqRAEAEKILKEkltAINEATRLKTEaeiALKEKEAENDRLKR 1905
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEA---RAEAAEIIAE---ARKEAEAIAEE---AKAEAEAEAERIIA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141765 1906 KAEEEGYQ-----RKVLEDQAAQHKQAIEEKIgqLKKSSDTelDRQKKIVEETLKQ 1956
Cdd:COG0711 100 QAEAEIEQerakaLAELRAEVADLAVAIAEKI--LGKELDA--AAQAALVDRFIAE 151
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1751-1899 |
2.86e-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: 43.90 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1751 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAE----KETMSNTEKSKQLL 1826
Cdd:pfam05911 682 ENKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAEtqlkCMAESYEDLETRLT 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1827 ESEaAKMRELAEEATKLRSVAEEakkQRQIAEEEAAR--------QRAEAEKILKEklTAINEATRLKTEAEI-ALKEKE 1897
Cdd:pfam05911 762 ELE-AELNELRQKFEALEVELEE---EKNCHEELEAKclelqeqlERNEKKESSNC--DADQEDKKLQQEKEItAASEKL 835
|
..
gi 1207141765 1898 AE 1899
Cdd:pfam05911 836 AE 837
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2291-2438 |
2.89e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2291 KKLLEEEAENMKKLAEEAARLNIEAQEAAR---LRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQA 2367
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEAkelLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 2368 QVEAQKLLEAKKEMQQRLDQETEGFQK--SLEAERKRQ-----LEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQA 2438
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYRvaGLTPEQARKlllklLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
2360-2442 |
3.14e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 42.60 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2360 LQKQKDQAQVEAQKLLEAKKEMQQRLDQETEgfQKSLEAERKRQLeiTAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2439
Cdd:pfam11932 11 LAATLDQALDLAEKAVAAAAQSQKKIDKWDD--EKQELLAEYRAL--KAELESLEVYNRQLERLVASQEQEIASLERQIE 86
|
...
gi 1207141765 2440 EIK 2442
Cdd:pfam11932 87 EIE 89
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
45-159 |
3.31e-03 |
|
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: 41.11 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 45 QKKTFTKWVNKHLVKhwKAEAQRHI------TDLYEDLRDGHNLISLLEVLSGETLPrERDVVRNSRLPrekgrmrFHKL 118
Cdd:cd21292 25 EKVAFVNWINKNLGD--DPDCKHLLpmdpntDDLFEKVKDGILLCKMINLSVPDTID-ERAINKKKLTV-------FTIH 94
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207141765 119 QNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 159
Cdd:cd21292 95 ENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4311-4341 |
3.49e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.08 E-value: 3.49e-03
10 20 30
....*....|....*....|....*....|.
gi 1207141765 4311 AGILDTDTLEKVSVTEAMHRNLVDNITGQRL 4341
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2210-2450 |
3.58e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.41 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2210 SSVEEELVKVKVQLDETDKQKSVLDVEL-KRLKQEVSDAIKQKAQVEDELSKVkiqMEDLLKLKLKIEKENQELMKKdkd 2288
Cdd:COG5185 206 SIKESETGNLGSESTLLEKAKEIINIEEaLKGFQDPESELEDLAQTSDKLEKL---VEQNTDLRLEKLGENAESSKR--- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2289 ntkklLEEEAENMKKLAEEAARLNIEAQEAARLRQ-IAESDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAEKLQKQKDQ 2366
Cdd:COG5185 280 -----LNENANNLIKQFENTKEKIAEYTKSIDIKKaTESLEEQLAAAEAEQELEESKRETETGiQNLTAEIEQGQESLTE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2367 AQVEAQKLLEAKKEMQQ--RLDQETEGFQKSLEAERKRQLEITAEAEK-LKVKVTQLSDAQSKAEEEAKKFKKQADEIKI 2443
Cdd:COG5185 355 NLEAIKEEIENIVGEVElsKSSEELDSFKDTIESTKESLDEIPQNQRGyAQEILATLEDTLKAADRQIEELQRQIEQATS 434
|
....*..
gi 1207141765 2444 RLQETEK 2450
Cdd:COG5185 435 SNEEVSK 441
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2211-2449 |
3.58e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2211 SVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEdllklklKIEKENQELMKKDKDnt 2290
Cdd:PRK01156 194 SSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLED-------MKNRYESEIKTAESD-- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2291 KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVE 2370
Cdd:PRK01156 265 LSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKK 344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141765 2371 AQKLLEAKKEMQQrLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETE 2449
Cdd:PRK01156 345 KSRYDDLNNQILE-LEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2294-2440 |
3.84e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2294 LEEEAENMKKLAEEAARLNIEAQE--AARLRQIAESDLAKQ-RELAEKMLEEKKQAIQ----EAAKLKAEAEKLQKQKDQ 2366
Cdd:PRK07735 37 LEEENREKEKALPKNDDMTIEEAKrrAAAAAKAKAAALAKQkREGTEEVTEEEKAKAKakaaAAAKAKAAALAKQKREGT 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141765 2367 AQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2440
Cdd:PRK07735 117 EEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGE 190
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2291-2440 |
4.18e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2291 KKLLEEEAENMKKLAE---EAARLNIEAQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAEKLQKQKDQ 2366
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKEAEAIKKEALLE-AKEEIHKLRNEFEKELRERRNELQKLeKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141765 2367 AQVEAQKLLEAKKEMQQRLDQ--ETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2440
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQEleKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVEEEARHEAAVLIKEIEE 180
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
47-156 |
4.56e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 43.01 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 47 KTFTKWVNKHLVKHwkaeaqrHITDLYEDLRDGhnlISLLEVLSGETLPRERDVVRNSRLPREKGRM-RFHKLQNVQIAL 125
Cdd:COG5069 382 RVFTFWLNSLDVSP-------EITNLFGDLRDQ---LILLQALSKKLMPMTVTHKLVKKQPASGIEEnRFKAFENENYAV 451
|
90 100 110
....*....|....*....|....*....|.
gi 1207141765 126 DFLKHRQVKLVNIRNDDIADGNpKLTLGLIW 156
Cdd:COG5069 452 DLGITEGFSLVGIKGLEILDGI-RLKLTLVW 481
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1831-1974 |
4.61e-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: 42.96 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1831 AKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEE 1910
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1911 GYQRKVLEDQAAQHKQAIEE------KIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKA 1974
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2408-2617 |
4.67e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2408 AEAEKLKVKVtqlsdAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEK 2487
Cdd:PRK09510 75 KRAEEQRKKK-----EQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2488 EKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKEtllkkekaieeekkkLEKQFEDEVKKaealKAEQERQRK 2567
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAE---------------AAAKAAAEAKK----KAEAEAKKK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2568 LMEEERKKlqSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAE 2617
Cdd:PRK09510 211 AAAEAKKK--AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
2292-2414 |
4.76e-03 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 43.17 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2292 KLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESdLAKQrelAEKMLEEKKQAIQEAAKLKAEA-----EKLQKQKDQ 2366
Cdd:PRK00290 499 GLSDEEIERMVKDAEANAEEDKKRKELVEARNQADS-LIYQ---TEKTLKELGDKVPADEKEKIEAaikelKEALKGEDK 574
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2367 AQVEA--QKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLK 2414
Cdd:PRK00290 575 EAIKAktEELTQASQKLGEAMYQQAQAAQGAAGAAAKDDDVVDAEFEEVK 624
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2202-2519 |
5.07e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2202 AEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQmedllklklkiekenQE 2281
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE---------------LA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2282 LMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQ 2361
Cdd:COG4372 98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2362 KQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEI 2441
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 2442 KIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIL 2519
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1780-2317 |
5.24e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1780 VNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEA---KKQRQI 1856
Cdd:COG5185 3 QRSKFLQVKNPLAKEGNANKELIEILLESSKSEGKTLVFITILFFPLGISRDSLRVTLRSVINVLDGLNYQndvKKSESS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1857 AEEEAARQRA-EAEKILKEKLTAINEATRLKTEAEIA---LKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKI 1932
Cdd:COG5185 83 VKARKFLKEKkLDTKILQEYVNSLIKLPNYEWSADILislLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVETGIIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1933 GQLKKSSDTELDRQKK--IVEETLKQRKVVEEEihiLKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFR 2010
Cdd:COG5185 163 DIFGKLTQELNQNLKKleIFGLTLGLLKGISEL---KKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2011 KLALEEEKKRKEA---EAKVKQIQAAEEEAARQH----KAAQEEVGRLMKLAEEAKKQkeIAEKEAEKQVILVQEAAQKC 2083
Cdd:COG5185 240 DPESELEDLAQTSdklEKLVEQNTDLRLEKLGENaessKRLNENANNLIKQFENTKEK--IAEYTKSIDIKKATESLEEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2084 SAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakaqedA 2163
Cdd:COG5185 318 LAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEE------------------L 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2164 EKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEK-------TLKQKSSVEEELVKVKVQLDE--TDKQKSVLD 2234
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRqieelqrQIEQATSSNEEVSKLLNELISelNKVMREADE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2235 VELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIE 2314
Cdd:COG5185 460 ESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
...
gi 1207141765 2315 AQE 2317
Cdd:COG5185 540 ALE 542
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1450-1661 |
5.38e-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: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1450 DSEKQKHNIQRElqelktlSEQEIKAKSQQVEEAllsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVdADKlr 1529
Cdd:COG2268 200 DARIAEAEAERE-------TEIAIAQANREAEEA---ELEQEREIETARIAEAEAELAKKKAEERREAETARAE-AEA-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1530 nAAQEEAEKLRKQVAEETQKKRKAEE-ELKRKseaekdaakekkkaledlEKFKLQAEEAERHLKQAELEKQRQIQVVE- 1607
Cdd:COG2268 267 -AYEIAEANAEREVQRQLEIAEREREiELQEK------------------EAEREEAELEADVRKPAEAEKQAAEAEAEa 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141765 1608 --EVAKKTAATQLESKQVALTARLEESLKNEQVMVIQ-LQEEAEHLKKQQAEADKAR 1661
Cdd:COG2268 328 eaEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEkLPEIAEAAAKPLEKIDKIT 384
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2105-2413 |
5.40e-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: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2105 DKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAA 2184
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2185 LKLKQEADSEMAKYKKLAEKTLKQKSSVEEelvkvkvQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQ 2264
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDE-------FNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2265 MEDLLKLKLKIEKENQELMKKDKDN-----TKKLLEEEAENMKKLAEEAARLNIEAQEA---ARLRQIAESDLAKQRElA 2336
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQDEKAErdelrAKLYQEEQERKERQKEREEAEKKARQRQElqqAREEQIELKERRLAEE-A 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2337 EKMLEEKKQAIQEAAKL----KAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQET-EGFQKSLEAERKRQLEITAEAE 2411
Cdd:pfam13868 257 EREEEEFERMLRKQAEDeeieQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEElEEGERLREEEAERRERIEEERQ 336
|
..
gi 1207141765 2412 KL 2413
Cdd:pfam13868 337 KK 338
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1165-1691 |
5.50e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1165 IEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLrERWQAVFAQIELRQRELDL 1244
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNL-EKKQKKFDQMLAEEKAISA 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1245 lnrqmqAYRESYDwliRWIADAKQRQDKLHAvpiggskgLQEQLTQEKKLLEEIEK-NKDKVEDCQKFAKGYIDAIKDYE 1323
Cdd:pfam01576 619 ------RYAEERD---RAEAEAREKETRALS--------LARALEEALEAKEELERtNKQLRAEMEDLVSSKDDVGKNVH 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1324 lQLVTYKALVEPIASPLkKAKMESASDDI-IQEYVTLRTRYSeLMTLSSQYikfiietQRRLQDEEKAAEKLKEEERKKM 1402
Cdd:pfam01576 682 -ELERSKRALEQQVEEM-KTQLEELEDELqATEDAKLRLEVN-MQALKAQF-------ERDLQARDEQGEEKRRQLVKQV 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1403 AEMQAELE---KQKQLAETHAKaiaKAEQEANELKTKMkDEVSKRQDVAVDSEK----QKHNIQRELQELKtLSEQEIKA 1475
Cdd:pfam01576 752 RELEAELEderKQRAQAVAAKK---KLELDLKELEAQI-DAANKGREEAVKQLKklqaQMKDLQRELEEAR-ASRDEILA 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1476 KSQQVEEALLSrtrIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVA---EETQKKRK 1552
Cdd:pfam01576 827 QSKESEKKLKN---LEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAqleEELEEEQS 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1553 AEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAK---KTAATQLESKQVALTARL 1629
Cdd:pfam01576 904 NTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKskfKSSIAALEAKIAQLEEQL 983
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1630 EESLKNEQVMVIQLQEEAEHLKK-------QQAEADKAREQAEKELETWRQkaneaLRLRL-QAEEEANK 1691
Cdd:pfam01576 984 EQESRERQAANKLVRRTEKKLKEvllqvedERRHADQYKDQAEKGNSRMKQ-----LKRQLeEAEEEASR 1048
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2294-2629 |
5.67e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2294 LEEEAENMKKLAEE----AARLNIeAQEAARLR-QI--AESDLAkqrELAEKmLEEKKQAIQEAAKLKAEAEKlqkQKDQ 2366
Cdd:PRK04863 316 LAELNEAESDLEQDyqaaSDHLNL-VQTALRQQeKIerYQADLE---ELEER-LEEQNEVVEEADEQQEENEA---RAEA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2367 AQveaQKLLEAKKEM---QQRLD-QETEG--FQKSLEA-ERKRQL----------------EITAEAEKLKVKV----TQ 2419
Cdd:PRK04863 388 AE---EEVDELKSQLadyQQALDvQQTRAiqYQQAVQAlERAKQLcglpdltadnaedwleEFQAKEQEATEELlsleQK 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2420 LSDAQSKAEEEAKKFK---KQADEI-KIRLQETEKHTSEKHTVvEKLEVQRLQSKQEAdglHKAIADLEKEKEKLKKEAA 2495
Cdd:PRK04863 465 LSVAQAAHSQFEQAYQlvrKIAGEVsRSEAWDVARELLRRLRE-QRHLAEQLQQLRMR---LSELEQRLRQQQRAERLLA 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2496 DLQKQSKEMANVQQ--EQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLME--- 2570
Cdd:PRK04863 541 EFCKRLGKNLDDEDelEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREqsg 620
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 2571 ---EERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRieqEKLLAEENKNLrEKLQQL 2629
Cdd:PRK04863 621 eefEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEI---ERLSQPGGSED-PRLNAL 678
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1594-1911 |
5.95e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.92 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1594 QAELEKQRQiQVVEevAKKTAATQLESKQVALTARLEESLKNE---QVMVIQLQEEAEHLKKQQAEADKAREQAEKELET 1670
Cdd:PLN03229 435 EGEVEKLKE-QILK--AKESSSKPSELALNEMIEKLKKEIDLEyteAVIAMGLQERLENLREEFSKANSQDQLMHPVLME 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1671 WRQKANEALRLRL-QAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQR-KMA---EETAKQK 1745
Cdd:PLN03229 512 KIEKLKDEFNKRLsRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIKeKMEalkAEVASSG 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1746 LAAEQELirlradfehaeqqrtvlDDELqrlkndVNSAVKQKKELEEELIKVRKEME---ILLQQKSKAEKETMSNTEKS 1822
Cdd:PLN03229 592 ASSGDEL-----------------DDDL------KEKVEKMKKEIELELAGVLKSMGlevIGVTKKNKDTAEQTPPPNLQ 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1823 KQL--LESEAAKMRELAEEATKLRSVAEEAKKqrQIAEEEAARQRAEAEKI------LKEKLTAINEATRLKT-----EA 1889
Cdd:PLN03229 649 EKIesLNEEINKKIERVIRSSDLKSKIELLKL--EVAKASKTPDVTEKEKIealeqqIKQKIAEALNSSELKEkfeelEA 726
|
330 340
....*....|....*....|....
gi 1207141765 1890 EIALKEK--EAENDRLKRKAEEEG 1911
Cdd:PLN03229 727 ELAAAREtaAESNGSLKNDDDKEE 750
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1527-1692 |
5.97e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1527 KLRNAAQEEAEKLRKQVAEETQK-----KRKAEEELKrkseaekdaakekkkaledlEKFKLQAEEAERHLKQAELEKQR 1601
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKeaeaiKKEALLEAK--------------------EEIHKLRNEFEKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1602 Q----IQVVEEVAKKTAAtqLESKQVALTARlEESLKNEQVMVIQLQEEAEHLKKQQAE---------ADKAR----EQA 1664
Cdd:PRK12704 87 LekrlLQKEENLDRKLEL--LEKREEELEKK-EKELEQKQQELEKKEEELEELIEEQLQelerisgltAEEAKeillEKV 163
|
170 180
....*....|....*....|....*...
gi 1207141765 1665 EKELETwrQKANEALRLRLQAEEEANKK 1692
Cdd:PRK12704 164 EEEARH--EAAVLIKEIEEEAKEEADKK 189
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1406-1666 |
5.99e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1406 QAELEKQKQlaethAKAiAKAEQEANELKTKMKDEVSKrqdvAVDSEKQKHNIQRELQELKTLSEQEIKA-KSQQVEEAL 1484
Cdd:PRK05035 459 QARLEREKA-----ARE-ARHKKAAEARAAKDKDAVAA----ALARVKAKKAAATQPIVIKAGARPDNSAvIAAREARKA 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1485 LSRTRIEEEihiirlqlettmkQKNTAETELLQLRAKAVDADKLRNAAQEEAEKlrKQVAEETQKKRKAEEEL---KRKS 1561
Cdd:PRK05035 529 QARARQAEK-------------QAAAAADPKKAAVAAAIARAKAKKAAQQAANA--EAEEEVDPKKAAVAAAIaraKAKK 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1562 EAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAtqleskqVALTARLEESLKNEQVMVI 1641
Cdd:PRK05035 594 AAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA-------VAAAIARAKARKAAQQQAN 666
|
250 260
....*....|....*....|....*
gi 1207141765 1642 QLQEEAEHLKKQQAEADKAREQAEK 1666
Cdd:PRK05035 667 AEPEEAEDPKKAAVAAAIARAKAKK 691
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2039-2143 |
6.08e-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: 39.93 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2039 RQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAaqkcsaaEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLA 2118
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREA-------QQNYERELVLHAEDIKALQALREELNELKAEI 73
|
90 100
....*....|....*....|....*
gi 1207141765 2119 QEAEKAKDNAEKEAALLHKKAEEAE 2143
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQK 98
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1708-2144 |
6.23e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.72 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1708 REAKKRAKAEEAALKQKEAAEMElgnQRKMAEETAKQKLAAEQELIRLRADFEHAEQQrtvlddelqrlkndvnsAVKQK 1787
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAE---KRAAAEAEQKAKEEAEEERLAELEAKRQAEEE-----------------AREAK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1788 KELEEELIKVRKEMEillQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAE----EEAAR 1863
Cdd:COG3064 62 AEAEQRAAELAAEAA---KKLAEAEKAA----AEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAkrkaEEEAK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1864 QRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTEL 1943
Cdd:COG3064 135 RKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1944 DRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEA 2023
Cdd:COG3064 215 ALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2024 EAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMA 2103
Cdd:COG3064 295 LVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGA 374
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1207141765 2104 QDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER 2144
Cdd:COG3064 375 LLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAA 415
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1783-1909 |
6.35e-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: 39.52 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1783 AVKQKKELEEELIKVRKEMEillqqksKAEKETMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEEAKKQRQIAEEEAA 1862
Cdd:pfam20492 4 AEREKQELEERLKQYEEETK-------KAQEELEESEETAEELEE----ERRQAEEEAERLEQKRQEAEEEKERLEESAE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207141765 1863 RQRAEAEKILKEKLTAINEATRLKTEAEialkEKEAENDRLKRKAEE 1909
Cdd:pfam20492 73 MEAEEKEQLEAELAEAQEEIARLEEEVE----RKEEEARRLQEELEE 115
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1060-1483 |
6.78e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1060 TQRATEQKKVQTELEGIKKDLDKVVEKSEAVLATSQQSSSAPVLRSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQ 1139
Cdd:pfam05483 356 ATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELK 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1140 GAE-DILNKYENQLREVNKVPVNEKEIEASQ----TQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVEL 1214
Cdd:pfam05483 436 GKEqELIFLLQAREKEIHDLEIQLTAIKTSEehylKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLEL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1215 EHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESY----DWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQ 1290
Cdd:pfam05483 516 KKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1291 EKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMEsasddiIQEYVTLRTRYSELMTLS 1370
Cdd:pfam05483 596 CNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK------FEEIIDNYQKEIEDKKIS 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1371 SQYIKFIIETQRRLQDEE-KAAEKLKEEERKKMAEMQAELEKQKQlaeTHAKAIAKAEQEANELKTKMKDEVSKRqdvaV 1449
Cdd:pfam05483 670 EEKLLEEVEKAKAIADEAvKLQKEIDKRCQHKIAEMVALMEKHKH---QYDKIIEERDSELGLYKNKEQEQSSAK----A 742
|
410 420 430
....*....|....*....|....*....|....
gi 1207141765 1450 DSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEA 1483
Cdd:pfam05483 743 ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEA 776
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1755-2142 |
6.94e-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: 42.57 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1755 LRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMR 1834
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1835 ELAEEATKLrSVAEEAKKQRqIAEEEAARQRAEAEKILKEkltaiNEATRLKTEAEIA---LKEKEAENDRLKRKAEEEG 1911
Cdd:pfam07888 112 ELSEEKDAL-LAQRAAHEAR-IRELEEDIKTLTQRVLERE-----TELERMKERAKKAgaqRKEEEAERKQLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1912 YQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIveeTLKQRKVVEEEIHILKLNF--EKASSGKQELELELKKLK 1989
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL---TTAHRKEAENEALLEELRSlqERLNASERKVEGLGEELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1990 GIAdeTQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQE---------EVGRLMKLAEEAKK 2060
Cdd:pfam07888 262 SMA--AQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADkdrieklsaELQRLEERLQEERM 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2061 QKEIAEKE--AEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKlKEEFEKAKKLAQEAEKAKDNAEKEAALLHKK 2138
Cdd:pfam07888 340 EREKLEVElgREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK-QELLEYIRQLEQRLETVADAKWSEAALTSTE 418
|
....
gi 1207141765 2139 AEEA 2142
Cdd:pfam07888 419 RPDS 422
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1826-2068 |
7.05e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1826 LESEAAKMRELAEEATKLRSVAEEAKKQRQIAEE-EAARQRAEAEKILKEKLTAINEATRLKTeAEIALKEKEAENDRLK 1904
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIELLEPiRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1905 RKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKlnfekassgkqelele 1984
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE---------------- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1985 lkklkgiadetqkskakaeeeaEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEI 2064
Cdd:COG4913 366 ----------------------ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
....
gi 1207141765 2065 AEKE 2068
Cdd:COG4913 424 LEAE 427
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2200-2530 |
7.10e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2200 KLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkieken 2279
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2280 QELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEK 2359
Cdd:COG4372 72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2360 LQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2439
Cdd:COG4372 152 LKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2440 EIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIL 2519
Cdd:COG4372 232 GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIG 311
|
330
....*....|.
gi 1207141765 2520 QQSFFAEKETL 2530
Cdd:COG4372 312 ALEDALLAALL 322
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1518-1676 |
7.19e-03 |
|
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: 41.23 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1518 LRAKAVDADKLRNAAQEEAEK------LRKQVAEETQK---KRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEA 1588
Cdd:pfam13904 61 LAAKQRQRQKELQAQKEEREKeeqeaeLRKRLAKEKYQewlQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1589 ERHLKQAELEKQRQIQvveevAKKtaatqleskqvaltarleeslkneqvmviqlQEEAEHLKKQQAEADKAREQAEKEL 1668
Cdd:pfam13904 141 KEVLQEWERKKLEQQQ-----RKR-------------------------------EEEQREQLKKEEEEQERKQLAEKAW 184
|
....*...
gi 1207141765 1669 ETWRQKAN 1676
Cdd:pfam13904 185 QKWMKNVK 192
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2284-2430 |
7.23e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2284 KKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKmLEEKKQAIQ---EAAKLKAEAEKL 2360
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVRnnkEYEALQKEIESL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141765 2361 QKQKDQA---QVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEE 2430
Cdd:COG1579 102 KRRISDLedeILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
2549-2631 |
7.38e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 42.67 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2549 EDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEE----MNGKQKEM--QDLEK--KRIEQeklLAEEN- 2619
Cdd:pfam13779 495 QERLSEALERGASDEEIAKLMQELREALDDYMQALAEQAQQNPQDlqqpDDPNAQEMtqQDLQRmlDRIEE---LARSGr 571
|
90
....*....|...
gi 1207141765 2620 -KNLREKLQQLQS 2631
Cdd:pfam13779 572 rAEAQQMLSQLQQ 584
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1577-1793 |
7.45e-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: 42.06 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1577 DLEKFKLQAEEAERHLKQAE-----LEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLK 1651
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKkeekaLLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1652 KQQAEADKAREQAEKELETWRQKANEALRlRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAkaeEAALKQKEAAEMEL 1731
Cdd:COG4942 108 ELLRALYRLGRQPPLALLLSPEDFLDAVR-RLQYLKYLAPARREQAEELRADLAELAALRAEL---EAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141765 1732 GNQRKmaeETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEE 1793
Cdd:COG4942 184 EEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3995-4029 |
7.66e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.08 E-value: 7.66e-03
10 20 30
....*....|....*....|....*....|....*
gi 1207141765 3995 LLEAQAATGYIIDPIKNLKMNVQEAVKMGVVGPEF 4029
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
2280-2387 |
7.69e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 181442 [Multi-domain] Cd Length: 141 Bit Score: 40.06 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2280 QELMKKDKDNTKKLLEEEAEnmkkLAEEAARLNIEAQEAARlrQIAESDLAKQRELAEKMLEEKKQAIqeAAKLKAEAEK 2359
Cdd:PRK08476 40 NASIKNDLEKVKTNSSDVSE----IEHEIETILKNAREEAN--KIRQKAIAKAKEEAEKKIEAKKAEL--ESKYEAFAKQ 111
|
90 100
....*....|....*....|....*....
gi 1207141765 2360 LQKQKDQAQVEAQ-KLLEAKKEMQQRLDQ 2387
Cdd:PRK08476 112 LANQKQELKEQLLsQMPEFKEALNAKLSK 140
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1382-1692 |
7.71e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1382 RRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEAN---ELKTKMKDEVSKRQDVAVDSEKQKHNI 1458
Cdd:pfam13868 24 RDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyrqELEEQIEEREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1459 QRELQELKTLSEQEIKAKSQQVEEALlsrtriEEEIHIIRLQLEttMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEK 1538
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLR------EEIDEFNEEQAE--WKELEKEEEREEDERILEYLKEKAEREEEREAER 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1539 LRKQVAEETQKKRKAEEELKRKseaekdaakeKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQL 1618
Cdd:pfam13868 176 EEIEEEKEREIARLRAQQEKAQ----------DEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141765 1619 ESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELE-TWRQKANEALRLRLQAEEEANKK 1692
Cdd:pfam13868 246 ELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEkQIEEREEQRAAEREEELEEGERL 320
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
2305-2449 |
7.78e-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: 40.02 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2305 AEEAARLNIEAQEAARLRQIAESDLAKQRELAEKML--EEKKQAIQEAAKLKAEAEKL-QKQKDQAQVEAQKLLEAKKEM 2381
Cdd:pfam05672 9 AEEAARILAEKRRQAREQREREEQERLEKEEEERLRkeELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEER 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141765 2382 QQRLDQETEGFQKSLEAERKRQLEitaEAEKLKVKVTQLsdaQSKAEEEAKKFKKQADEIKIRLQETE 2449
Cdd:pfam05672 89 EQREQEEQERLQKQKEEAEAKARE---EAERQRQEREKI---MQQEEQERLERKKRIEEIMKRTRKSD 150
|
|
| SH3_Eps8 |
cd11764 |
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ... |
848-882 |
8.00e-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: 37.24 E-value: 8.00e-03
10 20 30
....*....|....*....|....*....|....*
gi 1207141765 848 EITVHKGDECALVNNSQPYkWKVRDSSGNEAVVPS 882
Cdd:cd11764 15 ELSVLKGEYLEVLDDSRQW-WKVRNSRGQVGYVPH 48
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
51-158 |
8.01e-03 |
|
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: 39.20 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 51 KWVNKHLvkhWKAEAQR-HITDLYEDLRDGHNLISLLEVLSGETLPR--------ERDVVRNSRlprekgrmrfHKLQNV 121
Cdd:cd21218 17 RWVNYHL---KKAGPTKkRVTNFSSDLKDGEVYALLLHSLAPELCDKelvlevlsEEDLEKRAE----------KVLQAA 83
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141765 122 QiALDFLKHrqvklvnIRNDDIADGNPKLTLGLIWTI 158
Cdd:cd21218 84 E-KLGCKYF-------LTPEDIVSGNPRLNLAFVATL 112
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1823-1937 |
8.05e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1823 KQLLESEAAKMRELA----EEATKlrsVAEEAKKQRQI-AEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKE 1897
Cdd:PRK12704 26 KKIAEAKIKEAEEEAkrilEEAKK---EAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1207141765 1898 AENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKK 1937
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| T3SSipB |
pfam16535 |
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial ... |
2332-2448 |
8.12e-03 |
|
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial proteins that invade human intestinal cells via the type III secretion system translocators. T3SSipB represents the coiled -coil region of the proteins and is shown to be homologous in activity to the pore-forming toxins of other Gram-negative pathogens, such as colicin Ia.
Pssm-ID: 435406 [Multi-domain] Cd Length: 155 Bit Score: 40.33 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 2332 QRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKR-QLEITAEA 2410
Cdd:pfam16535 37 QQQKGLELSDEFQTALSEAEEATDAYEKAINKLKNAKSKAKAAEKKIDQAQTRLQSLAPDSPGKAKLEAAEqQAGIKKDA 116
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141765 2411 EKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQET 2448
Cdd:pfam16535 117 LQADRTLDKALDAASKLTTKAMAKEKEADDFSAKFQGT 154
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1775-1892 |
8.23e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1775 RLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQR 1854
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207141765 1855 qiaeEEAARQRAEAEKILKEKLTAINEATRLK----TEAEIA 1892
Cdd:COG0542 481 ----EQRYGKIPELEKELAELEEELAELAPLLreevTEEDIA 518
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
660-740 |
8.29e-03 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 38.84 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 660 WLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNVQMTGDKLLKDGHPARKTIEAFTAALQTQWSWILQL 739
Cdd:pfam00435 16 WIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERWEQLLEL 95
|
.
gi 1207141765 740 C 740
Cdd:pfam00435 96 A 96
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1593-1932 |
8.84e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1593 KQAELEKQRQIQVVEEVAKKTAATQLESKQV-ALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETW 1671
Cdd:COG5022 822 LQKTIKREKKLRETEEVEFSLKAEVLIQKFGrSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVN 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1672 RQKANEALRLRLQAEEEANKKTAaqeeaekqkeeakreakkrakaeeaaLKQKEAAEMELGNQRKMAEETAKQKLAAEQE 1751
Cdd:COG5022 902 LELESEIIELKKSLSSDLIENLE--------------------------FKTELIARLKKLLNNIDLEEGPSIEYVKLPE 955
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1752 LIRLRadfehaeQQRTVLDDELQRLKNdvnsAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESE-- 1829
Cdd:COG5022 956 LNKLH-------EVESKLKETSEEYED----LLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPve 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1830 ----AAKMRELAEEATKLRSVAEEaKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKR 1905
Cdd:COG5022 1025 vaelQSASKIISSESTELSILKPL-QKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEV 1103
|
330 340
....*....|....*....|....*..
gi 1207141765 1906 KAEEEGYQRKVLEDQAAQHKQAIEEKI 1932
Cdd:COG5022 1104 TNRNLVKPANVLQFIVAQMIKLNLLQE 1130
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1651-1804 |
9.12e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.31 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1651 KKQQAEADK---AREQAEK-ELEtwRQK-----ANEALR---LRLQAEEEANKKTAaqeeaekqkeeakrEAKKRAKAEE 1718
Cdd:PTZ00491 662 KSQEAAARHqaeLLEQEARgRLE--RQKmhdkaKAEEQRtklLELQAESAAVESSG--------------QSRAEALAEA 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1719 AALKQKEAAEMELGNQRkmaeeTAKQKLAAEQELIRLRadfehaeqQRTVLDDELQRLKNDVnsAVKQKKELEE-ELIKV 1797
Cdd:PTZ00491 726 EARLIEAEAEVEQAELR-----AKALRIEAEAELEKLR--------KRQELELEYEQAQNEL--EIAKAKELADiEATKF 790
|
....*..
gi 1207141765 1798 RKEMEIL 1804
Cdd:PTZ00491 791 ERIVEAL 797
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3381-3419 |
9.52e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.54 E-value: 9.52e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1207141765 3381 YLQGSDCIAGVFFQKTKEKLSIYQAMKQKLLTSDTGMSL 3419
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1651-1748 |
9.70e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 39.76 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141765 1651 KKQQAEADKAREQAEKELETWRQKANEalrLRLQAEEEANKKtaaqeeaekqkeeakrEAKKRAKAEEAALKQKEAAEME 1730
Cdd:PRK05759 48 ERAKKELELAQAKYEAQLAEARAEAAE---IIEQAKKRAAQI----------------IEEAKAEAEAEAARIKAQAQAE 108
|
90
....*....|....*...
gi 1207141765 1731 LGNQRKMAEETAKQKLAA 1748
Cdd:PRK05759 109 IEQERKRAREELRKQVAD 126
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2547-2618 |
9.71e-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: 39.13 E-value: 9.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141765 2547 QFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMN--GKQKEMQDLEKKRIEQEKLLAEE 2618
Cdd:pfam20492 17 QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKErlEESAEMEAEEKEQLEAELAEAQE 90
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