|
Name |
Accession |
Description |
Interval |
E-value |
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
67-183 |
7.99e-72 |
|
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: 236.14 E-value: 7.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 67 DRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRERdvvrsvrlprekGRMRFHKLQNVQIALD 146
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRER------------GRMRFHRLQNVQTALD 68
|
90 100 110
....*....|....*....|....*....|....*..
gi 1927222982 147 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 183
Cdd:cd21188 69 FLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
64-194 |
3.94e-68 |
|
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: 226.06 E-value: 3.94e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 64 DERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRErdvvrsvrlpreKGRMRFHKLQNVQI 143
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE------------KGRMRFHKLQNVQI 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1927222982 144 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQINGQSE 194
Cdd:cd21235 69 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
196-301 |
6.34e-67 |
|
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: 222.20 E-value: 6.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 196 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLD 275
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1927222982 276 PEDVDVPHPDEKSIITYVSSLYDAMP 301
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
56-192 |
3.95e-65 |
|
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: 217.93 E-value: 3.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 56 ERAVIRIADERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRErdvvrsvrlpreKGRMRF 135
Cdd:cd21236 4 ENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPRE------------KGRMRF 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222982 136 HKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQINGQ 192
Cdd:cd21236 72 HRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
197-301 |
9.02e-63 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 209.94 E-value: 9.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 197 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDP 276
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1927222982 277 EDVDVPHPDEKSIITYVSSLYDAMP 301
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
64-193 |
2.60e-58 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 197.95 E-value: 2.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 64 DERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGetlprerdvvrsVRLPREKGRMRFHKLQNVQI 143
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSG------------VKLPREKGRMRFHRLQNVQI 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1927222982 144 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQINGQS 193
Cdd:cd21237 69 ALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
197-301 |
1.55e-57 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 195.21 E-value: 1.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 197 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERdLGVTRLLDP 276
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1927222982 277 EDVDVPHPDEKSIITYVSSLYDAMP 301
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
195-301 |
1.11e-50 |
|
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: 175.62 E-value: 1.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 195 DMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERdLGVTRLL 274
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1927222982 275 DPEDVDVPHPDEKSIITYVSSLYDAMP 301
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
69-184 |
2.43e-47 |
|
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: 166.02 E-value: 2.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 69 VQKKTFTKWVNKHLIKSQRQ-VTDLYEDLRDGHNLISLLEVLSGEtlprerdvvrsvRLPREKGRMRFHKLQNVQIALDF 147
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKPpIKDLFEDLRDGTRLLALLEVLTGK------------KLKPEKGRMRVHHLNNVNRALQV 69
|
90 100 110
....*....|....*....|....*....|....*..
gi 1927222982 148 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 184
Cdd:cd21186 70 LEQNNVKLVNISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
56-180 |
5.91e-47 |
|
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: 165.23 E-value: 5.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 56 ERAVIR-IADERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRErdvvrsvrlprEKGRMR 134
Cdd:cd21246 2 ERSRIKaLADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKP-----------TKGKMR 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1927222982 135 FHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 180
Cdd:cd21246 71 IHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
197-297 |
2.41e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 162.97 E-value: 2.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 197 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDP 276
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1927222982 277 EDVDVPHPDEKSIITYVSSLY 297
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 ... |
197-297 |
5.68e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 156.40 E-value: 5.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 197 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDP 276
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1927222982 277 EDVDVPHPDEKSIITYVSSLY 297
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
65-184 |
2.38e-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: 152.14 E-value: 2.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 65 ERDRVQKKTFTKWVNKHLIKSQR--QVTDLYEDLRDGHNLISLLEVLSGEtlprerdvvrsvRLPREKGRM--RFHKLQN 140
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGE------------KLPCEKGRRlkRVHFLSN 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1927222982 141 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 184
Cdd:cd21241 69 INTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
56-180 |
3.42e-42 |
|
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: 151.68 E-value: 3.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 56 ERAVIR-IADERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRErdvvrsvrlprEKGRMR 134
Cdd:cd21193 2 EKGRIRaLQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKP-----------NRGRLR 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1927222982 135 FHKLQNVQIALDFLkHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 180
Cdd:cd21193 71 VQKIENVNKALAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1383-2625 |
1.53e-41 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 170.01 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1383 TDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELdkqkqlaevHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEkqkhn 1462
Cdd:NF041483 90 ADAERELRDARAQTQRILQEHAEHQARLQAEL---------HTEAVQRRQQLDQELAERRQTVESHVNENVAWAE----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1463 iqlelhELKNLSEQQ---IMDKSKQVDDALQSRVKIEEEirliRLQLETTVKQKSTAES---ELKQLRDRA-AEAEKLRK 1535
Cdd:NF041483 156 ------QLRARTESQarrLLDESRAEAEQALAAARAEAE----RLAEEARQRLGSEAESaraEAEAILRRArKDAERLLN 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1536 AAQEEA-------EKLRKQVNEETQKKRMAEEELKRKAEAEKEaakqkqkalEDLENLKRQAEEAERQVKQAEIEKERQI 1608
Cdd:NF041483 226 AASTQAqeatdhaEQLRSSTAAESDQARRQAAELSRAAEQRMQ---------EAEEALREARAEAEKVVAEAKEAAAKQL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1609 QVAHVA-AQKSAAAELQSKHMsfVEKTSKLEESLKQEHGAVL---QLQHEAAALKKQQEDAERAREEAEKELEKWRQKAN 1684
Cdd:NF041483 297 ASAESAnEQRTRTAKEEIARL--VGEATKEAEALKAEAEQALadaRAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAE 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1685 EALRlrlQAEEEAHKKS-LAQEDAEKQKEEAEREAKK-RAKAEDSALKQKEMAENELERQRkvAESTAQQkltaeQELIR 1762
Cdd:NF041483 375 EVLT---KASEDAKATTrAAAEEAERIRREAEAEADRlRGEAADQAEQLKGAAKDDTKEYR--AKTVELQ-----EEARR 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1763 LRADfdnAEQQRSLLEDELYRLKNE-----VVAAQQQRKQLEDELAKVRSEMDvliQLKSKAEKEtmsnSERSKQLLEVE 1837
Cdd:NF041483 445 LRGE---AEQLRAEAVAEGERIRGEarreaVQQIEEAARTAEELLTKAKADAD---ELRSTATAE----SERVRTEAIER 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1838 ATKMRDLAE--------EASKLRAIAEE-AKHQRQVAEEEAARQRAEAERILKEKLA-AISDATRLKTEAE-------IA 1900
Cdd:NF041483 515 ATTLRRQAEetlertraEAERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEerltaaeEA 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1901 LKEKEAENERLRRQAEDEAYQRKAledqanqhkqQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRIlKLNFE 1980
Cdd:NF041483 595 LADARAEAERIRREAAEETERLRT----------EAAERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAV-RLRSE 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1981 KASsgkldlelELNKLKNIAEETQQsKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLK 2060
Cdd:NF041483 664 AAA--------EAERLKSEAQESAD-RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAR 734
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2061 KKAEE----ARKQKDDADKEAEKQILMA-QQAAQKCSAAEQQvqsvlAQQKEDTImqtklkeeyekakklakqaEAAKEK 2135
Cdd:NF041483 735 EQSEEllasARKRVEEAQAEAQRLVEEAdRRATELVSAAEQT-----AQQVRDSV-------------------AGLQEQ 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2136 AEREAALLRQQAEE-AERQKAaaeqeaanqaKAQEDAERLRKEAEfeaAKRAQAENAALKQKQQADAEMAKHKKLAEQTL 2214
Cdd:NF041483 791 AEEEIAGLRSAAEHaAERTRT----------EAQEEADRVRSDAY---AERERASEDANRLRREAQEETEAAKALAERTV 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2215 KQKFQvEQEltkvKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVK----VQMEELLKLKLRIEEENQRL 2290
Cdd:NF041483 858 SEAIA-EAE----RLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAE 932
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2291 IKKDKDNTQKFLAKEADNMK-KLAEDAARLSVEAQ-EAARLRQIAEDDLNQqraladkmlkekmqAIQEASRLRAEAEml 2368
Cdd:NF041483 933 ARAEAERLRDEARAEAERVRaDAAAQAEQLIAEATgEAERLRAEAAETVGS--------------AQQHAERIRTEAE-- 996
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2369 qRQKDLAQEQAQKLLEDKQLMQQR-LDEETEEYQK--SLEAERKRQLEIIAESEKLKLqvsqLSEAQAKAQEEAKKFKKQ 2445
Cdd:NF041483 997 -RVKAEAAAEAERLRTEAREEADRtLDEARKDANKrrSEAAEQADTLITEAAAEADQL----TAKAQEEALRTTTEAEAQ 1071
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2446 ADSI-------ASRLHETelATQEKMTVVEK--------LEVARLTSS---KEADDLRKAI-ADLEKEKSRLKKEAEDLQ 2506
Cdd:NF041483 1072 ADTMvgaarkeAERIVAE--ATVEGNSLVEKartdadelLVGARRDATairERAEELRDRItGEIEELHERARRESAEQM 1149
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2507 NKSKEMADAQQKQIEHektvlQQTFLSEKEMLLKKEKLIEEEKKRLESqfeeeVKKAKALKDEQERQKQQMEDEKKKLQA 2586
Cdd:NF041483 1150 KSAGERCDALVKAAEE-----QLAEAEAKAKELVSDANSEASKVRIAA-----VKKAEGLLKEAEQKKAELVREAEKIKA 1219
|
1290 1300 1310
....*....|....*....|....*....|....*....
gi 1927222982 2587 TMDAalnkqkEAEKEMHNKQKEMKELERKRleqERILAE 2625
Cdd:NF041483 1220 EAEA------EAKRTVEEGKRELDVLVRRR---EDINAE 1249
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
63-297 |
3.09e-40 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 160.88 E-value: 3.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 63 ADERDRVQKKTFTKWVNKHLIKS-QRQVTDLYEDLRDGHNLISLLEVLSGETLPRERdvvrsvrlprEKGRMRFHKLQNV 141
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYN----------ETPETRIHVMENV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 142 QIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQingQSEDMTAKEKLLLWSQRMTDGYQ-GIRCDN 220
Cdd:COG5069 73 SGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 221 FTTSWRDGKLFNAVIHKHYPRLVDmgrvYRQTNLE------NLEQAFGVAERDLGVTRLLDPEDV-DVPHPDEKSIITYV 293
Cdd:COG5069 150 FFRSWRDGLAFSALIHDSRPDTLD----PNVLDLQkknkalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYV 225
|
....
gi 1927222982 294 SSLY 297
Cdd:COG5069 226 SWYI 229
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
62-180 |
3.89e-40 |
|
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: 146.71 E-value: 3.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 62 IADERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRErdvvrsvrlprEKGRMRFHKLQNV 141
Cdd:cd21318 31 LADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKP-----------TRGRMRIHSLENV 99
|
90 100 110
....*....|....*....|....*....|....*....
gi 1927222982 142 QIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 180
Cdd:cd21318 100 DKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
56-180 |
5.34e-40 |
|
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: 145.97 E-value: 5.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 56 ERAVIR-IADERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRErdvvrsvrlprEKGRMR 134
Cdd:cd21317 17 ERSRIKaLADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKP-----------TKGRMR 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1927222982 135 FHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 180
Cdd:cd21317 86 IHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
193-297 |
1.11e-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: 144.38 E-value: 1.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 193 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTR 272
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1927222982 273 LLDPEDVDVPHPDEKSIITYVSSLY 297
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
931-1008 |
2.27e-39 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 141.97 E-value: 2.27e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 931 LSWQYLMRDYTQIRSWNITMLKTMKPEEYRLVMRNLELHYQDYMRDSQDSQLFGPDDRMQIEEDYTKSTQHFDSLIRS 1008
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
196-301 |
1.43e-38 |
|
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: 140.92 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 196 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLD 275
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1927222982 276 PEDVDVPHPDEKSIITYVSSLYDAMP 301
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
65-184 |
1.53e-38 |
|
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: 141.17 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 65 ERDRVQKKTFTKWVNKHLIK--SQRQVTDLYEDLRDGHNLISLLEVLSGEtlprerdvvrsvRLPREKGRM--RFHKLQN 140
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKlsQPIVINDLFVDIKDGTALLRLLEVLSGQ------------KLPIESGRVlqRAHKLSN 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1927222982 141 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 184
Cdd:cd21190 69 IRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
184-299 |
8.23e-38 |
|
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: 139.03 E-value: 8.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 184 ISDIQIngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGV 263
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1927222982 264 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 299
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
196-297 |
3.99e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 136.92 E-value: 3.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 196 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLD 275
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1927222982 276 PEDVDVPHPDEKSIITYVSSLY 297
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
67-180 |
5.42e-37 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 136.37 E-value: 5.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 67 DRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPrerdvvrsvrlPREKGRMRFHKLQNVQIALD 146
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLP-----------KPERGKMRFHKIANVNKALD 71
|
90 100 110
....*....|....*....|....*....|....
gi 1927222982 147 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 180
Cdd:cd21214 72 FIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1818-2649 |
7.63e-37 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 154.91 E-value: 7.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1818 KAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAI--AEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKT 1895
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKkkAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1896 EAEIALKEKEAENERLRRQAEDeayQRKALEDQANQHKQQIE-----EKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEE 1970
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEaarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1971 EIRIlklnfEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQ 2050
Cdd:PTZ00121 1242 AKKA-----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2051 ---------AAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSvlAQQKEDTImqTKLKEEYEK 2121
Cdd:PTZ00121 1317 adeakkkaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE--AKKKADAA--KKKAEEKKK 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2122 AKKLAKQAEAAKEKAE--REAALLRQQAEEAERQKAAAEQEAANQAKAQE--DAERLRKEAEfeaaKRAQAENAALKQKQ 2197
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADelKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEakKADEAKKKAE----EAKKAEEAKKKAEE 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2198 QADAEMAKHKklAEQTLKQKfQVEQELTKVKLKLDETDKQksvldEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELL 2277
Cdd:PTZ00121 1469 AKKADEAKKK--AEEAKKAD-EAKKKAEEAKKKADEAKKA-----AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2278 KlklriEEEnqrliKKDKDNTQKflakeADNMKKLAEdaARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQE 2357
Cdd:PTZ00121 1541 K-----AEE-----KKKADELKK-----AEELKKAEE--KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2358 ASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEII-AESEKLKLQVSQLSEAQAKAQ 2436
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkAAEEAKKAEEDKKKAEEAKKA 1683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2437 EEAKkfKKQADSIASRLHETELATQEKMTVVEklEVARLTSSKEADDLRKAIAD-LEKEKSRLKKEAEDLQNKSKEMADA 2515
Cdd:PTZ00121 1684 EEDE--KKAAEALKKEAEEAKKAEELKKKEAE--EKKKAEELKKAEEENKIKAEeAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2516 QQKQIEHEKTVlqQTFLSEKEMLLKKEKLIEEEKKRLESQfeeevKKAKALKDEQE--------------RQKQQMEDEK 2581
Cdd:PTZ00121 1760 AHLKKEEEKKA--EEIRKEKEAVIEEELDEEDEKRRMEVD-----KKIKDIFDNFAniieggkegnlvinDSKEMEDSAI 1832
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2582 KKLQATMDAALNKQKEAEKEMHNKQKEMKELERKR--LEQERILAEENQKLREKLQQLEEAQKDQPDKEV 2649
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEadFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
69-182 |
2.79e-36 |
|
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: 134.45 E-value: 2.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 69 VQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRERdvvrsvrlprEKGRMRFHKLQNVQIALDFL 148
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYN----------KNPKMRVQKLENVNKALEFI 73
|
90 100 110
....*....|....*....|....*....|....
gi 1927222982 149 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 182
Cdd:cd21215 74 KSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
193-297 |
5.73e-36 |
|
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: 134.03 E-value: 5.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 193 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTR 272
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1927222982 273 LLDPEDVDVPHPDEKSIITYVSSLY 297
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
65-184 |
9.14e-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: 133.03 E-value: 9.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 65 ERDRVQKKTFTKWVNKHLIKSQ--RQVTDLYEDLRDGHNLISLLEVLSGEtlprerdvvrsvRLPREKGRMRFHKLQNVQ 142
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQ------------QLPREKGHNVFQCRSNIE 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1927222982 143 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 184
Cdd:cd21242 69 TALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1383-2310 |
5.14e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 149.14 E-value: 5.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1383 TDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEkeaqelKLRMQEEVNRREDAVVDAEKQKHN 1462
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAE------EARKAEDARKAEEARKAEDAKRVE 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1463 IQLELHELKNLSEQQIMDKSKQVDDALQS-RVKIEEEIRlirlqlettvKQKSTAESELKQLRDRAAEAEKLRKAAQE-E 1540
Cdd:PTZ00121 1156 IARKAEDARKAEEARKAEDAKKAEAARKAeEVRKAEELR----------KAEDARKAEAARKAEEERKAEEARKAEDAkK 1225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1541 AEKLRKQvnEETQKKrmaEEELKRKAEAEKEAAKQKQKALEDLENLKRQ----AEEAERQVKQAEIEKERQIQVAHVAAQ 1616
Cdd:PTZ00121 1226 AEAVKKA--EEAKKD---AEEAKKAEEERNNEEIRKFEEARMAHFARRQaaikAEEARKADELKKAEEKKKADEAKKAEE 1300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1617 KSAAAELQSKhmsfVEKTSKLEESLKQEHgavlQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANealrlrlQAEEE 1696
Cdd:PTZ00121 1301 KKKADEAKKK----AEEAKKADEAKKKAE----EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE-------AAEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1697 AHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRlRADFDNAEQQRSL 1776
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEEAK 1444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1777 LEDELYRLKNEVVAAQQQRKQLE-----DELAKVRSEMDVLIQLKSKAEKETMSNSERSKqlleveATKMRDLAEEASKl 1851
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEeakkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKK------AAEAKKKADEAKK- 1517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1852 raiAEEAKHQRQVAEEEAARQRAEAerilkEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQ 1931
Cdd:PTZ00121 1518 ---AEEAKKADEAKKAEEAKKADEA-----KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1932 HKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRV-VEEEIRilklnfEKASSGKLDLELELNKLKNIAEETQQSKLRA 2010
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkKAEEEK------KKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2011 EEEAEKLRKLALEEEKRRREAEEKVKKiaaaeEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQK 2090
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDEKKA-----AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2091 CSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAA-KEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQE 2169
Cdd:PTZ00121 1739 AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAViEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGN 1818
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2170 DAERLRKEAEFEAAKraQAENAALKQKQQADaEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLK 2249
Cdd:PTZ00121 1819 LVINDSKEMEDSAIK--EVADSKNMQLEEAD-AFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDK 1895
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 2250 DEVDDAVKQRGQVEE--ELLKVKVQMEELLKLKlrIEEENQRLIKKDKDN--TQKFLAKEADNMK 2310
Cdd:PTZ00121 1896 DDIEREIPNNNMAGKnnDIIDDKLDKDEYIKRD--AEETREEIIKISKKDmcINDFSSKFCDYMK 1958
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
181-297 |
1.42e-34 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 130.56 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 181 HFQISDIQINGQSEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQA 260
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1927222982 261 FGVAERDLGVTRLLDPEDVDVPHPDEKSIITYVSSLY 297
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
200-301 |
4.15e-34 |
|
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: 128.31 E-value: 4.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 200 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED 278
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1927222982 279 VDVPHPDEKSIITYVSSLYDAMP 301
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1904-2679 |
9.89e-34 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 144.90 E-value: 9.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1904 KEAENERLRRQAEDEAYQ--RKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVE----EEIRILKL 1977
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEeaFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEarkaEDAKRVEI 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1978 NFEKASSGKLDLELELNKLKNIAEETQQSKLRaeeEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELD 2057
Cdd:PTZ00121 1157 ARKAEDARKAEEARKAEDAKKAEAARKAEEVR---KAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2058 RLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSvlaQQKEDTIMQTKLKEEYEKAKKL--AKQAEAAKEK 2135
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE---ARKADELKKAEEKKKADEAKKAeeKKKADEAKKK 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2136 AE--REAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQt 2213
Cdd:PTZ00121 1311 AEeaKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE- 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2214 lkqkfqveqeltkvKLKLDETDKQKsvldEELQRLKDEVDDAVKQRGQVEEellkVKVQMEEllklKLRIEEENQRLIKK 2293
Cdd:PTZ00121 1390 --------------KKKADEAKKKA----EEDKKKADELKKAAAAKKKADE----AKKKAEE----KKKADEAKKKAEEA 1443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2294 DKDNTQKFLAKEadnmKKLAEDAARLSVEAQEAARLRQIAEddlnqQRALADKMLKEKMQAIQEASRLRAEAEMLQRQkd 2373
Cdd:PTZ00121 1444 KKADEAKKKAEE----AKKAEEAKKKAEEAKKADEAKKKAE-----EAKKADEAKKKAEEAKKKADEAKKAAEAKKKA-- 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2374 laqEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRL 2453
Cdd:PTZ00121 1513 ---DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2454 HETELatQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLS 2533
Cdd:PTZ00121 1590 EEARI--EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2534 EKEmllkkeklieeekkrlesqfEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELE 2613
Cdd:PTZ00121 1668 KKA--------------------EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 2614 RK-RLEQERILAEENQKlreklqQLEEAQKDQPDK-EVIHVTMVETTKNVYNGQNVGDVVDSAEKKPD 2679
Cdd:PTZ00121 1728 NKiKAEEAKKEAEEDKK------KAEEAKKDEEEKkKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
197-297 |
2.50e-33 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 125.98 E-value: 2.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 197 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDP 276
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1927222982 277 EDVDVPHPDEKSIITYVSSLY 297
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
56-180 |
7.63e-33 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 126.70 E-value: 7.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 56 ERAVIR-IADERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRErdvvrsvrlprEKGRMR 134
Cdd:cd21316 39 ERSRIKaLADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKP-----------TKGRMR 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1927222982 135 FHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 180
Cdd:cd21316 108 IHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
64-184 |
3.18e-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: 3.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 64 DERDRVQKKTFTKWVNKHLIKSQRQ-VTDLYEDLRDGHNLISLLEVLSGEtlprerdvvrsvRLPREKGRMRFHKLQNVQ 142
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKPpIEDLFTDLQDGRRLLELLEGLTGQ------------KLVKEKGSTRVHALNNVN 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1927222982 143 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 184
Cdd:cd21231 69 KALQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1534-2399 |
3.30e-32 |
|
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: 139.04 E-value: 3.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1534 RKAAQEEA---EKLRKQVNEETQKKRMAEEELKRkaeaekeaakqkqkaLED--------LENLKRQAEEAER--QVKQA 1600
Cdd:TIGR02168 157 RRAIFEEAagiSKYKERRKETERKLERTRENLDR---------------LEDilnelerqLKSLERQAEKAERykELKAE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1601 EIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWR 1680
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1681 QKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQEL 1760
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1761 IRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDvliqlkSKAEKETMSNSERSKQLLEVEATK 1840
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE------EAELKELQAELEELEEELEELQEE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1841 MRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAErILKEKLAAISDATRlktEAEIALKEKEAEN-------ERLRR 1913
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLD-SLERLQENLEGFSE---GVKALLKNQSGLSgilgvlsELISV 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1914 QAEDEAYQRKALEDQANQ----HKQQIEEKIVLLKKSS-------EAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKA 1982
Cdd:TIGR02168 532 DEGYEAAIEAALGGRLQAvvveNLNAAKKAIAFLKQNElgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFD 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1983 SSGKLDLELELNKL---KNIAEETQQSKLRAEEE-------------------AEKLRKLALEEEKRRREAEEKVKKIAA 2040
Cdd:TIGR02168 612 PKLRKALSYLLGGVlvvDDLDNALELAKKLRPGYrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEE 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2041 AEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYE 2120
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2121 KAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKaaaeqeaanqAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQAD 2200
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREAL----------DELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2201 AEMAKHKKLAEQTLK---QKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKvqmEELL 2277
Cdd:TIGR02168 842 DLEEQIEELSEDIESlaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR---RELE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2278 KLKLRIEEENQRLikkdkdntQKFLAKEADNMKKLAEDAarlSVEAQEAARLRQIAEDDLNQQRALADKmLKEK------ 2351
Cdd:TIGR02168 919 ELREKLAQLELRL--------EGLEVRIDNLQERLSEEY---SLTLEEAEALENKIEDDEEEARRRLKR-LENKikelgp 986
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2352 --MQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEdkqlMQQRLDEETEE 2399
Cdd:TIGR02168 987 vnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE----AIEEIDREARE 1032
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1514-2403 |
1.20e-31 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 137.96 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1514 STAESELKQLRD-RAAEAEKLRKAAQEEAEKLRKQVNEETQKKrmaEEELKRKAEAEKEAAKQKQKALEDLENlKRQAEE 1592
Cdd:PTZ00121 1075 SYKDFDFDAKEDnRADEATEEAFGKAEEAKKTETGKAEEARKA---EEAKKKAEDARKAEEARKAEDARKAEE-ARKAED 1150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1593 AERQVKQAEIEKERQIQVAHVAAQ-KSAAAELQSKHMSFVEKTSKLEESLKQEhgavlqlqheaAALKKQQEdaeraree 1671
Cdd:PTZ00121 1151 AKRVEIARKAEDARKAEEARKAEDaKKAEAARKAEEVRKAEELRKAEDARKAE-----------AARKAEEE-------- 1211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1672 aekelekwrQKANEALRLRLQAEEEAHKKSlaqEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQ 1751
Cdd:PTZ00121 1212 ---------RKAEEARKAEDAKKAEAVKKA---EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK 1279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1752 QKLTAEQELIRLRADFDNAEQQRSLleDELYRLKNEVVAAQQQRKQLE------DELAKVRSEMDVLIQLKSKAEKETMS 1825
Cdd:PTZ00121 1280 ADELKKAEEKKKADEAKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEeakkkaDAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1826 NSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQvAEEEAARQRAEAERiLKEKLAAISDATRLKTEAEIALKEKE 1905
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE-AKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEEKKKADE 1435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1906 AENERLRRQAEDEAYQRKALEDQANQHKQQIEEKivllKKSSEAEMERQRAIVDDTLKQRrvvEEEIRILKLNFEKASSG 1985
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA----KKADEAKKKAEEAKKADEAKKK---AEEAKKKADEAKKAAEA 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1986 KLDLElelnKLKNIAEETQQSKLRAEEEAEKLRKLaleeekrrrEAEEKVKKiaaaeeeaarqrqaaQDELDRLK--KKA 2063
Cdd:PTZ00121 1509 KKKAD----EAKKAEEAKKADEAKKAEEAKKADEA---------KKAEEKKK---------------ADELKKAEelKKA 1560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2064 EEARKqKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALL 2143
Cdd:PTZ00121 1561 EEKKK-AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2144 RQQAEEAER-------QKAAAEQEAANQAKAQED---AERLRKEaefEAAKRAQAENAALKQKQQADAEMAKHKKLAEQT 2213
Cdd:PTZ00121 1640 KKEAEEKKKaeelkkaEEENKIKAAEEAKKAEEDkkkAEEAKKA---EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2214 LKQKFQVEQELTKVKL----KLDETDKQKSvldEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQR 2289
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAeeakKEAEEDKKKA---EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2290 L-----IKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAArlrqiaeDDLNQQRALADKMLKEKMQAIQEASRLRAE 2364
Cdd:PTZ00121 1794 MevdkkIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVA-------DSKNMQLEEADAFEKHKFNKNNENGEDGNK 1866
|
890 900 910
....*....|....*....|....*....|....*....
gi 1927222982 2365 AEMLQRQKDLAQEQAQKLLEDKqlMQQRLDEETEEYQKS 2403
Cdd:PTZ00121 1867 EADFNKEKDLKEDDEEEIEEAD--EIEKIDKDDIEREIP 1903
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
69-184 |
6.58e-31 |
|
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: 119.31 E-value: 6.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 69 VQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRerdvvrSVRLPRekgrMRFHKLQNVQIALDFL 148
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGR------VIKKPL----NQHQKLENVTLALKAM 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 1927222982 149 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 184
Cdd:cd21227 74 AEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
196-294 |
7.32e-31 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 119.07 E-value: 7.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 196 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLD 275
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1927222982 276 PEDVDVPHPDEKSIITYVS 294
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
200-302 |
1.73e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 118.11 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 200 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTN-LENLEQAFGVAERDLGVTRLLDPE 277
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1927222982 278 DVDVPHPDEKSIITYVSSLYDAMPR 302
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
196-294 |
4.04e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 116.86 E-value: 4.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 196 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLD 275
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1927222982 276 PEDVDVPHPDEKSIITYVS 294
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1359-2149 |
4.08e-30 |
|
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: 132.49 E-value: 4.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1359 QEYVTLRTKYSEL-MTLTSQYIKFITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELdkqkqlaEVHAKAIAKAEKEAQE 1437
Cdd:TIGR02168 213 ERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL-------EELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1438 LklrmQEEVNRREDAVVDAEKQKHNIQLELHELknlsEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAE 1517
Cdd:TIGR02168 286 L----QKELYALANEISRLEQQKQILRERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1518 SELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQV 1597
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1598 KQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEH-------------GAVLQLQHEAAALKKQQED 1664
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAqlqarldslerlqENLEGFSEGVKALLKNQSG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1665 AERAREEAEKEL---EKWRQKANEALRLRLQAeeeahkksLAQEDAEKQKEEAEreakkrakaedsALKQKE-----MAE 1736
Cdd:TIGR02168 518 LSGILGVLSELIsvdEGYEAAIEAALGGRLQA--------VVVENLNAAKKAIA------------FLKQNElgrvtFLP 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1737 NELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLK--NEVVAAQQQRKQLEDELAKVRSEMDVLIQ 1814
Cdd:TIGR02168 578 LDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIVTLDGDLVRP 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1815 ---LKSKAEKETMSNSERSKQLLEVEAtKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDAT 1891
Cdd:TIGR02168 658 ggvITGGSAKTNSSILERRREIEELEE-KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1892 RLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEdQANQHKQQIEEKIVLLkkssEAEMERQRAIVDDTLKQRRVVEEE 1971
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEEL----EAQIEQLKEELKALREALDELRAE 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1972 IRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQA 2051
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2052 AQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMqtklkeEYEKAKKLAKQAEA 2131
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL------TLEEAEALENKIED 965
|
810
....*....|....*...
gi 1927222982 2132 AKEKAEREAALLRQQAEE 2149
Cdd:TIGR02168 966 DEEEARRRLKRLENKIKE 983
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
65-186 |
8.39e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 116.14 E-value: 8.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 65 ERDRVQKKTFTKWVNKHLIKSQR--QVTDLYEDLRDGHNLISLLEVLSGETLPRERdvvrsvrlprEKGRMRFHKLQNVQ 142
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEY----------KPSSHRIFRLNNIA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1927222982 143 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 186
Cdd:cd21191 71 KALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
184-299 |
1.19e-29 |
|
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: 115.70 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 184 ISDIQingqSEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGV 263
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1927222982 264 AERDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLYDA 299
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1386-1938 |
1.28e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 130.44 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1386 QRRLEDEEKAAEKLKAEEqkkmammqAELDKQKQLAEvhaKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQL 1465
Cdd:COG1196 238 EAELEELEAELEELEAEL--------EELEAELAELE---AELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1466 ELHELKNLSEQQimdkskqvDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLR 1545
Cdd:COG1196 307 LEERRRELEERL--------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1546 KQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQvaHVAAQKSAAAELQS 1625
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE--ALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1626 KHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRL-QAEEEAHKKSLAQ 1704
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLaGAVAVLIGVEAAY 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1705 EDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDEL--Y 1782
Cdd:COG1196 537 EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAryY 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1783 RLKNEVV----------AAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETmsnsERSKQLLEVEATKMRDLAEEASKLR 1852
Cdd:COG1196 617 VLGDTLLgrtlvaarleAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR----RELLAALLEAEAELEELAERLAEEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1853 AIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQH 1932
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
....*.
gi 1927222982 1933 KQQIEE 1938
Cdd:COG1196 773 EREIEA 778
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
68-182 |
2.17e-29 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 114.89 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 68 RVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRERDvvrsvrlprEKGRMRFHKLQNVQIALDF 147
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYN---------RRPAFQQHYLENVSTALKF 73
|
90 100 110
....*....|....*....|....*....|....*
gi 1927222982 148 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 182
Cdd:cd21183 74 IEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
68-185 |
2.39e-29 |
|
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: 115.24 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 68 RVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRErdvvrsvrlpREKGRMRFHKLQNVQIALDF 147
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKF----------NKRPTFRSQKLENVSVALKF 83
|
90 100 110
....*....|....*....|....*....|....*....
gi 1927222982 148 LKHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 185
Cdd:cd21311 84 LEEDEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1525-2525 |
4.15e-29 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 129.18 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1525 DRAAEAEKLRKAAQEEAEKLRKqvneetqkkrmaeeelkrkaeaekeaakqkqkaledlenlkrqaeEAERQVKQAEIEK 1604
Cdd:NF041483 69 DIGYQAEQLLRNAQIQADQLRA---------------------------------------------DAERELRDARAQT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1605 ERQIQvAHVAAQKSAAAELqskHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQqeDAERAREEAEKELEKWRQKAN 1684
Cdd:NF041483 104 QRILQ-EHAEHQARLQAEL---HTEAVQRRQQLDQELAERRQTVESHVNENVAWAEQ--LRARTESQARRLLDESRAEAE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1685 EALrlrlqAEEEAHKKSLAQEDAEKQKEEAEreaKKRAKAEDSALKQKEMAENELErqrkvAESTAQQKLTAEQELIR-- 1762
Cdd:NF041483 178 QAL-----AAARAEAERLAEEARQRLGSEAE---SARAEAEAILRRARKDAERLLN-----AASTQAQEATDHAEQLRss 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1763 LRADFDNAEQQRSlledELYRlknevvAAQQQRKQLEDELAKVRSEMD-VLIQLKSKAEKETMS----NSERSKQL---- 1833
Cdd:NF041483 245 TAAESDQARRQAA----ELSR------AAEQRMQEAEEALREARAEAEkVVAEAKEAAAKQLASaesaNEQRTRTAkeei 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1834 --LEVEATKMRD-LAEEASKLRA---------IAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKT-----E 1896
Cdd:NF041483 315 arLVGEATKEAEaLKAEAEQALAdaraeaeklVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTraaaeE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1897 AEIALKEKEAENERLRRQAEDEAYQRK--ALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDtlkqRRVVEEEIRI 1974
Cdd:NF041483 395 AERIRREAEAEADRLRGEAADQAEQLKgaAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEG----ERIRGEARRE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1975 LKLNFEKASSGKLDLeleLNKLKNIAEETQQSklrAEEEAEKLRKLALEEEKRRREAEEkvkkiaaaeeeaarqrqaaqd 2054
Cdd:NF041483 471 AVQQIEEAARTAEEL---LTKAKADADELRST---ATAESERVRTEAIERATTLRRQAE--------------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2055 elDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSaaEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEA-AK 2133
Cdd:NF041483 524 --ETLERTRAEAERLRAEAEEQAEEVRAAAERAARELR--EETERAIAARQAEAAEELTRLHTEAEERLTAAEEALAdAR 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2134 EKAEReaaLLRQQAEEAERQKAAAEQEAAN-QAKAQEDAERLRKEAEFEA-AKRAQAENAALKQKQQADAEMAKHKKLAE 2211
Cdd:NF041483 600 AEAER---IRREAAEETERLRTEAAERIRTlQAQAEQEAERLRTEAAADAsAARAEGENVAVRLRSEAAAEAERLKSEAQ 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2212 QTlKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELL-KLKLRIEE---EN 2287
Cdd:NF041483 677 ES-ADRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLaSARKRVEEaqaEA 755
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2288 QRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQE------------AARLRQIAEDDLNQQRALAdkmLKEKMQAI 2355
Cdd:NF041483 756 QRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEEeiaglrsaaehaAERTRTEAQEEADRVRSDA---YAERERAS 832
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2356 QEASRLRAEAemlQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKrqlEIIAESEKlklqvsQLSEAQAKA 2435
Cdd:NF041483 833 EDANRLRREA---QEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEAS---DTLASAEQ------DAARTRADA 900
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2436 QEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTS--SKEADDLR--------KAIADLEKEKSRLKKEAEDL 2505
Cdd:NF041483 901 REDANRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDeaRAEAERVRadaaaqaeQLIAEATGEAERLRAEAAET 980
|
1050 1060
....*....|....*....|
gi 1927222982 2506 QNKSKEMADAQQKQIEHEKT 2525
Cdd:NF041483 981 VGSAQQHAERIRTEAERVKA 1000
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
69-184 |
4.45e-29 |
|
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: 113.95 E-value: 4.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 69 VQKKTFTKWVNKHLIKSQR-QVTDLYEDLRDGHNLISLLEVLSGETLPRERdvvrsvrlprekGRMRFHKLQNVQIALDF 147
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKER------------GSTRVHALNNVNRVLQV 69
|
90 100 110
....*....|....*....|....*....|....*..
gi 1927222982 148 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 184
Cdd:cd21232 70 LHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1394-2276 |
9.25e-29 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 128.02 E-value: 9.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1394 KAAEKLKAEEQKKMAMMQAELDK---------QKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVD-AEKQKHNI 1463
Cdd:NF041483 323 KEAEALKAEAEQALADARAEAEKlvaeaaekaRTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEeAERIRREA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1464 QLELHELKNLSEQQIMD-KSKQVDDALQSR---VKIEEEIRLIRLQLET-------------------TVKQ----KSTA 1516
Cdd:NF041483 403 EAEADRLRGEAADQAEQlKGAAKDDTKEYRaktVELQEEARRLRGEAEQlraeavaegerirgearreAVQQieeaARTA 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1517 ESELKQLRDRA--------AEAEKLRKAAQEEAEKLRKQVnEETQKKRMAEEELKRKAEAekeaakqkqkalEDLENLKR 1588
Cdd:NF041483 483 EELLTKAKADAdelrstatAESERVRTEAIERATTLRRQA-EETLERTRAEAERLRAEAE------------EQAEEVRA 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1589 QAEEAERQVKQaeiEKERQIQvahvAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERA 1668
Cdd:NF041483 550 AAERAARELRE---ETERAIA----ARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLRTEAAE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1669 -----REEAEKELEKWRQKA------------NEALRLRLQAEEEAHK-KSLAQEDAEKQKEE----AER----EAKKRA 1722
Cdd:NF041483 623 rirtlQAQAEQEAERLRTEAaadasaaraegeNVAVRLRSEAAAEAERlKSEAQESADRVRAEaaaaAERvgteAAEALA 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1723 KAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELI---RLRADFDNAEQQRsLLEDELYRLKNEVVAAQQQRKQLE 1799
Cdd:NF041483 703 AAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasaRKRVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVR 781
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1800 DELAKVRSEMDVLIQ-LKSKAEKEtmsnSERSKQLLEVEATKMRDLAeEASKLRAiAEEAKHQRQVAEEEAARQRAEAER 1878
Cdd:NF041483 782 DSVAGLQEQAEEEIAgLRSAAEHA----AERTRTEAQEEADRVRSDA-YAERERA-SEDANRLRREAQEETEAAKALAER 855
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1879 ILKEKLA--------AISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAleDQANQHKQQIEEkivllkKSSEAE 1950
Cdd:NF041483 856 TVSEAIAeaerlrsdASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRS--DAAAQADRLIGE------ATSEAE 927
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1951 MERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSklrAEEEAEKLRKLALEEEKRRRE 2030
Cdd:NF041483 928 RLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGS---AQQHAERIRTEAERVKAEAAA 1004
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2031 AEEKVKKiAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSA-AEQQVQSVL--AQQKE 2107
Cdd:NF041483 1005 EAERLRT-EAREEADRTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTeAEAQADTMVgaARKEA 1083
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2108 DTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAeRQKAAAEQEAANQAKAQEDAERLRKEAE-----FEA 2182
Cdd:NF041483 1084 ERIVAEATVEGNSLVEKARTDADELLVGARRDATAIRERAEEL-RDRITGEIEELHERARRESAEQMKSAGErcdalVKA 1162
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2183 AKRAQAENAALKQKQQADAEMAKHK------KLAEQTLKQKFQVEQELTKvklkldETDKQKSVLDEELQRL----KDEV 2252
Cdd:NF041483 1163 AEEQLAEAEAKAKELVSDANSEASKvriaavKKAEGLLKEAEQKKAELVR------EAEKIKAEAEAEAKRTveegKREL 1236
|
970 980
....*....|....*....|....
gi 1927222982 2253 DDAVKQRGQVEEELLKVKVQMEEL 2276
Cdd:NF041483 1237 DVLVRRREDINAEISRVQDVLEAL 1260
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
200-301 |
1.67e-28 |
|
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: 112.36 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 200 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED 278
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1927222982 279 VDVPHPDEKSIITYVSSLYDAMP 301
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
202-297 |
1.93e-28 |
|
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: 112.06 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 202 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED-VD 280
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1927222982 281 VPHPDEKSIITYVSSLY 297
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1400-2019 |
2.97e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.82 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1400 KAEEQKKMAMMQAELDK--------QKQLAEVHAKAiAKAEKeAQELKLRMQE---EVNRREDAVVDAEKQKHNIQLELH 1468
Cdd:COG1196 174 KEEAERKLEATEENLERledilgelERQLEPLERQA-EKAER-YRELKEELKEleaELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1469 ELKNLSEQ-QIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQ 1547
Cdd:COG1196 252 EAELEELEaELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1548 VNEETQKKRMAEEELKRKAEAekeaakqkqkaLEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELqskh 1627
Cdd:COG1196 332 LEELEEELEELEEELEEAEEE-----------LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA---- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1628 msfvEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDA 1707
Cdd:COG1196 397 ----ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1708 EKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEqQRSLLEDELYRLKNE 1787
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY-EAALEAALAAALQNI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1788 VVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAE- 1866
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAr 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1867 -EEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKK 1945
Cdd:COG1196 632 lEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1946 sSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKAssgkLDLELELNKLKNIAEETQQSK---------------LRA 2010
Cdd:COG1196 712 -AEEERLEEELEEEALEEQLEAEREELLEELLEEEEL----LEEEALEELPEPPDLEELERElerlereiealgpvnLLA 786
|
....*....
gi 1927222982 2011 EEEAEKLRK 2019
Cdd:COG1196 787 IEEYEELEE 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1827-2502 |
3.47e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.82 E-value: 3.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1827 SERSKQL--LEVEATKmrdlAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAisdaTRLKTEAEIALKEK 1904
Cdd:COG1196 196 GELERQLepLERQAEK----AERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEA----ELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1905 EAENERLRRQAEDEAYQRK-ALEDQANQHKQQIEEKI-VLLKKSSEAEMERQRAivddtlkqrrvvEEEIRILKLNFEKA 1982
Cdd:COG1196 268 ELEELRLELEELELELEEAqAEEYELLAELARLEQDIaRLEERRRELEERLEEL------------EEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1983 SSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKK 2062
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2063 AEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAAL 2142
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2143 LRQQAEEAE---RQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAqAENAALKQKQQADAEMAKHKKLAEQTLKQKFQ 2219
Cdd:COG1196 496 LLEAEADYEgflEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA-ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2220 VEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKL-RIEEENQRLIKKDKDNT 2298
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALrRAVTLAGRLREVTLEGE 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2299 QKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQ 2378
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2379 AQklLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKlKLQ----VSQLSEAQAKAQEEAKKFkkqadsiasrlh 2454
Cdd:COG1196 735 EE--LLEELLEEEELLEEEALEELPEPPDLEELERELERLER-EIEalgpVNLLAIEEYEELEERYDF------------ 799
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1927222982 2455 eteLATQekmtvVEKLEVARltsskeaDDLRKAIADLEKEKSRLKKEA 2502
Cdd:COG1196 800 ---LSEQ-----REDLEEAR-------ETLEEAIEEIDRETRERFLET 832
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1543-2259 |
5.17e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.05 E-value: 5.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1543 KLRKqvnEETQKK-RMAEEELKRkaeaekeaakqkqkaLED--------LENLKRQAEEAERQVKQAEIEKERQIQV--- 1610
Cdd:COG1196 171 KERK---EEAERKlEATEENLER---------------LEDilgelerqLEPLERQAEKAERYRELKEELKELEAELlll 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1611 ------AHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKAN 1684
Cdd:COG1196 233 klreleAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1685 EALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLR 1764
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1765 ADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDvliqlkskaeketmsnsERSKQLLEVEATKMRDL 1844
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE-----------------EEEEALEEAAEEEAELE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1845 AEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKA 1924
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1925 LEDqanqhkqqieekivllkkssEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSgkldlELELNKLKNIAEETQ 2004
Cdd:COG1196 536 YEA--------------------ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT-----FLPLDKIRARAALAA 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2005 QSKLRAEEEAEKLRKLALEEEKRRREAEEKVkkiaaaeeeaarqRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMA 2084
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDT-------------LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2085 QQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQ 2164
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2165 AKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKK---LAeqtlkqkfqvEQELTKVKLKLDETDKQKSVL 2241
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnlLA----------IEEYEELEERYDFLSEQREDL 807
|
730 740
....*....|....*....|.
gi 1927222982 2242 DEELQRLKD---EVDDAVKQR 2259
Cdd:COG1196 808 EEARETLEEaieEIDRETRER 828
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1867-2647 |
5.55e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 125.17 E-value: 5.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1867 EEAA------RQRAEAERilkeKLAAISDA-TRLkteaEIALKEKEAENERLRRQAEdEAYQRKALEDQANQHKQQIeek 1939
Cdd:TIGR02168 162 EEAAgiskykERRKETER----KLERTRENlDRL----EDILNELERQLKSLERQAE-KAERYKELKAELRELELAL--- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1940 IVLLKKSSEAEMERQRAIVDDTLKQRR-------VVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEE 2012
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEeltaelqELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2013 EAEKLRKlaleeekrrreaeeKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCS 2092
Cdd:TIGR02168 310 RLANLER--------------QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2093 AAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAE 2172
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2173 RLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQE----LTKVKLKLD----------ETDKQK 2238
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEgvkaLLKNQSGLSgilgvlseliSVDEGY 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2239 S-----VLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLA 2313
Cdd:TIGR02168 536 EaaieaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLR 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2314 ----------------EDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAI---QEASRLRAEAEMLQRQKDL 2374
Cdd:TIGR02168 616 kalsyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILerrREIEELEEKIEELEEKIAE 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2375 AQEQAQKLLEDkqlmQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLH 2454
Cdd:TIGR02168 696 LEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2455 ETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKsKEMADAQQKQIEHEKTVLQQTfLSE 2534
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-LESLERRIAATERRLEDLEEQ-IEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2535 KEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELER 2614
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1927222982 2615 K--RLEQER-----ILAEENQKLREKLQQLEEAQKDQPDK 2647
Cdd:TIGR02168 930 RleGLEVRIdnlqeRLSEEYSLTLEEAEALENKIEDDEEE 969
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1708-2399 |
9.78e-28 |
|
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: 9.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1708 EKQKEEAEREAKK----RAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYR 1783
Cdd:COG1196 199 ERQLEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1784 LKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEketmsnsERSKQLLEVEATKMRDLAEEASKLRAIAEEakhqrq 1863
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELE-------ERLEELEEELAELEEELEELEEELEELEEE------ 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1864 vaEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEkivll 1943
Cdd:COG1196 346 --LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER----- 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1944 KKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALE 2023
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2024 EEKRRREAEEKVKKiaAAEEEAARQRQAAQDELDRLKKKAEEARkqkddadkEAEKQILMAQQAAQKCSAAEQQVqsvla 2103
Cdd:COG1196 499 AEADYEGFLEGVKA--ALLLAGLRGLAGAVAVLIGVEAAYEAAL--------EAALAAALQNIVVEDDEVAAAAI----- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2104 qqkedtimqtklkeEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAErqkaaaeqeaanqakaqEDAERLRKEAEFEAA 2183
Cdd:COG1196 564 --------------EYLKAAKAGRATFLPLDKIRARAALAAALARGAI-----------------GAAVDLVASDLREAD 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2184 KRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVE 2263
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2264 EELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAArlrqIAEDDLNQQRAL 2343
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL----PEPPDLEELERE 768
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 2344 ADKmLKEKMQ--------AIQEASRLRAEAEMLQRQK-DLaqEQAQKLLEDkqlMQQRLDEETEE 2399
Cdd:COG1196 769 LER-LEREIEalgpvnllAIEEYEELEERYDFLSEQReDL--EEARETLEE---AIEEIDRETRE 827
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1705-2632 |
3.08e-27 |
|
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: 122.77 E-value: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1705 EDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRaDFDNAEQQRSLLEDELYRL 1784
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALE-YYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1785 KNEVVaaQQQRKQLEDELAKVRSEMDVLIQLKSKAEKEtmsnSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQV 1864
Cdd:pfam02463 231 YLKLN--EERIDLLQELLRDEQEEIESSKQEIEKEEEK----LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1865 AEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEaENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLK 1944
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELK-ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1945 KSSEAEMERQRaivddtlKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEE 2024
Cdd:pfam02463 384 ERLSSAAKLKE-------EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2025 EKRRREAEEKVKKIAAAEEeaarqrqaaqdeldrLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQ 2104
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLK---------------ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2105 QKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEaak 2184
Cdd:pfam02463 522 GRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE--- 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2185 RAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEE 2264
Cdd:pfam02463 599 IDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEI 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2265 ELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKfLAKEADNMKklaedaarlsveaqeaARLRQIAEDDLNQQRALA 2344
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIKKKEQREKEELKK-LKLEAEELL----------------ADRVQEAQDKINEELKLL 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2345 DKMLKEKMQAIQEASRLRAEAEMLQRQkdlaQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQ 2424
Cdd:pfam02463 742 KQKIDEEEEEEEKSRLKKEEKEEEKSE----LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2425 VSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAED 2504
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE 897
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2505 LQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKL 2584
Cdd:pfam02463 898 EKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNL 977
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 1927222982 2585 QATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQErilaEENQKLRE 2632
Cdd:pfam02463 978 MAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIE----ETCQRLKE 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1430-2259 |
9.43e-27 |
|
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: 121.32 E-value: 9.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1430 KAEKEAQELKL-RMQEEVNRREDAVVDAEKQKHNIQL------ELHELKN-LSEQQIMDKSKQVDDALQSRVKIEEEIRL 1501
Cdd:TIGR02168 171 KERRKETERKLeRTRENLDRLEDILNELERQLKSLERqaekaeRYKELKAeLRELELALLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1502 IRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAkqkqkalE 1581
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE-------A 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1582 DLENLKRQAEEAERQVkqAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQ 1661
Cdd:TIGR02168 324 QLEELESKLDELAEEL--AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1662 QEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAE-DSALKQKEMAENELE 1740
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEElREELEEAEQALDAAE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1741 RQrkvaESTAQQKLTAEQELIR--------LRADFDNAEQQR-------SLLE-DELY----------RLKNEVVAAQQQ 1794
Cdd:TIGR02168 482 RE----LAQLQARLDSLERLQEnlegfsegVKALLKNQSGLSgilgvlsELISvDEGYeaaieaalggRLQAVVVENLNA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1795 RKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLR----------AIAEEAKHQRQV 1864
Cdd:TIGR02168 558 AKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvLVVDDLDNALEL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1865 AEEEAARQR---AEAERILKEKL----AAISDATRLKTEAEIA--------LKEKEAENERLRRQAEDEAYQRKALEDQA 1929
Cdd:TIGR02168 638 AKKLRPGYRivtLDGDLVRPGGVitggSAKTNSSILERRREIEeleekieeLEEKIAELEKALAELRKELEELEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1930 NQHKQQIEEKIVLLKKS---SEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQS 2006
Cdd:TIGR02168 718 RKELEELSRQISALRKDlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2007 KLRAEEEAEKLRKlaleeekrrreaeeKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQ 2086
Cdd:TIGR02168 798 LKALREALDELRA--------------ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2087 AAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKaaaeqeAANQAK 2166
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL------EGLEVR 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2167 AQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQ 2246
Cdd:TIGR02168 938 IDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
890
....*....|....*.
gi 1927222982 2247 RLK---DEVDDAVKQR 2259
Cdd:TIGR02168 1018 TLEeaiEEIDREARER 1033
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
184-299 |
1.63e-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: 107.09 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 184 ISDIQIngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGV 263
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1927222982 264 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 299
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
182-299 |
1.97e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 107.09 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 182 FQISDIQIngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAF 261
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1927222982 262 GVAERDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 299
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2055-2643 |
3.90e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 118.89 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2055 ELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQsvlAQQKEDTIMQtklKEEYEKAKKLAkQAEAAKE 2134
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE---ELELELEEAQ---AEEYELLAELA-RLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2135 KAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTL 2214
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2215 KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKD 2294
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2295 KDNTQKFLAKEAdnmkklAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDL 2374
Cdd:COG1196 466 AELLEEAALLEA------ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2375 AQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLH 2454
Cdd:COG1196 540 LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2455 ETELATQEkmtVVEKLEVARLTSSKEADDLRKAIADLE-----KEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQ 2529
Cdd:COG1196 620 DTLLGRTL---VAARLEAALRRAVTLAGRLREVTLEGEggsagGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2530 TFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEM 2609
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
570 580 590
....*....|....*....|....*....|....*..
gi 1927222982 2610 KELER---KRLEQERILAEENQKLREKLQQLEEAQKD 2643
Cdd:COG1196 777 EALGPvnlLAIEEYEELEERYDFLSEQREDLEEARET 813
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
68-185 |
8.67e-26 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 105.11 E-value: 8.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 68 RVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRERDvvrsvrlPREKgrMRFHKLQNVQIALDF 147
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYH-------PRPN--FRQMKLENVSVALEF 85
|
90 100 110
....*....|....*....|....*....|....*...
gi 1927222982 148 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 185
Cdd:cd21310 86 LDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1386-2336 |
1.32e-25 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 117.38 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1386 QRRLEDEEKAAEKL--KAEEQKKMAMMQAELDKQKQLAEVH-----AKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEK 1458
Cdd:pfam02463 153 ERRLEIEEEAAGSRlkRKKKEALKKLIEETENLAELIIDLEelklqELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1459 QKHNIQLELHELKNLSEQQIMDKSKQVDDalqsrvKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQ 1538
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIE------KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1539 EEAEKLRKQVNEETQKKRMAEEELKRkaeaeKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKS 1618
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKK-----EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1619 AAAELQSKHMSFVEKTSKLEESLKQehgavlqlQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAH 1698
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKE--------AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1699 KKslaqEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKltAEQELIRLRADFDNAEQQRSLLE 1778
Cdd:pfam02463 454 EK----QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESK--ARSGLKVLLALIKDGVGGRIISA 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1779 DELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEA 1858
Cdd:pfam02463 528 HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1859 KHQRQVAEEEAARQRAEAERILKEKlaaisdatrLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEE 1938
Cdd:pfam02463 608 LDKATLEADEDDKRAKVVEGILKDT---------ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEI 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1939 KIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKldLELELNKLKNIAEETQQSKLRAEEEAEKLR 2018
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR--VQEAQDKINEELKLLKQKIDEEEEEEEKSR 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2019 KlaleeekrrreaeekvKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKcsAAEQQV 2098
Cdd:pfam02463 757 L----------------KKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKE--EAELLE 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2099 QSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEA 2178
Cdd:pfam02463 819 EEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEE 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2179 EFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQ--TLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAv 2256
Cdd:pfam02463 899 KKELEEESQKLNLLEEKENEIEERIKEEAEILLKyeEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNL- 977
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2257 KQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQeaARLRQIAEDD 2336
Cdd:pfam02463 978 MAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGS--AELRLEDPDD 1055
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
68-182 |
2.17e-25 |
|
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: 103.34 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 68 RVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRERDvvrsvrlprEKGRMRFHKLQNVQIALDF 147
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYN---------KRPTFRQMKLENVSVALEF 73
|
90 100 110
....*....|....*....|....*....|....*
gi 1927222982 148 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 182
Cdd:cd21228 74 LERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
61-184 |
3.05e-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: 103.68 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 61 RIADERDRVQKKTFTKWVNKHLIKSQRQV--TDLYEDLRDGHNLISLLEVLSGETLPRErdvvrsvrlprEKGRMRFHKL 138
Cdd:cd21247 12 KLQEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRP-----------SRGKMRVHFL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1927222982 139 QNVQIALDFLKHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 184
Cdd:cd21247 81 ENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
200-299 |
4.00e-25 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 102.36 E-value: 4.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 200 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED- 278
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1927222982 279 VDVPHPDEKSIITYVSSLYDA 299
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1708-2503 |
1.09e-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: 114.38 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1708 EKQKEEAER----EAKKRAKAEDSALKQKEMAENELERQRKVAEStaqqkltAEQELIRLRADFDNAEQQRSLLEDELYR 1783
Cdd:TIGR02168 206 ERQAEKAERykelKAELRELELALLVLRLEELREELEELQEELKE-------AEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1784 LKNEVVAAQQqrkqledelakvrsEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKlRAIAEEAKHQRQ 1863
Cdd:TIGR02168 279 LEEEIEELQK--------------ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK-LDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1864 VAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQ----HKQQIEEK 1939
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERledrRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1940 IVLLKKSSEAEMERQRAIVD-------DTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEE 2012
Cdd:TIGR02168 424 EELLKKLEEAELKELQAELEeleeeleELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2013 EAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAE-------------- 2078
Cdd:TIGR02168 504 FSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNElgrvtflpldsikg 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2079 -----------KQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAE--------------AAK 2133
Cdd:TIGR02168 584 teiqgndreilKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRivtldgdlvrpggvITG 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2134 EKAEREAALLRQQAE--EAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAE 2211
Cdd:TIGR02168 664 GSAKTNSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2212 QTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKvqmEELLKLKLRIEEENQRLI 2291
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR---EALDELRAELTLLNEEAA 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2292 KK--DKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQ 2369
Cdd:TIGR02168 821 NLreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2370 RQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKsLEAERKRQLEIIAESEKLKLQ-----VSQLSEAQAKAQEEAKKFKK 2444
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLEeaealENKIEDDEEEARRRLKRLEN 979
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222982 2445 QADsiasRLHETELATQEKMtvvEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAE 2503
Cdd:TIGR02168 980 KIK----ELGPVNLAAIEEY---EELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAR 1031
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1751-2642 |
1.31e-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: 114.38 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1751 QQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQrKQLEDELAKVRSEMDVLiQLKSKAEKEtmsnsERS 1830
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELALLVL-RLEELREEL-----EEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1831 KQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAArqraEAERILKEKLAAISDATRLKTEAEIALKEKEAENER 1910
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE----ELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1911 LRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKkSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLE 1990
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELE-SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1991 LELNKLKNIAEETQQSKLRAEEEAEKLRKlaleeekrrreaeekvkkiaAAEEEAARQRQAAQDELDRLKKKAEEARKQK 2070
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLK--------------------KLEEAELKELQAELEELEEELEELQEELERL 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2071 DDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAqqkedtiMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEA 2150
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLD-------SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2151 ERQKaaaeqeaanqaKAQEDAERLRKEA----EFEAAKRAQAenaALKQKQQADAEM-----AKHKKLAEQTLKQKFQVE 2221
Cdd:TIGR02168 533 EGYE-----------AAIEAALGGRLQAvvveNLNAAKKAIA---FLKQNELGRVTFlpldsIKGTEIQGNDREILKNIE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2222 QELTkVKLKLDETDKQ-KSVLDEELQRLK--DEVDDAVKQRGQVEEELLKVKVQMEELLK----LKLRIEEENQRLikkd 2294
Cdd:TIGR02168 599 GFLG-VAKDLVKFDPKlRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIVTLDGDLVRPggviTGGSAKTNSSIL---- 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2295 kdNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDL 2374
Cdd:TIGR02168 674 --ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2375 AQEQAQKLLEDKQLMQQRLDEETEEYQkslEAERKRQleiiaeseklklqvsQLSEAQAKAQEEAKKFKKQADSIASRLH 2454
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELA---EAEAEIE---------------ELEAQIEQLKEELKALREALDELRAELT 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2455 ETELATQEKMTVVEKLEvarltssKEADDLRKAIADLEKEKSRLKKEAEDLqnkSKEMADAQQKQIEHEKTVlqQTFLSE 2534
Cdd:TIGR02168 814 LLNEEAANLRERLESLE-------RRIAATERRLEDLEEQIEELSEDIESL---AAEIEELEELIEELESEL--EALLNE 881
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2535 KEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQA------------------TMDAALNKQK 2596
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlevridnlqerlseeyslTLEEAEALEN 961
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1927222982 2597 EAEKEMHNKQKEMKELERKR-------LEQERILAEENQKLREKLQQLEEAQK 2642
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKIkelgpvnLAAIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
184-299 |
1.92e-24 |
|
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: 101.34 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 184 ISDIQIngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGV 263
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1927222982 264 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 299
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1709-2608 |
3.90e-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: 112.84 E-value: 3.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1709 KQKEEAEReakKRAKAEDsALKQKEMAENELERQRKVAESTAQQKltaeQELIRLRADFDNAEQQRSL-----LEDELYR 1783
Cdd:TIGR02168 172 ERRKETER---KLERTRE-NLDRLEDILNELERQLKSLERQAEKA----ERYKELKAELRELELALLVlrleeLREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1784 LKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKEtmsnserskqlLEVEATKMRDLAEEASKLRAIAEEAKHQRQ 1863
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1864 VAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLL 1943
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1944 KKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLale 2023
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE--- 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2024 eekrrreaeekvkkiaaaeeeaarqrqAAQDELDRLKKKAEEARKQkddADKEAEKQILMAQQAAQKCSAAEQQVQSVLA 2103
Cdd:TIGR02168 470 ---------------------------LEEAEQALDAAERELAQLQ---ARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2104 QQKEDTIMQTKLKEEYEKA----------------KKLAKQAEAAKEKAE--REAALLRQQAEEAERQKAAAEQEAANQA 2165
Cdd:TIGR02168 520 GILGVLSELISVDEGYEAAieaalggrlqavvvenLNAAKKAIAFLKQNElgRVTFLPLDSIKGTEIQGNDREILKNIEG 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2166 KAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKK-------LAEQTLKQKFQVEQELTKVKLKLDETDKQK 2238
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRpgyrivtLDGDLVRPGGVITGGSAKTNSSILERRREI 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2239 SVLDEELQRLKDEVDDAVKQRGQVEEELLkvkvQMEELLKLKLRIEEENQRLIkkdkDNTQKFLAKEADNMKKLAEDAAR 2318
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELE----ELEEELEQLRKELEELSRQI----SALRKDLARLEAEVEQLEERIAQ 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2319 LSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKL---LEDKQLMQQRLDE 2395
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLER 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2396 ETEEYQKSLEaERKRQLEIIAES-EKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVAR 2474
Cdd:TIGR02168 832 RIAATERRLE-DLEEQIEELSEDiESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2475 LTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNK-SKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLE 2553
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 2554 SqfEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDaalnkqkEAEKEMHNKQKE 2608
Cdd:TIGR02168 991 A--IEEYEELKERYDFLTAQKEDLTEAKETLEEAIE-------EIDREARERFKD 1036
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
196-302 |
6.86e-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: 6.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 196 MTAKEKLLLWSQRMTDGY-QGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVY--RQTNLENLEQAFGVAERDLGVTR 272
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1927222982 273 -LLDPEDVDvpHPDEKSIITYVSSLYDAMPR 302
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
200-300 |
8.37e-24 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 98.69 E-value: 8.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 200 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPEDV 279
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1927222982 280 DVPHPDEKSIITYVSSLYDAM 300
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
202-297 |
8.38e-24 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 98.76 E-value: 8.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 202 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED-VD 280
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1927222982 281 VPHPDEKSIITYVSSLY 297
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
197-301 |
1.01e-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: 98.71 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 197 TAKEKLLLWSQRMTDGYqGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDP 276
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1927222982 277 EDVDVPHPDEKSIITYVSSLYDAMP 301
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1866-2644 |
1.33e-23 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 110.83 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1866 EEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQAnqhkqqiEEKIVLLKK 1945
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA-------KKALEYYQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1946 SSEAEMERQRAIVDDTLKqrrvveEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQS-KLRAEEEAEKLRKLALEE 2024
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLK------LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVlKENKEEEKEKKLQEEELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2025 EKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQ 2104
Cdd:pfam02463 290 LLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2105 QKEDTIMqTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAK 2184
Cdd:pfam02463 370 QLEEELL-AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2185 RAQAEN--AALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVldEELQRLKDEVDDAVKQRGQV 2262
Cdd:pfam02463 449 EKEELEkqELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKAR--SGLKVLLALIKDGVGGRIIS 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2263 EEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRA 2342
Cdd:pfam02463 527 AHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2343 LADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLK 2422
Cdd:pfam02463 607 QLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAE 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2423 LQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEA 2502
Cdd:pfam02463 687 SELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEK 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2503 EDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKK 2582
Cdd:pfam02463 767 SELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQ 846
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222982 2583 KLQatmdaalnkqKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQ 2644
Cdd:pfam02463 847 KLE----------KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEE 898
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1867-2529 |
5.03e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.87 E-value: 5.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1867 EEAA------RQRAEAERILK---EKLAAISDAT--------RLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQA 1929
Cdd:COG1196 162 EEAAgiskykERKEEAERKLEateENLERLEDILgelerqlePLERQAEKAERYRELKEELKELEAELLLLKLRELEAEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1930 NQHKQQIEEKivllkkssEAEMERQRAivddtlkQRRVVEEEIRILKLNFEkassgklDLELELnklkniaEETQQSKLR 2009
Cdd:COG1196 242 EELEAELEEL--------EAELEELEA-------ELAELEAELEELRLELE-------ELELEL-------EEAQAEEYE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2010 AEEEAEKLRKlaleeekrrreaeekvkkiaaaeeeaarqrqaaqdELDRLKKKAEEARKQKDDADKEAEkqilmaqQAAQ 2089
Cdd:COG1196 293 LLAELARLEQ-----------------------------------DIARLEERRRELEERLEELEEELA-------ELEE 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2090 KCSAAEQQVQSVLAQQKEdtimqtkLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQE 2169
Cdd:COG1196 331 ELEELEEELEELEEELEE-------AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2170 DAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLK 2249
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2250 DEVDDAVkqrgQVEEELLKVKVQMEELLK-LKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAAR 2328
Cdd:COG1196 484 EELAEAA----ARLLLLLEAEADYEGFLEgVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2329 LRQIAEDDLNQQRAL----ADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSL 2404
Cdd:COG1196 560 AAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2405 EAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDL 2484
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1927222982 2485 RKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQ 2529
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
184-299 |
5.18e-23 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 97.45 E-value: 5.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 184 ISDIQIngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGV 263
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1927222982 264 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 299
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
197-297 |
1.14e-22 |
|
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: 95.57 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 197 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERdLGVTRLLDP 276
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1927222982 277 EDV---DVphPDEKSIITYVSSLY 297
Cdd:cd21198 80 ADMvllSV--PDKLSVMTYLHQIR 101
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
830-896 |
2.28e-22 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 93.10 E-value: 2.28e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222982 830 QLKPRN--PTHSIkgklPIQAVCDFKQQEITVHKGDECALLNNSQPFKWKVLNRSGHEAVVPSVCFMVP 896
Cdd:pfam17902 1 PLKQRRspVTRPI----PVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
72-181 |
3.16e-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: 93.92 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 72 KTFTKWVNKHLIKSQRQ-VTDLYEDLRDGHNLISLLEVLSGETLPrERDVvrsvrlprEKGRMRFHKLQNVQIALDFLKH 150
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPpVTNFSSDLKDGVALCALLNSLSPGLVD-KKKV--------AASLSRFKKIENINLALSFAEK 71
|
90 100 110
....*....|....*....|....*....|.
gi 1927222982 151 RQVKLVNIRNDDIADGnPKLTLGLIWTIILH 181
Cdd:smart00033 72 LGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
69-184 |
1.38e-21 |
|
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: 92.73 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 69 VQKKTFTKWVNKHLIKSQ--RQVTDLYEDLRDGHNLISLLEVLSGETLPrerdvvrsvrlPREKGRMRFHKLQNVQIALD 146
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPGLVD-----------KKKLNKSEFDKLENINLALD 70
|
90 100 110
....*....|....*....|....*....|....*....
gi 1927222982 147 FLKHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 184
Cdd:pfam00307 71 VAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
198-297 |
3.13e-21 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 91.47 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 198 AKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPE 277
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1927222982 278 D-VDVPHPDEKSIITYVSSLY 297
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1192-2082 |
3.46e-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: 102.83 E-value: 3.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1192 DSLEAELKKATAVSDKMSRvhsERDAELDHYRQLLSSLQDRWKAVFSQIDLRQRELEQLGRQLgyyresydwlirwinda 1271
Cdd:TIGR02168 203 KSLERQAEKAERYKELKAE---LRELELALLVLRLEELREELEELQEELKEAEEELEELTAEL----------------- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1272 kqrqekiqavtitdsKTLKEQLAQEKKLLEEVEgnkDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLASPLKKTkld 1351
Cdd:TIGR02168 263 ---------------QELEEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL--- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1352 sasdniiqeyvtlrtkyselmtltsqyikfitdsQRRLEDEEKAAEKLKAEEqkkmAMMQAELDKQKQLAEVHAKAIAKA 1431
Cdd:TIGR02168 322 ----------------------------------EAQLEELESKLDELAEEL----AELEEKLEELKEELESLEAELEEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1432 EKEAQELKLRM---QEEVNRREDAVVDAEKQKHNIQLELHELKNLSEQQIMDKSKQVDDALQSRVKIEE-EIRLIRLQLE 1507
Cdd:TIGR02168 364 EAELEELESRLeelEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELE 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1508 TTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMaeeelkrkaeaekeaakqkqkaLEDLENLK 1587
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS----------------------LERLQENL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1588 RQAEEAERQVKQAEIEKERQIQVA----HVAAQKSAAAE------LQSKHMSFVEKTSKLEESLKQ-EHGAVLQL----- 1651
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILGVLseliSVDEGYEAAIEaalggrLQAVVVENLNAAKKAIAFLKQnELGRVTFLpldsi 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1652 -QHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRL----------QAEEEAHKKSLAQEDAEKQKEEAERE--- 1717
Cdd:TIGR02168 582 kGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLggvlvvddldNALELAKKLRPGYRIVTLDGDLVRPGgvi 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1718 AKKRAKAEDSAL-KQKEMAenELERQRKVAESTAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRK 1796
Cdd:TIGR02168 662 TGGSAKTNSSILeRRREIE--ELEEKIEELEEKIAE---LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1797 QLEDELAKVRSEMDVLIQLKSKAEKETMSNSERskqlLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEA 1876
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1877 ERiLKEKLAaisDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEE------KIVLLKKSSEAE 1950
Cdd:TIGR02168 813 TL-LNEEAA---NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEleseleALLNERASLEEA 888
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1951 MERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNiAEETQQSKLRAEE--EAEKLRKLALEEEKRR 2028
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV-RIDNLQERLSEEYslTLEEAEALENKIEDDE 967
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 1927222982 2029 REAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADkEAEKQIL 2082
Cdd:TIGR02168 968 EEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLT-EAKETLE 1020
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
68-185 |
5.71e-21 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 91.68 E-value: 5.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 68 RVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGEtlprerdvvRSVRLPREKGRMRFHKLQNVQIALDF 147
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQK---------RMYRKYHQRPTFRQMQLENVSVALEF 86
|
90 100 110
....*....|....*....|....*....|....*...
gi 1927222982 148 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 185
Cdd:cd21309 87 LDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
68-185 |
5.85e-21 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 91.69 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 68 RVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRERDvvrsvrlprEKGRMRFHKLQNVQIALDF 147
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHN---------QRPTFRQMQLENVSVALEF 89
|
90 100 110
....*....|....*....|....*....|....*...
gi 1927222982 148 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 185
Cdd:cd21308 90 LDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
197-296 |
2.47e-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: 88.69 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 197 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERdLGVTRLLDP 276
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1927222982 277 ED-VDVPHPDEKSIITYVSSL 296
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
197-297 |
4.42e-20 |
|
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: 88.17 E-value: 4.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 197 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDP 276
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1927222982 277 EDVDV--PHPDEKSIITYVSSLY 297
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
201-298 |
1.96e-19 |
|
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: 86.63 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 201 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLD-PEDV 279
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1927222982 280 DVPHPDEKSIITYVSSLYD 298
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1588-2642 |
3.38e-19 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 96.40 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1588 RQAEEAERQVKQAEIEKERQIQVAhvaaqkSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAAL--KKQQEDA 1665
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAE------SELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLaaRKQELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1666 ERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAER---EAKKRAKAEDSALKqkEMAENELERQ 1742
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKvttEAKIKKLEEDILLL--EDQNSKLSKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1743 RKVAE---STAQQKLTAEQELIRLRADFDNaeQQRSLLEDELYRLKNEVVAAQQQRK---QLEDELAKVRSEMdvlIQLK 1816
Cdd:pfam01576 154 RKLLEeriSEFTSNLAEEEEKAKSLSKLKN--KHEAMISDLEERLKKEEKGRQELEKakrKLEGESTDLQEQI---AELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1817 SKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKH----QRQVAEEEAARQRAEAE-RILKEKLAAisdat 1891
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQiselQEDLESERAARNKAEKQrRDLGEELEA----- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1892 rLKTEAEIALKEKEAENErLRRQAEDEAYQ-RKALEDQANQHKQQIEEkivLLKKSSEAEMERQRAIvddtlkqrrvveE 1970
Cdd:pfam01576 304 -LKTELEDTLDTTAAQQE-LRSKREQEVTElKKALEEETRSHEAQLQE---MRQKHTQALEELTEQL------------E 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1971 EIRILKLNFEKAssgKLDLELELNKLKNIAEETQQSKLRAEEEAEKLrklaleeekrrreaEEKVKKIAAAEEEAARQRQ 2050
Cdd:pfam01576 367 QAKRNKANLEKA---KQALESENAELQAELRTLQQAKQDSEHKRKKL--------------EGQLQELQARLSESERQRA 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2051 AAQDELDRLKKKAEEARKQKDDADKEAEKqilmaqqAAQKCSAAEQQVQSVLAQQKEDT----IMQTKLKEEYEKAKKLA 2126
Cdd:pfam01576 430 ELAEKLSKLQSELESVSSLLNEAEGKNIK-------LSKDVSSLESQLQDTQELLQEETrqklNLSTRLRQLEDERNSLQ 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2127 KQAE---AAKEKAEREAALLRQQAEEAERqkaaaeqeaanqaKAQEDAERLrkEAEFEAAKRAQAENAALKQKQQADAEM 2203
Cdd:pfam01576 503 EQLEeeeEAKRNVERQLSTLQAQLSDMKK-------------KLEEDAGTL--EALEEGKKRLQRELEALTQQLEEKAAA 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2204 AkhkklaEQTLKQKFQVEQELTKVKLKLDETDKQKSVLdEELQRLKDEV---DDAVKQRGQVEEELLKVKVQMEELLKLK 2280
Cdd:pfam01576 568 Y------DKLEKTKNRLQQELDDLLVDLDHQRQLVSNL-EKKQKKFDQMlaeEKAISARYAEERDRAEAEAREKETRALS 640
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2281 LRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAAR-LRQIAEDDLNQQRALADKMlkekmQAIQEAs 2359
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRaLEQQVEEMKTQLEELEDEL-----QATEDA- 714
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2360 RLRAEAEM----LQRQKDLAQEQAQKLLEDKQLMQQRLDEETEeyqksLEAERKRQLEIIAESEKLKLQVSQLS---EAQ 2432
Cdd:pfam01576 715 KLRLEVNMqalkAQFERDLQARDEQGEEKRRQLVKQVRELEAE-----LEDERKQRAQAVAAKKKLELDLKELEaqiDAA 789
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2433 AKAQEEA----KKFKKQADSIASRLHETELATQEKmtvveklevarLTSSKEADdlrKAIADLEKEKSRLKkeaEDLQnk 2508
Cdd:pfam01576 790 NKGREEAvkqlKKLQAQMKDLQRELEEARASRDEI-----------LAQSKESE---KKLKNLEAELLQLQ---EDLA-- 850
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2509 skeMADAQQKQIEHEKTVLQQTF---LSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDekkklq 2585
Cdd:pfam01576 851 ---ASERARRQAQQERDELADEIasgASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQ------ 921
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222982 2586 atmdaaLNKQKEAEKEMHNKQkemkELERKRLEQErilaeeNQKLREKLQQLEEAQK 2642
Cdd:pfam01576 922 ------LTTELAAERSTSQKS----ESARQQLERQ------NKELKAKLQEMEGTVK 962
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1398-2151 |
1.00e-18 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 94.65 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1398 KLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELKNL--SE 1475
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREAlqQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1476 QQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKStAESELKQLRDRAAEAEKL--RKAAQEEAEKLRKQVNEETQ 1553
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEA-VLEETQERINRARKAAPLaaHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1554 KKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEI---EKERQIQVAH----VAAQKSAAAELQSK 1626
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSireISCQQHTLTQhihtLQQQKTTLTQKLQS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1627 HMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQ--KANEAL------RLRLQAEEEAH 1698
Cdd:TIGR00618 398 LCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQceKLEKIHlqesaqSLKEREQQLQT 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1699 KKSLAQEDAEKQKEEAEReaKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLE 1778
Cdd:TIGR00618 478 KEQIHLQETRKKAVVLAR--LLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSER 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1779 DELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAeea 1858
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL--- 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1859 kHQRQVAEEEAarqraeaerilKEKLAaisdatrLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQiee 1938
Cdd:TIGR00618 633 -HLQQCSQELA-----------LKLTA-------LHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKE--- 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1939 KIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILklnfekaSSGKLDLELE---LNKLKNIAEETQQSKLRAEEEAE 2015
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAS-------SSLGSDLAARedaLNQSLKELMHQARTVLKARTEAH 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2016 KLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELdrlkkKAEEARKQKDDADKEAEKQILMAQQaaqkcsaaE 2095
Cdd:TIGR00618 764 FNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTL-----EAEIGQEIPSDEDILNLQCETLVQE--------E 830
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222982 2096 QQVQSVLAQQKEDTIMQTKLKEEYEKAKKlaKQAEAAKEKAEreaalLRQQAEEAE 2151
Cdd:TIGR00618 831 EQFLSRLEEKSATLGEITHQLLKYEECSK--QLAQLTQEQAK-----IIQLSDKLN 879
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1793-2640 |
1.55e-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: 94.36 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1793 QQRKQLEDELAKVrSEMDVLIQlKSKAEKETMS-NSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAAR 1871
Cdd:TIGR02169 153 VERRKIIDEIAGV-AEFDRKKE-KALEELEEVEeNIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1872 QRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAL-EDQANQHKQQIEEkivllkksSEAE 1950
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGE--------LEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1951 MERQRAIVDDTLKQRRVVEEEIRILklnfekassgkldlELELNKLKNIAEEtqqskLRAEEEAEKLRKLALEEEKRRRE 2030
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKL--------------EAEIDKLLAEIEE-----LEREIEEERKRRDKLTEEYAELK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2031 AEEKvkKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTI 2110
Cdd:TIGR02169 364 EELE--DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2111 MQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAER---QKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQ 2187
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKelsKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2188 AENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKV--------------------KLKLDETDKQKSVLDEELQR 2247
Cdd:TIGR02169 522 GVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKeaiellkrrkagratflplnKMRDERRDLSILSEDGVIGF 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2248 LKDEVDDAVKQRGQVeEELLKVKVQMEEL-----LKLKLRIEEENQRLIKKDKDNTQKFLAKE--ADNMKKLAEDAARLS 2320
Cdd:TIGR02169 602 AVDLVEFDPKYEPAF-KYVFGDTLVVEDIeaarrLMGKYRMVTLEGELFEKSGAMTGGSRAPRggILFSRSEPAELQRLR 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2321 VEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQkdlaQEQAQKLLEDKQLMQQRLDEETEEY 2400
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE----EEKLKERLEELEEDLSSLEQEIENV 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2401 QKSLEAERKRQLEIIAESEKLKLQVSQL--SEAQAKAQE---EAKKFKKQADSIASRLHETELATQEKMTVVEKLEvarl 2475
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEiqaELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE---- 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2476 tssKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMadaQQKQIEHEKTVLqqtflsekemllkkeklieeekkrlesQ 2555
Cdd:TIGR02169 833 ---KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL---EEELEELEAALR---------------------------D 879
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2556 FEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEEN--QKLREK 2633
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELslEDVQAE 959
|
....*..
gi 1927222982 2634 LQQLEEA 2640
Cdd:TIGR02169 960 LQRVEEE 966
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1167-1927 |
1.74e-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: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1167 VKEVETYRTKLKKMRAEAEGEQPVFDSLEAELKKATAVSDKMSRVHSERDAELDHYRQLLSSLQDRWKAVFSQIDLRQRE 1246
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1247 LEQLGRQLGYYRESYDWLIRWINDAKQRQEKIQAVTITDSKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKD 1326
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1327 YELQLVAYKAQVEPLASplKKTKLDSASDNIIQEYVTLRTKYSELMtltsqyikfITDSQRRLEDEEKAAEKLKAEEqkk 1406
Cdd:TIGR02168 391 LELQIASLNNEIERLEA--RLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEELEELQEEL--- 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1407 mAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLR------MQEEVNRREDAVVDAEKQKHNIQLELHELKNLSE----- 1475
Cdd:TIGR02168 457 -ERLEEALEELREELEEAEQALDAAERELAQLQARldslerLQENLEGFSEGVKALLKNQSGLSGILGVLSELISvdegy 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1476 ------------QQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTA---------ESELKQLRDRAAEAEKLR 1534
Cdd:TIGR02168 536 eaaieaalggrlQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGndreilkniEGFLGVAKDLVKFDPKLR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1535 KAAQ------------EEAEKLRKQVNEE---------------------------TQKKRMAEEELKRKAEAEKEAAKQ 1575
Cdd:TIGR02168 616 KALSyllggvlvvddlDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEELEEKIAE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1576 KQKALEDLENLKRQAEEAERQVKQAEIEKERQIqvahvaaqksaaaelqskhmsfvektSKLEESLKQEHGAVLQLQHEA 1655
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQI--------------------------SALRKDLARLEAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1656 AALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMA 1735
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1736 ENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQL 1815
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1816 KSKAEKETMS-NSERSKQLLEVEATKMRdLAEEASKLRA----IAEEAKHQRQVAEEEAARQRAEAERiLKEKLAAISDA 1890
Cdd:TIGR02168 910 RSELRRELEElREKLAQLELRLEGLEVR-IDNLQERLSEeyslTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPV 987
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1927222982 1891 TRLkteaeiALKEKEAENER---LRRQAEDEAYQRKALED 1927
Cdd:TIGR02168 988 NLA------AIEEYEELKERydfLTAQKEDLTEAKETLEE 1021
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
200-296 |
2.09e-18 |
|
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: 83.13 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 200 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTN----LENLEQAFGVAERDLGVTRLLD 275
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1927222982 276 PEDVDVPHPDEKSIITYVSSL 296
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1731-2643 |
2.11e-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: 93.98 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1731 QKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLL----EDELYRLKNEVVAAQQQRKQLEDELAKVR 1806
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLkekrEYEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1807 SEMDVLIQLKSKAEKEtmsnSERSKQLLEVEATKMRDLAEEasklraiaEEAKHQRQVAEEEAarQRAEAERILKEKLAA 1886
Cdd:TIGR02169 251 EELEKLTEEISELEKR----LEEIEQLLEELNKKIKDLGEE--------EQLRVKEKIGELEA--EIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1887 ISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQAnqhkqqieekivllkKSSEAEMERQRAIVDDtlkqrr 1966
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY---------------AELKEELEDLRAELEE------ 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1967 vVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRklaleeekrrreaeekvkkiaaaeeeaa 2046
Cdd:TIGR02169 376 -VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN---------------------------- 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2047 rqrqaaqDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQsvlaqqkedtimqtKLKEEYEKAKKla 2126
Cdd:TIGR02169 427 -------AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY--------------DLKEEYDRVEK-- 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2127 KQAEAAKEKAEREAAllRQQAEEAERQKAAAEQEAANQAK------AQEDAERLRKEAEFEAAKRAQAENAALKQKQQAD 2200
Cdd:TIGR02169 484 ELSKLQRELAEAEAQ--ARASEERVRGGRAVEEVLKASIQgvhgtvAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAK 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2201 A--EMAKHKKLAEQT---LKQKFQVEQELTKVKLK--------LDETDKQ-----KSVLDEELqrLKDEVDDAVKQRGQV 2262
Cdd:TIGR02169 562 EaiELLKRRKAGRATflpLNKMRDERRDLSILSEDgvigfavdLVEFDPKyepafKYVFGDTL--VVEDIEAARRLMGKY 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2263 -----EEELLK---------VKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAAR 2328
Cdd:TIGR02169 640 rmvtlEGELFEksgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2329 LRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRA---------EAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEE 2399
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEnvkselkelEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAE 799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2400 YQKsLEAERKRQLEIIAESE----KLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEvarl 2475
Cdd:TIGR02169 800 LSK-LEEEVSRIEARLREIEqklnRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE---- 874
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2476 tsskeaddlrKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQK---QIEHEKTVLQQTflsekemllkkeklieeeKKRL 2552
Cdd:TIGR02169 875 ----------AALRDLESRLGDLKKERDELEAQLRELERKIEEleaQIEKKRKRLSEL------------------KAKL 926
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2553 ESQFEEEVKKAKALKDEQERQKQQM-----EDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRleqeRILAEEN 2627
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEIPEEELsledvQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKR----AKLEEER 1002
|
970
....*....|....*.
gi 1927222982 2628 QKLREKLQQLEEAQKD 2643
Cdd:TIGR02169 1003 KAILERIEEYEKKKRE 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1455-2425 |
2.30e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 93.59 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1455 DAEKQKHNIQLELHElKNLSEQQIM--DKSKQVDDALQSRVKIEE--EIRLIRLQLETT--VKQKSTAESELKQLRDRAA 1528
Cdd:TIGR02169 169 DRKKEKALEELEEVE-ENIERLDLIidEKRQQLERLRREREKAERyqALLKEKREYEGYelLKEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1529 EAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALE-DLENLKRQAEEAERQVKQAEieKERQ 1607
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERSIAEKERELEDAE--ERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1608 IQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEAL 1687
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1688 RLRLQAEEEAHKKSLAQEDAekqkeeaeREAKKRAKAEDSALK-QKEMAENELERQRKVAESTAQQKLTAEQELIRLRAD 1766
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADL--------NAAIAGIEAKINELEeEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1767 FDNaeqqrslLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLiqlksKAEKETMSNSERskQLLEVEatkmrdlaE 1846
Cdd:TIGR02169 478 YDR-------VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVL-----KASIQGVHGTVA--QLGSVG--------E 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1847 EASKLRAIAEEAKHQRQVAEEEAARQRAEAerILKEKlaAISDATRLKTEAeiaLKEKEAENERLRRQ-AEDEAYQRKAL 1925
Cdd:TIGR02169 536 RYATAIEVAAGNRLNNVVVEDDAVAKEAIE--LLKRR--KAGRATFLPLNK---MRDERRDLSILSEDgVIGFAVDLVEF 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1926 EDQ-ANQHKQQIEEKIVLlkksseAEMERQRAIVDdtlkQRRVVEEEIRIlklnFEKASSgkldLELELNKLKNIAEETQ 2004
Cdd:TIGR02169 609 DPKyEPAFKYVFGDTLVV------EDIEAARRLMG----KYRMVTLEGEL----FEKSGA----MTGGSRAPRGGILFSR 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2005 QSKLRAEEEAEKLRKLaleeekrrreaeekvkkiaaaeeeaARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMA 2084
Cdd:TIGR02169 671 SEPAELQRLRERLEGL-------------------------KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI 725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2085 QQAAQKcsaaEQQVQSVLAQQKEDtimQTKLKEEYEKAKklAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQ 2164
Cdd:TIGR02169 726 EQLEQE----EEKLKERLEELEED---LSSLEQEIENVK--SELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEI 796
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2165 AKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDEtdkqksvLDEE 2244
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE-------LEEE 869
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2245 LQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEaDNMKKLAEDAARLSVEAQ 2324
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE-EELSEIEDPKGEDEEIPE 948
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2325 EAARLRQIAEDDLNQQRALaDKMLKEKMQAIQEAsrlraeAEMLQRQKDLaqeqaqklledkqlmqqrldeetEEYQKSL 2404
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEI-RALEPVNMLAIQEY------EEVLKRLDEL-----------------------KEKRAKL 998
|
970 980
....*....|....*....|.
gi 1927222982 2405 EAERKRQLEIIAESEKLKLQV 2425
Cdd:TIGR02169 999 EEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2302-2650 |
3.39e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.08 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2302 LAKEAdnmkKLAEDAARLSVEAQEA-ARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQ 2380
Cdd:COG1196 205 LERQA----EKAERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2381 KLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELAT 2460
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2461 QEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQtflsekemllk 2540
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA----------- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2541 keklieeekkrlESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQE 2620
Cdd:COG1196 430 ------------LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350
....*....|....*....|....*....|
gi 1927222982 2621 RILAEENQKLREKLQQLEEAQKDQPDKEVI 2650
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
197-295 |
1.11e-17 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 81.13 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 197 TAKEKLLLWSQRMTDGYqgiRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVY-RQTNLENLEQAFGVAERDLGVTRLLD 275
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1927222982 276 PEDVDVPHPDEKSIITYVSS 295
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
193-298 |
4.13e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 79.99 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 193 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTR 272
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1927222982 273 LLDPEDV-DVPHPDEKSIITYVSSLYD 298
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
199-297 |
4.51e-17 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 80.03 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 199 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED 278
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 1927222982 279 -VDVPHPDEKSIITYVSSLY 297
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1217-1803 |
4.88e-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: 4.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1217 AELDHYRQLLSSLQDRW-----KAVFSQIDLRQRELEQLGRQLgyyresydwlirwindaKQRQEKIQavtitdskTLKE 1291
Cdd:COG1196 220 EELKELEAELLLLKLREleaelEELEAELEELEAELEELEAEL-----------------AELEAELE--------ELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1292 QLAQEKKLLEEVEGNkdkvdecqkyakayidtikdyELQLVAYKAQVEplasplkkTKLDSASDNIIQEYVTLRTKYSEL 1371
Cdd:COG1196 275 ELEELELELEEAQAE---------------------EYELLAELARLE--------QDIARLEERRRELEERLEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1372 MTLTSQyikfitdsQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRRED 1451
Cdd:COG1196 326 AELEEE--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1452 AVVDAEKQKHNIQLELHELKNLSEQQImDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAE 1531
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELE-ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1532 KLRKAAQEEAEKLRKQvnEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQVA 1611
Cdd:COG1196 477 AALAELLEELAEAAAR--LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1612 HVAAQKSAAAELQSKH---MSFVEKTSKLEESLKQ---EHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANE 1685
Cdd:COG1196 555 DDEVAAAAIEYLKAAKagrATFLPLDKIRARAALAaalARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1686 ALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRa 1765
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE- 713
|
570 580 590
....*....|....*....|....*....|....*...
gi 1927222982 1766 dfdnAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELA 1803
Cdd:COG1196 714 ----EERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
197-296 |
5.16e-17 |
|
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: 79.51 E-value: 5.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 197 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERdLGVTRLLDP 276
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1927222982 277 ED-VDVPHPDEKSIITYVSSL 296
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
70-182 |
5.85e-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: 79.16 E-value: 5.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 70 QKKTFTKWVNKHLIKS--QRQVTDLYEDLRDGHNLISLLEVLSGETLPRerdvvrsvrlPREKGRMRFHKLQNVQIALDF 147
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPG----------IHSRPKTRAQKLENIQACLQF 70
|
90 100 110
....*....|....*....|....*....|....*
gi 1927222982 148 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 182
Cdd:cd21212 71 LAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1397-2154 |
9.25e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.59 E-value: 9.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1397 EKLKAEEQKKMammqaeldkQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELknlsEQ 1476
Cdd:TIGR02169 206 EREKAERYQAL---------LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI----EQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1477 QIMDKSKQVDDALQSR-VKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKK 1555
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEqLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1556 RMAEEELKrkaeaekeaakqkqkaledlenlKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTS 1635
Cdd:TIGR02169 353 DKLTEEYA-----------------------ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1636 KLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAE 1715
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1716 REAKkRAKAEDSALKQkemAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAeqqrslLEDEL-YRLKNEVVA---- 1790
Cdd:TIGR02169 490 RELA-EAEAQARASEE---RVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATA------IEVAAgNRLNNVVVEddav 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1791 AQQQRKQLEDE---------LAKVRSE----------------MDvLIQLKSKAEKE---------TMSNSERSKQL--- 1833
Cdd:TIGR02169 560 AKEAIELLKRRkagratflpLNKMRDErrdlsilsedgvigfaVD-LVEFDPKYEPAfkyvfgdtlVVEDIEAARRLmgk 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1834 -----LEVE------ATKMRDLAEEASKLRAIAEEAKHQRQVAEEEA--------ARQRAEAERILKEKLAAISDATR-- 1892
Cdd:TIGR02169 639 yrmvtLEGElfeksgAMTGGSRAPRGGILFSRSEPAELQRLRERLEGlkrelsslQSELRRIENRLDELSQELSDASRki 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1893 --LKTEAEIALKEKEAENERLRRQAEDEAYQRKALE------DQANQHKQQIEEKIVLLKKS---------------SEA 1949
Cdd:TIGR02169 719 geIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEnvkselKELEARIEELEEDLHKLEEAlndlearlshsripeIQA 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1950 EMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNiaeetQQSKLRAEEEAEKLRKLALEEEkrrr 2029
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE-----QIKSIEKEIENLNGKKEELEEE---- 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2030 eaeekVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKED- 2108
Cdd:TIGR02169 870 -----LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDe 944
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222982 2109 ----------TIMQTKLK----------------EEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQK 2154
Cdd:TIGR02169 945 eipeeelsleDVQAELQRveeeiralepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1382-2289 |
1.18e-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: 87.92 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1382 ITDSQRRLEDEEKAAEKLKAE---------------------------EQKKMAMMQAELDKQKQLAEVHAKAIAKAEKE 1434
Cdd:pfam01576 105 IQDLEEQLDEEEAARQKLQLEkvtteakikkleedillledqnsklskERKLLEERISEFTSNLAEEEEKAKSLSKLKNK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1435 AQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELKnlseQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKS 1514
Cdd:pfam01576 185 HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ----EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1515 TAESELKQLRDRAAEAEK---LRKAAQEEAEKLRKQVNEETQKKRMaeeELKRKAEAEKEAAKQKQKALEDLENLKRQAE 1591
Cdd:pfam01576 261 NALKKIRELEAQISELQEdleSERAARNKAEKQRRDLGEELEALKT---ELEDTLDTTAAQQELRSKREQEVTELKKALE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1592 EaERQVKQAEIEKERQiqvahvaAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREE 1671
Cdd:pfam01576 338 E-ETRSHEAQLQEMRQ-------KHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1672 AEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENEL--ERQRKVAEST 1749
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLqeETRQKLNLST 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1750 AQQKLTAEQEliRLRADFDNAEQQRSLLEDELYRLKNEVvaaQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSER 1829
Cdd:pfam01576 490 RLRQLEDERN--SLQEQLEEEEEAKRNVERQLSTLQAQL---SDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEK 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1830 SKQLLEVEATKMRdLAEEaskLRAIAEEAKHQRQVAEEEAARQRaEAERILKEKLAAISDATRLKTEAEIALKEKEAENE 1909
Cdd:pfam01576 565 AAAYDKLEKTKNR-LQQE---LDDLLVDLDHQRQLVSNLEKKQK-KFDQMLAEEKAISARYAEERDRAEAEAREKETRAL 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1910 RLRRQAEDEAYQRKALEDQANQHKQQIEEkIVLLKKS---SEAEMERQRAIVDDTLKQRRVVEEEiriLKLNFEKASSGK 1986
Cdd:pfam01576 640 SLARALEEALEAKEELERTNKQLRAEMED-LVSSKDDvgkNVHELERSKRALEQQVEEMKTQLEE---LEDELQATEDAK 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1987 LDLELELNKLKNIAEETQQSKlraEEEAEKLRKLALEEEKRRREAEEKVKKiaaAEEEAARQRQAAQDELDRLKKKAEEA 2066
Cdd:pfam01576 716 LRLEVNMQALKAQFERDLQAR---DEQGEEKRRQLVKQVRELEAELEDERK---QRAQAVAAKKKLELDLKELEAQIDAA 789
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2067 RKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDT---------IMQtkLKEEYEKAKKLAKQAEAAK---- 2133
Cdd:pfam01576 790 NKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEkklknleaeLLQ--LQEDLAASERARRQAQQERdela 867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2134 --------------EKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQA 2199
Cdd:pfam01576 868 deiasgasgksalqDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQN 947
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2200 DAEMAKHKKLaEQTLKQKFQ-----VEQELTKVKLKLDETDKQKSVLDEELQR----LKD---EVDDAVKQRGQVEEELL 2267
Cdd:pfam01576 948 KELKAKLQEM-EGTVKSKFKssiaaLEAKIAQLEEQLEQESRERQAANKLVRRtekkLKEvllQVEDERRHADQYKDQAE 1026
|
970 980
....*....|....*....|..
gi 1927222982 2268 KVKVQMEELLKLKLRIEEENQR 2289
Cdd:pfam01576 1027 KGNSRMKQLKRQLEEAEEEASR 1048
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
71-180 |
1.44e-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: 78.15 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 71 KKTFTKWVNKHL-IKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRErdvvrsvrlpREKGRMRFHKLQNVQIALDFLK 149
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKI----------NKKPKSPFKKRENINLFLNACK 70
|
90 100 110
....*....|....*....|....*....|...
gi 1927222982 150 HRQV-KLVNIRNDDI-ADGNPKLTLGLIWTIIL 180
Cdd:cd00014 71 KLGLpELDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
199-302 |
1.55e-16 |
|
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: 78.17 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 199 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED 278
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1927222982 279 VDV--PHPDEKSIITYVSSLYDAMPR 302
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
199-298 |
2.15e-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: 77.70 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 199 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED 278
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1927222982 279 VDV--PHPDEKSIITYVSSLYD 298
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2056-2649 |
5.02e-16 |
|
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: 85.88 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2056 LDRLKKKAEEARKQKDDADKEAEKqilmAQQAAQKcSAAEQQVQ-SVLAQQKEDtimqtkLKEEYEKAKKLAKQAEAAKE 2134
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQAEK----AERYKEL-KAELRELElALLVLRLEE------LREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2135 KAEREAALLRQQAEEAERQKAAAEQEAANQAK----AQEDAERLRKEAEFEAAKRAQAENaalkQKQQADAEMAKHKKLA 2210
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKelyaLANEISRLEQQKQILRERLANLER----QLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2211 EQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRL 2290
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2291 iKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAE-DDLNQQRALADKMLKEKMQAIQEA--------SRL 2361
Cdd:TIGR02168 413 -EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEElERLEEALEELREELEEAEQALDAAerelaqlqARL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2362 RAEAEMLQRQKDLAQEQAQKLLEDKQLMQQR-----LDEETEEYQKSLEA---------------ERKRQLEIIAESEKL 2421
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKALLKNQSGLSGILgvlseLISVDEGYEAAIEAalggrlqavvvenlnAAKKAIAFLKQNELG 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2422 KLQVSQL----------SEAQAKAQEE------------AKKFKK----------------QADSIASRLH--------- 2454
Cdd:TIGR02168 572 RVTFLPLdsikgteiqgNDREILKNIEgflgvakdlvkfDPKLRKalsyllggvlvvddldNALELAKKLRpgyrivtld 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2455 ---------------ETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQ----NKSKEMADA 2515
Cdd:TIGR02168 652 gdlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRkeleELSRQISAL 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2516 QQKQIEHEKTVlqQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQ 2595
Cdd:TIGR02168 732 RKDLARLEAEV--EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222982 2596 KEA---EKEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQPDKEV 2649
Cdd:TIGR02168 810 AELtllNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
199-300 |
6.71e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 76.66 E-value: 6.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 199 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED 278
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1927222982 279 -VDVPHPDEKSIITYVSSLYDAM 300
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
201-298 |
8.14e-16 |
|
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: 76.07 E-value: 8.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 201 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLD-PEDV 279
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1927222982 280 DVPHPDEKSIITYVSSLYD 298
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1166-1823 |
1.31e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1166 DVKEVETYRTKLKKMRAEAEgeqpvfdSLEAELKKATAVSDKMSRVHSERDAELDHYRQLLSSLQDRWKAVFSQIDLRQR 1245
Cdd:COG1196 223 KELEAELLLLKLRELEAELE-------ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1246 ELEQLGRQLGYYRESydwlirwINDAKQRQEKIQAvtitdskTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIK 1325
Cdd:COG1196 296 ELARLEQDIARLEER-------RRELEERLEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1326 DYELQLVAYKAQVEPlasplkktkldsasdnIIQEYVTLRTKYSELMTLTSQYIKFITDSQRRLEDEEKAAEKLKAEEQk 1405
Cdd:COG1196 362 EAEEALLEAEAELAE----------------AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1406 kmAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELKNLSEQQIMDKSKQV 1485
Cdd:COG1196 425 --ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1486 DDALQSRVKIEEEIRLIRLQLEttvkqkstaesELKQLRDRAAEAEKLrkAAQEEAEKLRKQVNEETQKKRMAEEELKRk 1565
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAG-----------AVAVLIGVEAAYEAA--LEAALAAALQNIVVEDDEVAAAAIEYLKA- 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1566 aeaekeaakqkqkalEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEH 1645
Cdd:COG1196 569 ---------------AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1646 GAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAE 1725
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1726 DSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVA-------------AQ 1792
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllaieeyeEL 793
|
650 660 670
....*....|....*....|....*....|..
gi 1927222982 1793 QQRKQ-LEDELAKVRSEMDVLIQLKSKAEKET 1823
Cdd:COG1196 794 EERYDfLSEQREDLEEARETLEEAIEEIDRET 825
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
70-182 |
3.93e-15 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 74.26 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 70 QKKTFTKWVNKHLIK--SQRQVTDLYEDLRDGHNLISLLEVLSGETLPrerDVVRSvrlPREKGRMRfhklQNVQIALDF 147
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLP---GIDWN---PTTDAERK----ENVEKVLQF 70
|
90 100 110
....*....|....*....|....*....|....*
gi 1927222982 148 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 182
Cdd:cd21213 71 MASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1497-2303 |
3.98e-15 |
|
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: 83.09 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1497 EEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKrkaeaekeaakqk 1576
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELK------------- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1577 qkaledlenlkrQAEEAERQVKQAEIEKERQIQVAhvaaqksaaaelqskhmsfvEKTSKLEESLKQEHGAVLQLQHEAA 1656
Cdd:TIGR00618 230 ------------HLREALQQTQQSHAYLTQKREAQ--------------------EEQLKKQQLLKQLRARIEELRAQEA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1657 ALKKQQedaerareeaeKELEKWRQKANEAlrlrlqaeeeAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMA- 1735
Cdd:TIGR00618 278 VLEETQ-----------ERINRARKAAPLA----------AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKq 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1736 ENELERQRKVaestaQQKLTAEQELIRlradfDNAEQQRSLLE--DELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLI 1813
Cdd:TIGR00618 337 QSSIEEQRRL-----LQTLHSQEIHIR-----DAHEVATSIREisCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1814 QLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAkhQRQVAEEEAARQRAEAERILKEKLAAISDATRL 1893
Cdd:TIGR00618 407 REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA--QCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1894 KTE---AEIALKEKEAENERL--RRQAEDEAYQRKALEDQANQHK-QQIEEKIVLLKKsseaEMERQRAIVDDTLKQRRV 1967
Cdd:TIGR00618 485 ETRkkaVVLARLLELQEEPCPlcGSCIHPNPARQDIDNPGPLTRRmQRGEQTYAQLET----SEEDVYHQLTSERKQRAS 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1968 VEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQsKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAAR 2047
Cdd:TIGR00618 561 LKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD-LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQ 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2048 QRQAAQDELDRLKKK-AEEARKQKDDADKEAEKQILMAQQAAQKcsAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLA 2126
Cdd:TIGR00618 640 ELALKLTALHALQLTlTQERVREHALSIRVLPKELLASRQLALQ--KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYD 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2127 KQAEaakekaEREAALLRQQAEEAERqkaaAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALK---QKQQADAEM 2203
Cdd:TIGR00618 718 REFN------EIENASSSLGSDLAAR----EDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgaELSHLAAEI 787
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2204 AKHKKLAEQTLKQKFQVEQEL-TKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKV---KVQMEELLKL 2279
Cdd:TIGR00618 788 QFFNRLREEDTHLLKTLEAEIgQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYeecSKQLAQLTQE 867
|
810 820 830
....*....|....*....|....*....|.
gi 1927222982 2280 KLRIEEE-------NQRLIKKDKDNTQKFLA 2303
Cdd:TIGR00618 868 QAKIIQLsdklngiNQIKIQFDGDALIKFLH 898
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1367-2151 |
5.86e-15 |
|
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: 82.53 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1367 KYSELMTLTSQYIKFITDSQRRLEDEEKA---AEKLKAEEQKKMAMMQAEL-DKQKQLAEVHAKaIAKAEKEAQELKLRM 1442
Cdd:pfam01576 174 KAKSLSKLKNKHEAMISDLEERLKKEEKGrqeLEKAKRKLEGESTDLQEQIaELQAQIAELRAQ-LAKKEEELQAALARL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1443 QEEVNRREDAVvdaeKQKHNIQLELHELKNLSEQQIMDKSKqvddALQSRVKIEEEIRLIRLQLETTVkQKSTAESELKQ 1522
Cdd:pfam01576 253 EEETAQKNNAL----KKIRELEAQISELQEDLESERAARNK----AEKQRRDLGEELEALKTELEDTL-DTTAAQQELRS 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1523 LRDRaaEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLE--NLKRQAEEAERQVKQA 1600
Cdd:pfam01576 324 KREQ--EVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALEseNAELQAELRTLQQAKQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1601 EIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKEL-EKW 1679
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLqEET 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1680 RQKANEALRLR-----------LQAEEEAHKKSLAQE---------DAEKQKE------EAEREAKKRAKAEDSALKQ-- 1731
Cdd:pfam01576 482 RQKLNLSTRLRqledernslqeQLEEEEEAKRNVERQlstlqaqlsDMKKKLEedagtlEALEEGKKRLQRELEALTQql 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1732 --KEMAENELERQRK-------------------VAESTAQQK----LTAEQELIRLRA--DFDNAEQQRSLLEDELYRL 1784
Cdd:pfam01576 562 eeKAAAYDKLEKTKNrlqqelddllvdldhqrqlVSNLEKKQKkfdqMLAEEKAISARYaeERDRAEAEAREKETRALSL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1785 KNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKeTMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAK----- 1859
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGK-NVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKlrlev 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1860 -------------HQRQVAEEEAARQRA----EAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQR 1922
Cdd:pfam01576 721 nmqalkaqferdlQARDEQGEEKRRQLVkqvrELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1923 KALEDQANQHKQQIEE------KIVLLKKSS-------EAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDL 1989
Cdd:pfam01576 801 KKLQAQMKDLQRELEEarasrdEILAQSKESekklknlEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1990 ELELNKLK----NIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKvkkiaaaeEEAARQRQAAQDELDRLKKKAEE 2065
Cdd:pfam01576 881 QDEKRRLEariaQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAE--------RSTSQKSESARQQLERQNKELKA 952
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2066 ARKQKDDADKEAEKQILMAQQAaqKCSAAEQQvqsvLAQQKEDTIMQTKLKEEYEKAKKLA--------KQAEAAKEKAE 2137
Cdd:pfam01576 953 KLQEMEGTVKSKFKSSIAALEA--KIAQLEEQ----LEQESRERQAANKLVRRTEKKLKEVllqvederRHADQYKDQAE 1026
|
890
....*....|....*..
gi 1927222982 2138 REAALLRQ---QAEEAE 2151
Cdd:pfam01576 1027 KGNSRMKQlkrQLEEAE 1043
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
67-178 |
6.39e-15 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 73.72 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 67 DRVQKKTFTKWVNKHLIKSQ-RQVTDLYEDLRDGHNLISLLEVLSGETLPRERDVvrsvrlpreKGRMRFHKLQNVQIAL 145
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDL---------EPKNRIQMIQNLHLAM 72
|
90 100 110
....*....|....*....|....*....|....
gi 1927222982 146 DFL-KHRQVKLVNIRNDDIADGNPKLTLGLIWTI 178
Cdd:cd21225 73 LFIeEDLKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4070-4108 |
6.54e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.20 E-value: 6.54e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1927222982 4070 LLEAQIATGGIIDPEESHRVPVEVAYKRGFFDEEMNEIL 4108
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
202-297 |
8.23e-15 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 73.55 E-value: 8.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 202 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAErDLGVTRLLDPED-VD 280
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1927222982 281 VPHPDEKSIITYVSSLY 297
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3756-3794 |
1.16e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.43 E-value: 1.16e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1927222982 3756 LLEAQAATGFIVDPVKNETLTVDEAVRKGIVGPEIHDKL 3794
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2353-2662 |
1.31e-14 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 80.94 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2353 QAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEdkQLMQQRLDEETEEyqKSLEAERKRQLEiiaESEK-----LKLQVSQ 2427
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFE--KMEQERLRQEKEE--KAREVERRRKLE---EAEKarqaeMDRQAAI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2428 LSEAQAKAQEEAKKFKK----QADSIASRLHETELATQ-EKMTVVEKLEVARLTSS----KEADDLRKaIADLEKEKSR- 2497
Cdd:pfam17380 336 YAEQERMAMERERELERirqeERKRELERIRQEEIAMEiSRMRELERLQMERQQKNervrQELEAARK-VKILEEERQRk 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2498 LKKEAEDLQNKSKEMADAQQKQIEhektVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQM 2577
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEARQREVR----RLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2578 EDEKKKLQATMDA-------ALNKQKEAEKEMHNKQKEMKELERKRL------------------EQERILAEENQKL-- 2630
Cdd:pfam17380 491 EQRRKILEKELEErkqamieEERKRKLLEKEMEERQKAIYEEERRREaeeerrkqqemeerrriqEQMRKATEERSRLea 570
|
330 340 350
....*....|....*....|....*....|....*.
gi 1927222982 2631 ----REKLQQLEEAQKDQPDKEVihVTMVETTKNVY 2662
Cdd:pfam17380 571 mereREMMRQIVESEKARAEYEA--TTPITTIKPIY 604
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1317-1964 |
1.41e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 81.11 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1317 AKAYIDTIKDYELQLVAYKAQVEPLAsPLKKTKldsasdniiQEYVTLRTKYSELMTLtsqyikfitDSQRRLEDEEKAA 1396
Cdd:COG4913 230 LVEHFDDLERAHEALEDAREQIELLE-PIRELA---------ERYAAARERLAELEYL---------RAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1397 EKLKAEEQKkmamMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDavvDAEKQKHNIQLELHELKNLSEQ 1476
Cdd:COG4913 291 ELLEAELEE----LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE---QLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1477 QimdkSKQVDDALQSRVKIEEEIRLIRLQLETTVKQkstAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNE-ETQKK 1555
Cdd:COG4913 364 L----EALLAALGLPLPASAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIASlERRKS 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1556 RMAEEELKRkaeaekeaakqkqkaledLENLKRQAEEAER---------QVKQAE------IEK---------------- 1604
Cdd:COG4913 437 NIPARLLAL------------------RDALAEALGLDEAelpfvgeliEVRPEEerwrgaIERvlggfaltllvppehy 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1605 ------------ERQIQVAHVAAQKSAAAELQSKHMSFVEK-TSK-------LEESLKQEHGAVL-----QLQHEAAALK 1659
Cdd:COG4913 499 aaalrwvnrlhlRGRLVYERVRTGLPDPERPRLDPDSLAGKlDFKphpfrawLEAELGRRFDYVCvdspeELRRHPRAIT 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1660 KQ-QEDAERAREeaekelEKWRQKA----------NEALRLRLQAEEEAHKKSLAQedAEKQKEEAEREAKKRAKAEDSA 1728
Cdd:COG4913 579 RAgQVKGNGTRH------EKDDRRRirsryvlgfdNRAKLAALEAELAELEEELAE--AEERLEALEAELDALQERREAL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1729 LKQKEMAENELErqrkvAESTAQQKLTAEQELIRLRADFDNAEQqrslLEDELYRLKNEVVAAQQQRKQLEDELAKVRSE 1808
Cdd:COG4913 651 QRLAEYSWDEID-----VASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1809 MDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKE-KLAAI 1887
Cdd:COG4913 722 LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWP 801
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222982 1888 SDATRLKTEAEiALKEKEAENERLRRQAEDEAYQR--KALEDQANQHKQQIEEKIvllkKSSEAEMERQRAIVDDTLKQ 1964
Cdd:COG4913 802 AETADLDADLE-SLPEYLALLDRLEEDGLPEYEERfkELLNENSIEFVADLLSKL----RRAIREIKERIDPLNDSLKR 875
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1808-2625 |
1.45e-14 |
|
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: 81.17 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1808 EMDVLIQLKSKAEKETMSNSERSKQLlEVEATKMRDLAEEA-SKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAA 1886
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQY-TQLALMEFAKKKSLhGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1887 ISDATRLKTEAEIALKEKEAENERLRRQ-------AEDEAY--QRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAI 1957
Cdd:TIGR00618 232 REALQQTQQSHAYLTQKREAQEEQLKKQqllkqlrARIEELraQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1958 VDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLkniaeETQQSKLRAEEEAEKLRKlaleeekrrreaeekvkk 2037
Cdd:TIGR00618 312 IHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTL-----HSQEIHIRDAHEVATSIR------------------ 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2038 iaaaeeeaaRQRQAAQDELDRLKKKAEEarKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKE 2117
Cdd:TIGR00618 369 ---------EISCQQHTLTQHIHTLQQQ--KTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQ 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2118 EYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQ 2197
Cdd:TIGR00618 438 RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2198 QADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELL 2277
Cdd:TIGR00618 518 QDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2278 KLKLRIEEENQRLIKKDKDNTQKfLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEdDLNQQRALADKMLKEKMQAIQE 2357
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRK-LQPEQDLQDVRLHLQQCSQELALKLTALHALQL-TLTQERVREHALSIRVLPKELL 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2358 ASRLRAEAEMlqrqkdlaQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQ---LEIIAESEKLKLQVSQLSEAQAK 2434
Cdd:TIGR00618 676 ASRQLALQKM--------QSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNeieNASSSLGSDLAAREDALNQSLKE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2435 AQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMAD 2514
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLV 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2515 AQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFE--EEVKKAKALkdeqeRQKQQMEDEKKKLQATMDAAL 2592
Cdd:TIGR00618 828 QEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKiiQLSDKLNGI-----NQIKIQFDGDALIKFLHEITL 902
|
810 820 830
....*....|....*....|....*....|...
gi 1927222982 2593 NKQKEAEKEMHNKQKEMKELERKRLEQERILAE 2625
Cdd:TIGR00618 903 YANVRLANQSEGRFHGRYADSHVNARKYQGLAL 935
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1243-2013 |
1.52e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 81.27 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1243 RQRELEQLGRQLGYYRESYDWLIRW-IND-----AKQRQEKIQAVTITDSKTLKEQLAQEKklLEEVEGNKDKVDECQKY 1316
Cdd:TIGR02169 118 RLSEIHDFLAAAGIYPEGYNVVLQGdVTDfismsPVERRKIIDEIAGVAEFDRKKEKALEE--LEEVEENIERLDLIIDE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1317 AKAYIDTIKDYELQLVAYKAqveplaspLKKTKLDSASDNIIQEYVTLRTKYSELMTLTSQYIKFITDSQRRLEDEEK-- 1394
Cdd:TIGR02169 196 KRQQLERLRREREKAERYQA--------LLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKrl 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1395 --AAEKLKAEEQKKMAMMQAE-LDKQKQLAEVHAKaIAKAEKEAQELKLRMQeevnrredavvDAEKQKHNIQLELHELK 1471
Cdd:TIGR02169 268 eeIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAE-IASLERSIAEKERELE-----------DAEERLAKLEAEIDKLL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1472 nlseQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEE 1551
Cdd:TIGR02169 336 ----AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1552 TQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQ-------------------AEIEKER---QIQ 1609
Cdd:TIGR02169 412 QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQlaadlskyeqelydlkeeyDRVEKELsklQRE 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1610 VAHVAAQKSAAAELQSkhmSFVEKTSKLEESLKQEHGAVLQL-----QH----EAAALKKQQEDAERAREEAEKELEKWR 1680
Cdd:TIGR02169 492 LAEAEAQARASEERVR---GGRAVEEVLKASIQGVHGTVAQLgsvgeRYataiEVAAGNRLNNVVVEDDAVAKEAIELLK 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1681 QK-------------ANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAER------------EAKKRAKAE------DSAL 1729
Cdd:TIGR02169 569 RRkagratflplnkmRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKyvfgdtlvvediEAARRLMGKyrmvtlEGEL 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1730 KQKEMAENELERQRKVAESTAQQKltaEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEM 1809
Cdd:TIGR02169 649 FEKSGAMTGGSRAPRGGILFSRSE---PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI 725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1810 DVLIQlKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAE--------RILK 1881
Cdd:TIGR02169 726 EQLEQ-EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelSKLE 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1882 EKLAAISDATRlktEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEkIVLLKKSSEAEMERQRAIVDDT 1961
Cdd:TIGR02169 805 EEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN-LNGKKEELEEELEELEAALRDL 880
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1927222982 1962 LKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEE 2013
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3423-3461 |
3.21e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 69.28 E-value: 3.21e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1927222982 3423 LLEAQAATGFMVDPVKKQCLSVDEAVKSGLVGPELHEKL 3461
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1712-2442 |
3.36e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.96 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1712 EEAEREAKKrakaedsALKQKEMAENELERQRKVAESTAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAA 1791
Cdd:COG4913 238 ERAHEALED-------AREQIELLEPIRELAERYAAARERL---AELEYLRAALRLWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1792 QQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEE-ASKLRAIAEEAKHQRQVAEE--- 1867
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARlEALLAALGLPLPASAEEFAAlra 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1868 EAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAE--DEAYQ--RKALEDQANQHKQQIeeKIV-- 1941
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniPARLLalRDALAEALGLDEAEL--PFVge 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1942 LLK-KSSEAEME----------RQRAIVDDTLKQ--RRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAE--ETQQS 2006
Cdd:COG4913 466 LIEvRPEEERWRgaiervlggfALTLLVPPEHYAaaLRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGklDFKPH 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2007 KLRAEEEAEKLRKLALeeekrrreaeekvkkiaaaeeeaarQRQAAQDELDRLKK--------KAEEARKQKDDADKEAE 2078
Cdd:COG4913 546 PFRAWLEAELGRRFDY-------------------------VCVDSPEELRRHPRaitragqvKGNGTRHEKDDRRRIRS 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2079 KQILmAQQAAQKCSAAEQQVQsvlaqqkedtimqtKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAae 2158
Cdd:COG4913 601 RYVL-GFDNRAKLAALEAELA--------------ELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV-- 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2159 qeaanqakAQEDAERLRKEAEFEAAKRAQAENAALKQKQQadaemakhkklaeqtlkqkfQVEQELTKVKLKLDETDKQK 2238
Cdd:COG4913 664 --------ASAEREIAELEAELERLDASSDDLAALEEQLE--------------------ELEAELEELEEELDELKGEI 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2239 SVLDEELQRLKDEVDDAvkqRGQVEEELLKVKVQMEELLKLKLRiEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAAR 2318
Cdd:COG4913 716 GRLEKELEQAEEELDEL---QDRLEAAEDLARLELRALLEERFA-AALGDAVERELRENLEERIDALRARLNRAEEELER 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2319 L-----------------SVEAQE--AARLRQIAEDDLNQQRALADKMLKEkmQAIQEASRLRAEaemLQRQKDLAQEQA 2379
Cdd:COG4913 792 AmrafnrewpaetadldaDLESLPeyLALLDRLEEDGLPEYEERFKELLNE--NSIEFVADLLSK---LRRAIREIKERI 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2380 QKL---LEDKQ---------LMQQRLDEETEEYQKSL-EAERKRQLEIIAESEKLKLQVSQL-----SEAQAKAQEEAKK 2441
Cdd:COG4913 867 DPLndsLKRIPfgpgrylrlEARPRPDPEVREFRQELrAVTSGASLFDEELSEARFAALKRLierlrSEEEESDRRWRAR 946
|
.
gi 1927222982 2442 F 2442
Cdd:COG4913 947 V 947
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2063-2654 |
3.54e-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: 79.83 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2063 AEEARKQK--------DDADKEAEKQILMAQQAAQKCSAAEQQVQ-------SVLAQQKEDTIMQTKLKEEYE------- 2120
Cdd:pfam01576 114 EEEAARQKlqlekvttEAKIKKLEEDILLLEDQNSKLSKERKLLEeriseftSNLAEEEEKAKSLSKLKNKHEamisdle 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2121 ----KAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKaaaeqeaanqakAQEDAERLRKEAEFEAA-----KRAQAENA 2191
Cdd:pfam01576 194 erlkKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQI------------AELRAQLAKKEEELQAAlarleEETAQKNN 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2192 ALKQKQQADAEMAkhkklaeqtlkqkfQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDD-----AVKQ--RGQVEE 2264
Cdd:pfam01576 262 ALKKIRELEAQIS--------------ELQEDLESERAARNKAEKQRRDLGEELEALKTELEDtldttAAQQelRSKREQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2265 ELLKVKVQMEE--------LLKLKLR----IEEENQRL--IKKDKDNTQKF-LAKEADNmKKLAEDAARLSVEAQEAARL 2329
Cdd:pfam01576 328 EVTELKKALEEetrsheaqLQEMRQKhtqaLEELTEQLeqAKRNKANLEKAkQALESEN-AELQAELRTLQQAKQDSEHK 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2330 RQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDK-------QLMQQRLDEETEeyQK 2402
Cdd:pfam01576 407 RKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVsslesqlQDTQELLQEETR--QK 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2403 SLEAERKRQLEiiaeSEKLKLQvSQLSEaqakaQEEAKK-FKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEA 2481
Cdd:pfam01576 485 LNLSTRLRQLE----DERNSLQ-EQLEE-----EEEAKRnVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2482 DDLRK-------AIADLEKEKSRLKKEAEDLQnkskeMADAQQKQI----EHEKTVLQQTFLSEKEMllkkEKLIEEEKK 2550
Cdd:pfam01576 555 EALTQqleekaaAYDKLEKTKNRLQQELDDLL-----VDLDHQRQLvsnlEKKQKKFDQMLAEEKAI----SARYAEERD 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2551 RLESQFEEEVKKAKALK---DEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHnkqkemkELERKRleqeRILAEEN 2627
Cdd:pfam01576 626 RAEAEAREKETRALSLAralEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVH-------ELERSK----RALEQQV 694
|
650 660
....*....|....*....|....*...
gi 1927222982 2628 QKLREKLQQLE-EAQKDQPDKEVIHVTM 2654
Cdd:pfam01576 695 EEMKTQLEELEdELQATEDAKLRLEVNM 722
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
197-294 |
5.03e-14 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 70.87 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 197 TAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTN-LENLEQAFGVAERDLGVTRLLD 275
Cdd:cd21230 1 TPKQRLLGWIQ---NKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1927222982 276 PEDVDVPHPDEKSIITYVS 294
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1287-1858 |
6.17e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.95 E-value: 6.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1287 KTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDYELQLvayKAQVEPLASPLKKTKLDSAsdnIIQEYVTLRT 1366
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL---EEKVKELKELKEKAEEYIK---LSEFYEEYLD 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1367 KYSELMTLTSQYIKFITDSQRRLEDEEKAAEKLKaEEQKKMAMMQAELDKQKQLAEVHAKAIAKaEKEAQELKLRMQ-EE 1445
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAK-KEELERLKKRLTgLT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1446 VNRREDAVVDAEKQKHNIQLELHEL---KNLSEQQIMDKSKQVDDALQSRVKI---------EEEIRLIR---LQLETTV 1510
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAKGKCpvcgrelteEHRKELLEeytAELKRIE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1511 KQKSTAESELKQLRDRAAEAEKLRKAaQEEAEKLRKQVNEetqkKRMAEEELKRKaeaekeaakqkqkaleDLENLKRQA 1590
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQ----LKELEEKLKKY----------------NLEELEKKA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1591 EEAERqVKQAEIEKERQIQVahVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGavlqlqheaaalkkqqedaerare 1670
Cdd:PRK03918 525 EEYEK-LKEKLIKLKGEIKS--LKKELEKLEELKKKLAELEKKLDELEEELAELLK------------------------ 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1671 eaekELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKvaesta 1750
Cdd:PRK03918 578 ----ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK------ 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1751 qqkltaeqELIRLRADFDNAEQQRslLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLiqlksKAEKETMSNSERS 1830
Cdd:PRK03918 648 --------ELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKL-----KEELEEREKAKKE 712
|
570 580
....*....|....*....|....*...
gi 1927222982 1831 KQLLEVEATKMRDLAEEASKLRAIAEEA 1858
Cdd:PRK03918 713 LEKLEKALERVEELREKVKKYKALLKER 740
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2377-2644 |
6.66e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 6.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2377 EQAQKLLEDkqlMQQRLD------EETEEYQKSLE-----AERKRQLEIIAESEKLKLQVSQLSEAQAK---AQEEAKKF 2442
Cdd:COG1196 175 EEAERKLEA---TEENLErledilGELERQLEPLErqaekAERYRELKEELKELEAELLLLKLRELEAEleeLEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2443 KKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEH 2522
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2523 EKTVLQQtfLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEM 2602
Cdd:COG1196 332 LEELEEE--LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1927222982 2603 HNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQ 2644
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2055-2650 |
7.84e-14 |
|
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: 78.86 E-value: 7.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2055 ELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLA-QQKEDTIMQTKLKEEYEKAKKLAKQAEAAK 2133
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQvLEKELKHLREALQQTQQSHAYLTQKREAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2134 EKAEREAALLRQQAEEAERQkaaaeQEAANQAKAQEDAERLRKEAefeaakRAQAENAALKQKQQADAEMAKHKKLAEQT 2213
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELR-----AQEAVLEETQERINRARKAA------PLAAHIKAVTQIEQQAQRIHTELQSKMRS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2214 LKQKFQVEQELTKVKLKLDETDKqksvLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLikk 2293
Cdd:TIGR00618 323 RAKLLMKRAAHVKQQSSIEEQRR----LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKL--- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2294 dKDNTQKFLAKEADNMKKLAEDAARlSVEAQEAARLR---QIAEDDLNQQRALADKMLKEKMQAIQEASR----LRAEAE 2366
Cdd:TIGR00618 396 -QSLCKELDILQREQATIDTRTSAF-RDLQGQLAHAKkqqELQQRYAELCAAAITCTAQCEKLEKIHLQEsaqsLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2367 MLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLeiIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQA 2446
Cdd:TIGR00618 474 QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQD--IDNPGPLTRRMQRGEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2447 DSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTV 2526
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2527 LQQTFLSEKEMLLKKEKLIEEekkrLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKE---MH 2603
Cdd:TIGR00618 632 LHLQQCSQELALKLTALHALQ----LTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCqtlLR 707
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 2604 NKQKEMKELERKRLEQERILAEENQKL------------------REKLQQLEEAQKDQPDKEVI 2650
Cdd:TIGR00618 708 ELETHIEEYDREFNEIENASSSLGSDLaaredalnqslkelmhqaRTVLKARTEAHFNNNEEVTA 772
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1938-2647 |
8.80e-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: 78.22 E-value: 8.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1938 EKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASsgkLDLELELNKLKNIAEETQQS-------KLRA 2010
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVS---LKLEEEIQENKDLIKENNATrhlcnllKETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2011 EEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEaarqrqaaqdeLDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQK 2090
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQVYMDLNNNIEKMILA-----------FEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2091 -CSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEaakEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQE 2169
Cdd:pfam05483 234 eINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE---EKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2170 DAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLK 2249
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2250 DEVDDAVKQRGQVE---EELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEA 2326
Cdd:pfam05483 391 SELEEMTKFKNNKEvelEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2327 ARLRQIAEDDLNQQ------RALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLedKQLmqQRLDEETEEY 2400
Cdd:pfam05483 471 KEVEDLKTELEKEKlknielTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERML--KQI--ENLEEKEMNL 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2401 QKSLEAERKrqlEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKE 2480
Cdd:pfam05483 547 RDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2481 ADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKtvlqqtfLSEKEMLlkkeklieeekkrlesqfeEEV 2560
Cdd:pfam05483 624 GSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK-------ISEEKLL-------------------EEV 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2561 KKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQK-EAEKEMHNKQKEMKELERKRLEQERI---LAEENQKLREKLQQ 2636
Cdd:pfam05483 678 EKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKhQYDKIIEERDSELGLYKNKEQEQSSAkaaLEIELSNIKAELLS 757
|
730
....*....|....
gi 1927222982 2637 LE---EAQKDQPDK 2647
Cdd:pfam05483 758 LKkqlEIEKEEKEK 771
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
63-181 |
8.86e-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: 70.39 E-value: 8.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 63 ADERDrvqKKTFTKWVNKHLIKsqRQVTDLYEDLRDGhnlISLLEVLsgETLprERDVVRSVRLPREKGRMRFHKLQNVQ 142
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLD--PLINNLYEDLRDG---LVLLQVL--DKI--QPGCVNWKKVNKPKPLNKFKKVENCN 68
|
90 100 110
....*....|....*....|....*....|....*....
gi 1927222982 143 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 181
Cdd:cd21219 69 YAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2116-2648 |
1.05e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 78.47 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2116 KEEYEKAKKLAKQAEAAKEK----AEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENA 2191
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELiidlEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2192 ALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLK-------DEVDDAVKQRGQVEE 2264
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLErrkvddeEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2265 ELLKVKVQMEELLKLKL---RIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQR 2341
Cdd:pfam02463 329 ELKKEKEEIEELEKELKeleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2342 ALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQA--QKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESE 2419
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLteEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2420 KLKLQVSQLSEAQA-KAQEEAKKFKKQADSIASRLHETELATQEKM-TVVEKLEVARLTSSKEADDLRKAIADLEKEKSR 2497
Cdd:pfam02463 489 LLSRQKLEERSQKEsKARSGLKVLLALIKDGVGGRIISAHGRLGDLgVAVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2498 LKKEAEDLQNK-----SKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQER 2572
Cdd:pfam02463 569 ALTELPLGARKlrlliPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGL 648
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222982 2573 QKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQPDKE 2648
Cdd:pfam02463 649 RKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
197-297 |
2.01e-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: 69.72 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 197 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAErDLGVTRLLDP 276
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1927222982 277 ED-VDVPHPDEKSIITYVSSLY 297
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1150-1897 |
2.86e-13 |
|
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: 77.03 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1150 LKQYEDCLREVHTVPNDVKEVETYRTKLKKMRAEAEGE----QPVFDSLEAELKKAT-----AVSDKMSRVHSER---DA 1217
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRleeiEQLLEELNKKIKDLGeeeqlRVKEKIGELEAEIaslER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1218 ELDHYRQLLSSLQDRWKAVFSQIDLRQRELEQLGRQLGYYRESYDWLIRWINDAKQRQEKIQAVTITDSKTLKEQLAQEK 1297
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1298 KLLEEVEGNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLASplKKTKLDSASDNIIQEYVTLRTKYSELMTLTSQ 1377
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA--KINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1378 YIKFITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQK---------------------QLAEVHAKAIAKAEKEAQ 1436
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRggraveevlkasiqgvhgtvaQLGSVGERYATAIEVAAG 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1437 ElklRMQEEVnrREDAVVDAE-----KQK----------HNIQLELHELKNLSEQQIMDKSKQV---DDALQSRVK---- 1494
Cdd:TIGR02169 547 N---RLNNVV--VEDDAVAKEaiellKRRkagratflplNKMRDERRDLSILSEDGVIGFAVDLvefDPKYEPAFKyvfg 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1495 -------IEEEIRL---IRL-QLETTVKQKSTA------------------ESELKQLRDRAAEAEKLRKAAQEEAEKLR 1545
Cdd:TIGR02169 622 dtlvvedIEAARRLmgkYRMvTLEGELFEKSGAmtggsraprggilfsrsePAELQRLRERLEGLKRELSSLQSELRRIE 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1546 KQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIqvAHVAAQKSAAAELQs 1625
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE--ARIEELEEDLHKLE- 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1626 khmsfvEKTSKLEESLKQEHgaVLQLQHEAAALKKQqedaeraREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQE 1705
Cdd:TIGR02169 779 ------EALNDLEARLSHSR--IPEIQAELSKLEEE-------VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1706 DAEKQKEEAERE---AKKRAKAEDSALKQKEMAENELerqrkvaestaqqkltaEQELIRLRADFDNAEQQRSLLEDELY 1782
Cdd:TIGR02169 844 DLKEQIKSIEKEienLNGKKEELEEELEELEAALRDL-----------------ESRLGDLKKERDELEAQLRELERKIE 906
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1783 RLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAE---KETMSNSERSKQLLEVEAtKMRDLaeEASKLRAIAEEAK 1859
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipEEELSLEDVQAELQRVEE-EIRAL--EPVNMLAIQEYEE 983
|
810 820 830
....*....|....*....|....*....|....*...
gi 1927222982 1860 HQRQVAEEEAARQRAEAERilKEKLAAISDATRLKTEA 1897
Cdd:TIGR02169 984 VLKRLDELKEKRAKLEEER--KAILERIEEYEKKKREV 1019
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2294-2620 |
3.42e-13 |
|
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: 76.32 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2294 DKDNTQKFLAKEADNMKKLAEDAARlsveaqEAARLRQIAEDD------LNQQRALADKMLKEKMQAIQEASRLRAEA-- 2365
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAR------EVERRRKLEEAEkarqaeMDRQAAIYAEQERMAMERERELERIRQEErk 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2366 -EMLQ-RQKDLAQEQAQ-KLLEDKQLMQQRldeETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKaQEEAKKF 2442
Cdd:pfam17380 360 rELERiRQEEIAMEISRmRELERLQMERQQ---KNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE-QEEARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2443 KKQADSiASRLHETELATQEKMTVVEKLEVARltsSKEADDLRKAIaDLEKEKsRLKKEAEDLQNK--SKEMADAQQKQI 2520
Cdd:pfam17380 436 EVRRLE-EERAREMERVRLEEQERQQQVERLR---QQEEERKRKKL-ELEKEK-RDRKRAEEQRRKilEKELEERKQAMI 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2521 EHEKtvlqQTFLSEKEMLLkkeklieeekkRLESQFEEEVKKakalKDEQERQKQQMEDEKKKLQATMDAALNKQK---- 2596
Cdd:pfam17380 510 EEER----KRKLLEKEMEE-----------RQKAIYEEERRR----EAEEERRKQQEMEERRRIQEQMRKATEERSrlea 570
|
330 340
....*....|....*....|....*
gi 1927222982 2597 -EAEKEMhnkQKEMKELERKRLEQE 2620
Cdd:pfam17380 571 mEREREM---MRQIVESEKARAEYE 592
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1702-2629 |
5.07e-13 |
|
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: 76.24 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1702 LAQEDAEKQKEEAEREAKKRAKAEDSALK-----QKEMAENELERQrkVAESTAQQKLTAEQELIRLRADFDNAEQQRSL 1776
Cdd:TIGR00606 165 LSEGKALKQKFDEIFSATRYIKALETLRQvrqtqGQKVQEHQMELK--YLKQYKEKACEIRDQITSKEAQLESSREIVKS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1777 LEDELYRLKNevvaaqqQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAE 1856
Cdd:TIGR00606 243 YENELDPLKN-------RLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1857 EAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEI---ALKEKEAENERLRRQAEDEAYQRKALEDQanqhk 1933
Cdd:TIGR00606 316 EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqeHIRARDSLIQSLATRLELDGFERGPFSER----- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1934 qQIEEKIVLLKKSSEAEMERQRAIVDD-----TLKQRRVVEEEIRILKLNfEKASSGKLDLELELNKLKNIAEETQQ--- 2005
Cdd:TIGR00606 391 -QIKNFHTLVIERQEDEAKTAAQLCADlqskeRLKQEQADEIRDEKKGLG-RTIELKKEILEKKQEELKFVIKELQQleg 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2006 SKLRAEEEAEKLRKLALEEEKRRREAEEKVKKiaaaeeeaARQRQAAQDELDRLKKKAEEARKQKD-DADKEAEKQILMA 2084
Cdd:TIGR00606 469 SSDRILELDQELRKAERELSKAEKNSLTETLK--------KEVKSLQNEKADLDRKLRKLDQEMEQlNHHTTTRTQMEML 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2085 qqaAQKCSAAEQQVQSVLAQQKEDTIMQT-------KLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAA 2157
Cdd:TIGR00606 541 ---TKDKMDKDEQIRKIKSRHSDELTSLLgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2158 EQEAANQAKA----------QEDAERLRKEAEfEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKV 2227
Cdd:TIGR00606 618 EEQLSSYEDKlfdvcgsqdeESDLERLKEEIE-KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEF 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2228 KLKLDET-----DKQKSvLDEELQRLKDEVDDA-VKQRGQVEEELLKVKvQMEELLKLKLRIEEENQRLikKDKDNTQKF 2301
Cdd:TIGR00606 697 ISDLQSKlrlapDKLKS-TESELKKKEKRRDEMlGLAPGRQSIIDLKEK-EIPELRNKLQKVNRDIQRL--KNDIEEQET 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2302 LAKEADNMKKLAEDA-------ARLSVEAQEAAR--LRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQK 2372
Cdd:TIGR00606 773 LLGTIMPEEESAKVCltdvtimERFQMELKDVERkiAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLI 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2373 DLAQEQAQKLledkqlmQQRLDE-ETEEYQKSLEAERKRQLE-----IIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQA 2446
Cdd:TIGR00606 853 QDQQEQIQHL-------KSKTNElKSEKLQIGTNLQRRQQFEeqlveLSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2447 DSIASRLHETELATQEKMTVVEKlEVARLTSSKEadDLRKAIADlEKEKSRLKKEAE-DLQNKSKEMADAQQKQIEHEKT 2525
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIKE-KVKNIHGYMK--DIENKIQD-GKDDYLKQKETElNTVNAQLEECEKHQEKINEDMR 1001
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2526 VLQQTFLSEKEMLLKKEKLIEEEKKRLESQfEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNK 2605
Cdd:TIGR00606 1002 LMRQDIDTQKIQERWLQDNLTLRKRENELK-EVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGY 1080
|
970 980
....*....|....*....|....
gi 1927222982 2606 QKEMKELERKRLEQERILAEENQK 2629
Cdd:TIGR00606 1081 EKEIKHFKKELREPQFRDAEEKYR 1104
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1806-2527 |
5.12e-13 |
|
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: 76.03 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1806 RSEMDVLIQLKSKAEKETMSNSERSKQLL---EVEATKMRDLAEEASKLR-AIAEEA-------KHQRQVAEEEAARQRA 1874
Cdd:pfam12128 205 ILEDDGVVPPKSRLNRQQVEHWIRDIQAIagiMKIRPEFTKLQQEFNTLEsAELRLShlhfgykSDETLIASRQEERQET 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1875 EAE-----RILKEKLAAISDATRL-KTEAEIALKEKEAENERLRRQA----EDEAYQRKALEDQANQHKQQIEEkivlLK 1944
Cdd:pfam12128 285 SAElnqllRTLDDQWKEKRDELNGeLSAADAAVAKDRSELEALEDQHgaflDADIETAAADQEQLPSWQSELEN----LE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1945 KSSEAEMERQRAIVD--DTLKQRRVVEEEIRILKLN------FEKASSGKLDLELELNKLKN-IAEETQQSKLRAEEEAE 2015
Cdd:pfam12128 361 ERLKALTGKHQDVTAkyNRRRSKIKEQNNRDIAGIKdklakiREARDRQLAVAEDDLQALESeLREQLEAGKLEFNEEEY 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2016 KLrKLALEEEKRRREAEEKvkkiaaaEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKE---AEKQILMAQQAAQKCS 2092
Cdd:pfam12128 441 RL-KSRLGELKLRLNQATA-------TPELLLQLENFDERIERAREEQEAANAEVERLQSElrqARKRRDQASEALRQAS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2093 AAEQQVQSVLAQQKEDTIMQTKLKEEYekakkLAKQAEAAKEKAEREAA---LLRQ----QAEEAERQKAAAEQEAANQA 2165
Cdd:pfam12128 513 RRLEERQSALDELELQLFPQAGTLLHF-----LRKEAPDWEQSIGKVISpelLHRTdldpEVWDGSVGGELNLYGVKLDL 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2166 KAQEDAERLRKEAEFEAaKRAQAENAAlkqkqqaDAEMAKHKKLAEQTLKQKFQVEQ---ELTKVKLKLDETDKQKSVLD 2242
Cdd:pfam12128 588 KRIDVPEWAASEEELRE-RLDKAEEAL-------QSAREKQAAAEEQLVQANGELEKasrEETFARTALKNARLDLRRLF 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2243 EELQRLKDEVDDAVKQR-GQVEEELLKVKVQMEELL-KLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAE-DAARL 2319
Cdd:pfam12128 660 DEKQSEKDKKNKALAERkDSANERLNSLEAQLKQLDkKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALlKAAIA 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2320 SVEAQEAARLRQIAEDdlnQQRALADKMLKEkmqaiQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEE 2399
Cdd:pfam12128 740 ARRSGAKAELKALETW---YKRDLASLGVDP-----DVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPR 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2400 YQKSLEAERKRQLEIiaeseklklqVSQLSEAQAKAQEEAKKFKKQADSIASRLHETElatqEKMTVVeKLEVARLTSSK 2479
Cdd:pfam12128 812 LATQLSNIERAISEL----------QQQLARLIADTKLRRAKLEMERKASEKQQVRLS----ENLRGL-RCEMSKLATLK 876
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1927222982 2480 EADDlrkaIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVL 2527
Cdd:pfam12128 877 EDAN----SEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVI 920
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2056-2589 |
5.28e-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: 75.93 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2056 LDRLKKKAEEARKQKDDADKEAEKQILMAQqaAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEK 2135
Cdd:pfam15921 326 VSQLRSELREAKRMYEDKIEELEKQLVLAN--SELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2136 AEREAA------LLRQQAEEAERQkaaaeqeaanqakaQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKL 2209
Cdd:pfam15921 404 WDRDTGnsitidHLRRELDDRNME--------------VQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQ 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2210 AEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVD----DAVKQRGQVE---EELLKVKVQMEELLKLKlr 2282
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEatnaEITKLRSRVDlklQELQHLKNEGDHLRNVQ-- 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2283 IEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQ-EAARLrqiaEDDLNQQRALAD--KMLKEKMQA----- 2354
Cdd:pfam15921 548 TECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKAQL----EKEINDRRLELQefKILKDKKDAkirel 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2355 --------IQEASRLRAEAEMLQRQKDLAQEQAQkLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQvs 2426
Cdd:pfam15921 624 earvsdleLEKVKLVNAGSERLRAVKDIKQERDQ-LLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ-- 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2427 qLSEAQAKAQEEAKKFKKQADSIAsrlHETELAT-QEKMTVVEKLEVARLTSSKEAddLRKAIADLEKEKSRLKKEAEDL 2505
Cdd:pfam15921 701 -LKSAQSELEQTRNTLKSMEGSDG---HAMKVAMgMQKQITAKRGQIDALQSKIQF--LEEAMTNANKEKHFLKEEKNKL 774
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2506 QNKSKEMADAQQKQI-EHEKTVLQQTFLSEKemllkkeklieeeKKRLESQFEEEVKKAKALKDEQERQKQqmEDEKKKL 2584
Cdd:pfam15921 775 SQELSTVATEKNKMAgELEVLRSQERRLKEK-------------VANMEVALDKASLQFAECQDIIQRQEQ--ESVRLKL 839
|
....*
gi 1927222982 2585 QATMD 2589
Cdd:pfam15921 840 QHTLD 844
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2360-2644 |
5.46e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2360 RLRAEAEMLQRQKDLAQEQAQKLledKQLMQQRldEETEEYQKSLEAERKRQLEIIAeseklkLQVSQLSEAQAKAQEEA 2439
Cdd:COG1196 180 KLEATEENLERLEDILGELERQL---EPLERQA--EKAERYRELKEELKELEAELLL------LKLRELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2440 KKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQ 2519
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2520 IEHEKTVLQQTFLSEKEmllkkEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAE 2599
Cdd:COG1196 329 EEELEELEEELEELEEE-----LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1927222982 2600 KEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQ 2644
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2054-2649 |
7.62e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.49 E-value: 7.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2054 DELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAK 2133
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2134 EK---AEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEaefeaakraqaenaaLKQKQQADAEMAKHKKLA 2210
Cdd:PRK03918 238 EEieeLEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE---------------LKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2211 EQTLKQKFQVEQELTKVKLKLDETDKQKsvldEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKlRIEEENQRL 2290
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2291 IKKDKDNTQKFLAKEADNMKKlaedaARLSVEAqeaarlrqiAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQR 2370
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEK-----AKEEIEE---------EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2371 QkdLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEA--ERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADS 2448
Cdd:PRK03918 444 E--LTEEHRKELLEEYTAELKRIEKELKEIEEKERKlrKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELE 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2449 IASRLHET---ELATQEKMTVVEKLEVARLTS-SKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIE--- 2521
Cdd:PRK03918 522 KKAEEYEKlkeKLIKLKGEIKSLKKELEKLEElKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEpfy 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2522 ----------HEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESqFEEEVKKAKALKDEQE-----RQKQQMEDEKKKLQA 2586
Cdd:PRK03918 602 neylelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEE-LRKELEELEKKYSEEEyeelrEEYLELSRELAGLRA 680
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 2587 TMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERI--LAEENQKLREKLQQLEEAQKDQPDKEV 2649
Cdd:PRK03918 681 ELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLekALERVEELREKVKKYKALLKERALSKV 745
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2765-2802 |
8.43e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.04 E-value: 8.43e-13
10 20 30
....*....|....*....|....*....|....*...
gi 1927222982 2765 LLEAQAATGSILDPIKNQKLSVNEAVKEGVIGPELHNK 2802
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
197-297 |
1.35e-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: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 197 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAErDLGVTRLLDP 276
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1927222982 277 ED-VDVPHPDEKSIITYVSSLY 297
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2144-2461 |
1.38e-12 |
|
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: 74.39 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2144 RQQAEEAERQKAAAEQEAANQaKAQEdAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKL----AEQTLKQKFQ 2219
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEE-KARE-VERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELerirQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2220 VEQELTKVKL-KLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIkkdkdnt 2298
Cdd:pfam17380 365 IRQEEIAMEIsRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV------- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2299 QKFLAKEADNMKKLAEDAARlsvEAQEAARLRQIAEDdlNQQRALADKMLKEKMQAIQEASRLRAEAEMLQR-QKDLAQE 2377
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQE---RQQQVERLRQQEEE--RKRKKLELEKEKRDRKRAEEQRRKILEKELEERkQAMIEEE 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2378 QAQKLLEDKQLMQQRLDEETEEYQKSlEAERKRQLEiIAESEKLKLQVSQLSEAQAK--AQEEAKKFKKQADSIASRLHE 2455
Cdd:pfam17380 513 RKRKLLEKEMEERQKAIYEEERRREA-EEERRKQQE-MEERRRIQEQMRKATEERSRleAMEREREMMRQIVESEKARAE 590
|
....*.
gi 1927222982 2456 TELATQ 2461
Cdd:pfam17380 591 YEATTP 596
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
655-844 |
1.41e-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: 70.17 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 655 LHAFVSAATKELMWLNDKEEEEVNFDWSDRNSNMTAKKDNYSGLMRELELREKKVNDIQATGDKLVRDGHPGKKTVESFT 734
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 735 AALQTQWSWILQLCCCIEAHLKENTAYYQFFADVKEAQDKMKKMQENMKkkySCDRSTTATRLEDLLQDAVEEREQLNEF 814
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|
gi 1927222982 815 KTLATGLNKRAKSIIQLKPRNPTHSIKGKL 844
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
65-176 |
1.41e-12 |
|
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: 67.06 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 65 ERDRvQKKTFTKWVNKhlIKSQRQVTDLYEDLRDGhnLIsLLEVLSGeTLPRERDVVRSVRLPREKGRMRFHKLQNVQIA 144
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDG--LI-LLQAYDK-VIPGSVNWKKVNKAPASAEISRFKAVENTNYA 76
|
90 100 110
....*....|....*....|....*....|..
gi 1927222982 145 LDFLKHRQVKLVNIRNDDIADGNPKLTLGLIW 176
Cdd:cd21300 77 VELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1714-1916 |
1.47e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.87 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1714 AEREAKKRAKAEDSALKQK-EMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQ 1792
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1793 QQRKQLEDELAKV---------RSEMDVLiqLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQR- 1862
Cdd:COG4942 97 AELEAQKEELAELlralyrlgrQPPLALL--LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERa 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222982 1863 --QVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAE 1916
Cdd:COG4942 175 elEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
72-185 |
2.11e-12 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 66.49 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 72 KTFTKWVNKHLIKSQrqVTDLYEDLRDGHNLISLLEVLSGETLPRERdvvrsVRLPREKGRMRFHKLQNVQIALDFLKHR 151
Cdd:cd21298 9 KTYRNWMNSLGVNPF--VNHLYSDLRDGLVLLQLYDKIKPGVVDWSR-----VNKPFKKLGANMKKIENCNYAVELGKKL 81
|
90 100 110
....*....|....*....|....*....|....
gi 1927222982 152 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 185
Cdd:cd21298 82 KFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4344-4382 |
2.30e-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: 2.30e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1927222982 4344 LLEAQACTGGIIDPTTGERFSVTDATEKGLVDKVMVDRL 4382
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1379-2004 |
2.31e-12 |
|
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: 74.10 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1379 IKFITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEK 1458
Cdd:pfam12128 137 NLLNTREYRSIIQNDRTLLGRERVELRSLARQFALCDSESPLRHIDKIAKAMHSKEGKFRDVKSMIVAILEDDGVVPPKS 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1459 QKHNIQLE--LHELKNLseQQIMDKSKQVDdalqsrvKIEEEIRlirlQLETTVKQKSTAESELKQLRDRAAEAEKLRKA 1536
Cdd:pfam12128 217 RLNRQQVEhwIRDIQAI--AGIMKIRPEFT-------KLQQEFN----TLESAELRLSHLHFGYKSDETLIASRQEERQE 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1537 AQEEAEKLRKQVNEETQKKRmaeEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQvAHVAAQ 1616
Cdd:pfam12128 284 TSAELNQLLRTLDDQWKEKR---DELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQ-SELENL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1617 KSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQqedaerareeaekelEKWRQKAN-----EALRLRL 1691
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIRE---------------ARDRQLAVaeddlQALESEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1692 QAEEEAHKKSLaqEDAEKQKEEAEREAKKR---AKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFD 1768
Cdd:pfam12128 425 REQLEAGKLEF--NEEEYRLKSRLGELKLRlnqATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRD 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1769 NAEQQRSLLEDELYRLKNEVVAAQQQ------------RKQL---EDELAKVRSEmdvliQLKSKAEKETMSNSERSKQL 1833
Cdd:pfam12128 503 QASEALRQASRRLEERQSALDELELQlfpqagtllhflRKEApdwEQSIGKVISP-----ELLHRTDLDPEVWDGSVGGE 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1834 LEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRR 1913
Cdd:pfam12128 578 LNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRR 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1914 QAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRvveeEIRILKLNFEKASSGKLDLELEL 1993
Cdd:pfam12128 658 LFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKR----EARTEKQAYWQVVEGALDAQLAL 733
|
650
....*....|.
gi 1927222982 1994 NKLKNIAEETQ 2004
Cdd:pfam12128 734 LKAAIAARRSG 744
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1201-2021 |
3.24e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 73.46 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1201 ATAVSDKMSRVHSERDAELDHYRQLLSSLQDRWKAVFSQIDLRQRELEQLGRQLGYYRESYDWLIRWINDAKQRQEKIQA 1280
Cdd:TIGR00618 182 ALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1281 vtitdsktLKEQLAQEKKL---LEEVEGNKDKVDECQKYAKayidtikdyelqLVAYKAQVEPLasplkktkldsaSDNI 1357
Cdd:TIGR00618 262 --------LKQLRARIEELraqEAVLEETQERINRARKAAP------------LAAHIKAVTQI------------EQQA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1358 IQEYVTLRTKYSELMTLTSQYIKFITDS-----QRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAE-VHAKAIAKA 1431
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQssieeQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1432 EKEAQELKLRMQEEVNRREDAVVDAEKQKHNI--QLELHELKNLSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETt 1509
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRTSAFRDlqGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL- 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1510 vKQKSTAESELKQLRDRAAeaeklRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQ 1589
Cdd:TIGR00618 469 -KEREQQLQTKEQIHLQET-----RKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLET 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1590 AEEAERQVKQAEIEkerqiqvaHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQedaerar 1669
Cdd:TIGR00618 543 SEEDVYHQLTSERK--------QRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE------- 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1670 eeaekelekwRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAEST 1749
Cdd:TIGR00618 608 ----------DMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLAS 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1750 AQQKLTAEQELIR-LRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKEtmsnse 1828
Cdd:TIGR00618 678 RQLALQKMQSEKEqLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ------ 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1829 rskqlleveatkmrdlAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKlaaisdaTRLKTEAEIALKEKEAEN 1908
Cdd:TIGR00618 752 ----------------ARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFF-------NRLREEDTHLLKTLEAEI 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1909 ERLRRQAED--EAYQRKALEDQANQHkQQIEEKIVLLkksseAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSgk 1986
Cdd:TIGR00618 809 GQEIPSDEDilNLQCETLVQEEEQFL-SRLEEKSATL-----GEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG-- 880
|
810 820 830
....*....|....*....|....*....|....*
gi 1927222982 1987 ldleleLNKLKNIAEETQQSKLRAEEEAEKLRKLA 2021
Cdd:TIGR00618 881 ------INQIKIQFDGDALIKFLHEITLYANVRLA 909
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3168-3206 |
5.94e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.73 E-value: 5.94e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1927222982 3168 LLDAQMATGGIIDPVNSHHIPHDVACKRNYFDDEMKQNL 3206
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1420-1882 |
6.28e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.11 E-value: 6.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1420 LAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELKNLSEQQimdkskqvDDALQSRVKIEEEI 1499
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEL--------EELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1500 RLIR--LQLETTVKQKSTAESELKQLRDRA----------AEAEKLRKAAQEEAEKLRKQVNEETQKKR-MAEEELKRKA 1566
Cdd:COG4717 119 EKLEklLQLLPLYQELEALEAELAELPERLeeleerleelRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1567 EAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQK------SAAAELQSKHMSFVEKTSKLEES 1640
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1641 LkQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQ--------EDAEKQKE 1712
Cdd:COG4717 279 L-FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLElldrieelQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1713 EAEREAK-KRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELI--RLRADFDNAEQQ-----RSLLEDELYRL 1784
Cdd:COG4717 358 ELEEELQlEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELeeQLEELLGELEELlealdEEELEEELEEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1785 KNEVVAAQQQRKQLEDELAKVRSEMDVLiqlkskaekETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEE-AKHQRQ 1863
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQL---------EEDGELAELLQELEELKAELRELAEEWAALKLALELlEEAREE 508
|
490
....*....|....*....
gi 1927222982 1864 VAEEEAARQRAEAERILKE 1882
Cdd:COG4717 509 YREERLPPVLERASEYFSR 527
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1520-2021 |
6.37e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.38 E-value: 6.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1520 LKQLRDRAAEA----EKLRKAAQEEAEKLRKQVNEETQK---KRMAEEELKRKAEAekeaakqkqkalEDLENLKRQAEE 1592
Cdd:PRK02224 164 LEEYRERASDArlgvERVLSDQRGSLDQLKAQIEEKEEKdlhERLNGLESELAELD------------EEIERYEEQREQ 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1593 AERQVKQAE--IEKERQIQvAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALkkqqedaerare 1670
Cdd:PRK02224 232 ARETRDEADevLEEHEERR-EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL------------ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1671 EAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQE--DAEKQKEEAEREAKKRAKAEDSALKQKEMA---ENELERQRKV 1745
Cdd:PRK02224 299 LAEAGLDDADAEAVEARREELEDRDEELRDRLEECrvAAQAHNEEAESLREDADDLEERAEELREEAaelESELEEAREA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1746 AESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRsemdvliqlKSKAEKETM- 1824
Cdd:PRK02224 379 VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR---------ERVEEAEALl 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1825 --SNSERSKQLLE----VEATKMRDlaEEASKLRAIAEEAKHQRQVAEE--EAARQRAEAERILKEKLAAISDATRLKTE 1896
Cdd:PRK02224 450 eaGKCPECGQPVEgsphVETIEEDR--ERVEELEAELEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDLEELIAE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1897 AEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLkksseAEMERQRAIVDDTLKQRRVVEEEirilk 1976
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV-----AELNSKLAELKERIESLERIRTL----- 597
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1927222982 1977 lnFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLA 2021
Cdd:PRK02224 598 --LAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELE 640
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
88-179 |
7.39e-12 |
|
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: 64.92 E-value: 7.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 88 QVTDLYEDLRDGHNLISLLEVLSGETLPRERDVVRSVRLPRekgrmrfhKLQNVQIALDFLKHRQV----KLVNIRNDDI 163
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVPAISRLQ--------KLHNVEVALKALKEAGVlrggDGGGITAKDI 96
|
90
....*....|....*.
gi 1927222982 164 ADGNPKLTLGLIWTII 179
Cdd:cd21223 97 VDGHREKTLALLWRII 112
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1056-2015 |
8.18e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 72.31 E-value: 8.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1056 VEKEPLKECVQKTTEQKKVQVELEGLKKDLNKVSAKTKEVLASPQQTAsapvlrsELDLTVEKMdhthmlssVYLEKLKT 1135
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE-------KLELEEEYL--------LYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1136 VEMVIRNTQgaegvlkqyedclrevhtvpndvKEVETYRTKLKKMRAEAEGEQPVFDSLEAELKKATAVSDKMSRVHSER 1215
Cdd:pfam02463 235 NEERIDLLQ-----------------------ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1216 DAELDHYRQLLSSLQDRWKAVFSQIDLRQRELEQLGRQLGYYRESYdwlirwinDAKQRQEKIQAVTITDSKTLKEQLAQ 1295
Cdd:pfam02463 292 AKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI--------EELEKELKELEIKREAEEEEEEELEK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1296 EKKLLEEVEgnKDKVDECQKYAKAYIDTIKDYELQLvaykaqvEPLASPLKKTKLDSASDNIIQEYVTLRTKYSELMTLT 1375
Cdd:pfam02463 364 LQEKLEQLE--EELLAKKKLESERLSSAAKLKEEEL-------ELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1376 SQyiKFITDSQRRLEDEEKAAEKLKAEEQKKMAM-MQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVV 1454
Cdd:pfam02463 435 EE--ESIELKQGKLTEEKEELEKQELKLLKDELElKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1455 DAEKQKHN---IQLELHELKNLSEQQIMDKSKQ--VDDALQSRVKIEEEIRLIRLQLET---TVKQKSTAESELKQLRDR 1526
Cdd:pfam02463 513 LALIKDGVggrIISAHGRLGDLGVAVENYKVAIstAVIVEVSATADEVEERQKLVRALTelpLGARKLRLLIPKLKLPLK 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1527 AAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKER 1606
Cdd:pfam02463 593 SIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELT 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1607 QIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQedaerareeaekeLEKWRQKANEA 1686
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQ-------------EAQDKINEELK 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1687 LRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTaqqkLTAEQELIRLRAD 1766
Cdd:pfam02463 740 LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE----LRALEEELKEEAE 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1767 FDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMdvliqLKSKAEKETMSNSERSKQLLEVEATKMRDLAE 1846
Cdd:pfam02463 816 LLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELER-----LEEEITKEELLQELLLKEEELEEQKLKDELES 890
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1847 EASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALE 1926
Cdd:pfam02463 891 KEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKE 970
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1927 DQANQHKQQIEEKIVLLKKSSEAEMERQRAivddTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQS 2006
Cdd:pfam02463 971 ELGKVNLMAIEEFEEKEERYNKDELEKERL----EEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSA 1046
|
....*....
gi 1927222982 2007 KLRAEEEAE 2015
Cdd:pfam02463 1047 ELRLEDPDD 1055
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1909-2640 |
8.40e-12 |
|
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: 72.07 E-value: 8.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1909 ERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKS------SEAEMERQRAIVDDTLKQRRVVEEEIRilklnfeka 1982
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSvidlqtKLQEMQMERDAMADIRRRESQSQEDLR--------- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1983 ssgkldlelelNKLKNIAEETQQSKLRAEE-------EAEKLRKLALEEEKRRREaeekVKKIAAAEEEAARQRQAAQDE 2055
Cdd:pfam15921 145 -----------NQLQNTVHELEAAKCLKEDmledsntQIEQLRKMMLSHEGVLQE----IRSILVDFEEASGKKIYEHDS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2056 LDRL--KKKAEEARKQKDDADKEA---EKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEkAKKLAKQAE 2130
Cdd:pfam15921 210 MSTMhfRSLGSAISKILRELDTEIsylKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE-ITGLTEKAS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2131 AAKEKAEREAALLRQQAEEAERQKAAAEQEAAnqaKAQEDAERLRkeAEFEAAKRAQAENAALKQKQQ--ADAEMAKHKK 2208
Cdd:pfam15921 289 SARSQANSIQSQLEIIQEQARNQNSMYMRQLS---DLESTVSQLR--SELREAKRMYEDKIEELEKQLvlANSELTEART 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2209 LAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKD--------------EVDD-------------AVKQ--R 2259
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsitidhlrrELDDrnmevqrleallkAMKSecQ 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2260 GQVEEELLKVKVQMEELLK---LKLRIEEENQRLIKKDKDNTQKFLAKEadNMKKLAEDaarLSVEAQEAARLRQIAEDD 2336
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKvssLTAQLESTKEMLRKVVEELTAKKMTLE--SSERTVSD---LTASLQEKERAIEATNAE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2337 LNQQRALADKMLKEKMQAIQEASRLR---AEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEyQKSLEAErKRQLE 2413
Cdd:pfam15921 519 ITKLRSRVDLKLQELQHLKNEGDHLRnvqTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRT-AGAMQVE-KAQLE 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2414 IIAESEKLKLQVSQLseaqAKAQEEAKKFKKQADSIASRLHETEL--ATQEKMTVVEKLEVARLTSSKEADDLRKAIADL 2491
Cdd:pfam15921 597 KEINDRRLELQEFKI----LKDKKDAKIRELEARVSDLELEKVKLvnAGSERLRAVKDIKQERDQLLNEVKTSRNELNSL 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2492 EKEKSRLKKeaeDLQNKSKEMADAQQK---QIEHEKTVLQQTFLSEKEMllkkeklieeekkrlESQFEEEVKKAKALKD 2568
Cdd:pfam15921 673 SEDYEVLKR---NFRNKSEEMETTTNKlkmQLKSAQSELEQTRNTLKSM---------------EGSDGHAMKVAMGMQK 734
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 2569 EQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKEL-----ERKRLEQE-RILAEENQKLREKLQQLEEA 2640
Cdd:pfam15921 735 QITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELstvatEKNKMAGElEVLRSQERRLKEKVANMEVA 812
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3994-4032 |
8.53e-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: 8.53e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1927222982 3994 LLEAQAATGYVIDPIKNLKLTVSEAVRMGIVGPEFKDKL 4032
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1867-2504 |
1.29e-11 |
|
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: 71.29 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1867 EEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEekivLLKKS 1946
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCN----LLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1947 SEAEMERQRAIVDDTLKQRRV---VEEEIRILKLNFEKASSGKLDLELELN-KLKNIAEETQQSKLRAEEEAEKLRKLAL 2022
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVymdLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQVS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2023 EEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVL 2102
Cdd:pfam05483 244 LLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAT 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2103 AQQKEDTIMQTKLKEEYEKAKK----LAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLR--K 2176
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAahsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKnnK 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2177 EAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTL-----------------------------KQKFQVEQELTKV 2227
Cdd:pfam05483 404 EVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELifllqarekeihdleiqltaiktseehylKEVEDLKTELEKE 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2228 KLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKlKLRIEEENQRLIKKDKDNTQKFLAKEAD 2307
Cdd:pfam05483 484 KLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK-QIENLEEKEMNLRDELESVREEFIQKGD 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2308 NMK----KLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLL 2383
Cdd:pfam05483 563 EVKckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLE 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2384 EDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAK-----------KFKKQADSIA-- 2450
Cdd:pfam05483 643 LELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhkiaemvalmeKHKHQYDKIIee 722
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222982 2451 --SRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAED 2504
Cdd:pfam05483 723 rdSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2054-2644 |
1.40e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2054 DELDRLKKKAEEARKQKD---DADKEAEKqilmAQQAAQKCSAAEQQVQSVLAQQKEDTImqTKLKEEYEKAKKLAKQAE 2130
Cdd:COG4913 235 DDLERAHEALEDAREQIEllePIRELAER----YAAARERLAELEYLRAALRLWFAQRRL--ELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2131 AAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQ-EDAERLRKEAEfeaAKRAQAENAALKQKQQADAEMAKHKKL 2209
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGNGGDRLEQLEREiERLERELEERE---RRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2210 AEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLK--------- 2280
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDeaelpfvge 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2281 ---LRIEEEN-----QRLIkkdkdNTQKF--LAKEADnmkklaEDAARLSVEA-QEAARLR--QIAEDDLNQQR-ALADK 2346
Cdd:COG4913 466 lieVRPEEERwrgaiERVL-----GGFALtlLVPPEH------YAAALRWVNRlHLRGRLVyeRVRTGLPDPERpRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2347 MLKEKMQAiqEASRLRAEAEM-LQRQKDLAQ-EQAQKL-LEDKQLMQQRL-------------DEETEEYQKSLEAERKR 2410
Cdd:COG4913 535 SLAGKLDF--KPHPFRAWLEAeLGRRFDYVCvDSPEELrRHPRAITRAGQvkgngtrhekddrRRIRSRYVLGFDNRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2411 QlEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIA--SRLHETELATQEKMTVVEKLEVAR---LTSSKEADDLR 2485
Cdd:COG4913 613 A-ALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELerlDASSDDLAALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2486 KAIADLEKEKSRLKKEAEDLQNKSKEmADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKA 2565
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2566 LKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELER--KRLEQERiLAEENQKLREKLQQLEEAQKD 2643
Cdd:COG4913 771 LEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLAllDRLEEDG-LPEYEERFKELLNENSIEFVA 849
|
.
gi 1927222982 2644 Q 2644
Cdd:COG4913 850 D 850
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1896-2531 |
1.67e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.84 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1896 EAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVL---LKKSSE--AEMERQRAIVDDTLKQRRVVEE 1970
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLeaeIEDLREtiAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1971 EIR------ILKLNFEKASSGKL-----DLELELNKLKNIAEETQQSKLRAEEEAEKLRklaleeekrrreaeekvkkia 2039
Cdd:PRK02224 290 ELEeerddlLAEAGLDDADAEAVearreELEDRDEELRDRLEECRVAAQAHNEEAESLR--------------------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2040 aaeeeaarqrqaaqDELDRLKKKAEEARKQKDDADKEAEkqilmaqqaaqkcsAAEQQVQSVLAQQKEdtimqtkLKEEY 2119
Cdd:PRK02224 349 --------------EDADDLEERAEELREEAAELESELE--------------EAREAVEDRREEIEE-------LEEEI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2120 EKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRkeaefEAAKRAQaenaalkqkqqa 2199
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL-----EAGKCPE------------ 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2200 daemakhkklAEQTLKQKFQVEqeltkvklKLDETDKQKSVLDEELQRLKDEVDDaVKQRGQVEEELLKVKVQMEELLKL 2279
Cdd:PRK02224 457 ----------CGQPVEGSPHVE--------TIEEDRERVEELEAELEDLEEEVEE-VEERLERAEDLVEAEDRIERLEER 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2280 KLRIEE--ENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRAladkMLKEKMQAIQE 2357
Cdd:PRK02224 518 REDLEEliAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA----ELKERIESLER 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2358 ASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETeeyqksleaERKRQLEIiaeseklKLQVSQLSEAQAKaQE 2437
Cdd:PRK02224 594 IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR---------ERKRELEA-------EFDEARIEEARED-KE 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2438 EAKKFKKQADSIASRLHETELATQEKMTVVEklevarlTSSKEADDLRKAIADLEKEKSRLK---KEAEDLQNKSKEM-A 2513
Cdd:PRK02224 657 RAEEYLEQVEEKLDELREERDDLQAEIGAVE-------NELEELEELRERREALENRVEALEalyDEAEELESMYGDLrA 729
|
650
....*....|....*...
gi 1927222982 2514 DAQQKQIEHEKTVLQQTF 2531
Cdd:PRK02224 730 ELRQRNVETLERMLNETF 747
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
199-298 |
1.80e-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: 63.51 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 199 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMgRVYRQTN----LENLEQAFGVAER-DLGVTRL 273
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPK-INKKPKSpfkkRENINLFLNACKKlGLPELDL 79
|
90 100
....*....|....*....|....*
gi 1927222982 274 LDPEDVdVPHPDEKSIITYVSSLYD 298
Cdd:cd00014 80 FEPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1388-2019 |
1.91e-11 |
|
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: 70.91 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1388 RLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLeL 1467
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNL-L 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1468 HELKNLSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELK-QLRDRAAEAEKLRKAAQEEAEKLRK 1546
Cdd:pfam05483 161 KETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1547 QVN----EETQKK-RMAEEELKRKAEAEKEAAKQKQKALEDlENLKRQAEEAERQVKqaEIEKERQIQVAHVAAQKSAAA 1621
Cdd:pfam05483 241 QVSllliQITEKEnKMKDLTFLLEESRDKANQLEEKTKLQD-ENLKELIEKKDHLTK--ELEDIKMSLQRSMSTQKALEE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1622 ELQSKHMSFVEKTSKLEESLKQEHGAvlqlqHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKS 1701
Cdd:pfam05483 318 DLQIATKTICQLTEEKEAQMEELNKA-----KAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1702 LAQEDAEKQKEEAEREAKKRAKAEDSAL----KQKEMAENELE------------RQRKVAESTAQQKLTAEQELIRLRa 1765
Cdd:pfam05483 393 LEEMTKFKNNKEVELEELKKILAEDEKLldekKQFEKIAEELKgkeqelifllqaREKEIHDLEIQLTAIKTSEEHYLK- 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1766 dfdNAEQQRSLLEDElyRLKNEVVAAQQQRKQLEDElAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEA-----TK 1840
Cdd:pfam05483 472 ---EVEDLKTELEKE--KLKNIELTAHCDKLLLENK-ELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENleekeMN 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1841 MRDLAEEASK-LRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIA---LKEKEAENERLRRQAE 1916
Cdd:pfam05483 546 LRDELESVREeFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknIEELHQENKALKKKGS 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1917 DEAYQRKALEDQANQ-------HKQQIEE------KIVLLKKSSE----AEMERQRAIVDDTLKQR-------------- 1965
Cdd:pfam05483 626 AENKQLNAYEIKVNKlelelasAKQKFEEiidnyqKEIEDKKISEekllEEVEKAKAIADEAVKLQkeidkrcqhkiaem 705
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222982 1966 ------------RVVEE---EIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRK 2019
Cdd:pfam05483 706 valmekhkhqydKIIEErdsELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKM 774
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1801-2425 |
2.25e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1801 ELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAE--- 1877
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESleg 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1878 --RILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEdEAYQRKALEDQANQHKQQIEEKivllkkssEAEMERQR 1955
Cdd:PRK03918 253 skRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKR--------LSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1956 AIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLE---LELNKLKNIAEETQQ-SKLRAEEEAEKLRKLALEEEKRRREA 2031
Cdd:PRK03918 324 NGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2032 EEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAaqKCSAAEQQVQSVLAQQKEDTIM 2111
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTA--ELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2112 QTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAA--KRAQAE 2189
Cdd:PRK03918 482 LRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkKKLAEL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2190 NAALKQKQQADAEMakHKKLAEQTLKQKFQVEQELTKVK------LKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVE 2263
Cdd:PRK03918 562 EKKLDELEEELAEL--LKELEELGFESVEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2264 EELLKVKVQMEELlkLKLRIEEENQRLIKKdkdntqkflakeadnMKKLAEDAARLSVEAQEAARLRQIAEDDLnqqral 2343
Cdd:PRK03918 640 KRLEELRKELEEL--EKKYSEEEYEELREE---------------YLELSRELAGLRAELEELEKRREEIKKTL------ 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2344 adKMLKEKMQAIQEAsrlRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAE---RKRQ-LEIIAESE 2419
Cdd:PRK03918 697 --EKLKEELEEREKA---KKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASEIFEElteGKYSgVRVKAEEN 771
|
....*.
gi 1927222982 2420 KLKLQV 2425
Cdd:PRK03918 772 KVKLFV 777
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2143-2641 |
2.66e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2143 LRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRaqaenaalkQKQQADAEMAKHkklaEQTLKQKFQVEQ 2222
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE---------TRDEADEVLEEH----EERREELETLEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2223 ELTKVKLKLDETDKQKSVLDEELQ-------RLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEE--ENQRLIKK 2293
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRdlrerleELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrlEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2294 DKDNTQKFLAKEADNM----KKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQ 2369
Cdd:PRK02224 339 AHNEEAESLREDADDLeeraEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2370 RQKDLAQEQAQKLLEDKQLMQQRLDE-----------------ETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLS--- 2429
Cdd:PRK02224 419 EERDELREREAELEATLRTARERVEEaealleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEerl 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2430 ---EAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKL-----------EVARLTSSK---EADDLRKAIADLE 2492
Cdd:PRK02224 499 eraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELreraaeleaeaEEKREAAAEaeeEAEEAREEVAELN 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2493 KEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKR-LESQFEEE-VKKAKALKDEQ 2570
Cdd:PRK02224 579 SKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKReLEAEFDEArIEEAREDKERA 658
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222982 2571 ERQKQQMEDEKKKLQATMDAALNKQKEAEKEMhnkqkemKELERKRLEQERiLAEENQKLREKLQQLEEAQ 2641
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDLQAEIGAVENEL-------EELEELRERREA-LENRVEALEALYDEAEELE 721
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1424-1773 |
2.89e-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: 70.15 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1424 HAKAIAkaEKEAQELKLRMQEEVNRREDAVVDAEKQKHNiQLELHELknlSEQQIMDKSKQVDdALQSRVKIEEEIRLIR 1503
Cdd:pfam17380 280 HQKAVS--ERQQQEKFEKMEQERLRQEKEEKAREVERRR-KLEEAEK---ARQAEMDRQAAIY-AEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1504 LQLETTVKQ-KSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVnEETQKKRMAEEELKRKAEAEKEaakqkqkaleD 1582
Cdd:pfam17380 353 IRQEERKRElERIRQEEIAMEISRMRELERLQMERQQKNERVRQEL-EAARKVKILEEERQRKIQQQKV----------E 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1583 LENLKRQAEEA-ERQVKQAEIEKERQIQVAhvaaqksaaaelqskhmsfvektsKLEESLKQEHGAVLQLQHEAAALKKQ 1661
Cdd:pfam17380 422 MEQIRAEQEEArQREVRRLEEERAREMERV------------------------RLEEQERQQQVERLRQQEEERKRKKL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1662 QEDAERAREEAEKelEKWRQKANEALRLRLQA--EEEAHKKSLAQEDAEKQKEEAEREakKRAKAEDSALKQKEMAENE- 1738
Cdd:pfam17380 478 ELEKEKRDRKRAE--EQRRKILEKELEERKQAmiEEERKRKLLEKEMEERQKAIYEEE--RRREAEEERRKQQEMEERRr 553
|
330 340 350
....*....|....*....|....*....|....*..
gi 1927222982 1739 -LERQRKVAESTAQ-QKLTAEQELIRLRADFDNAEQQ 1773
Cdd:pfam17380 554 iQEQMRKATEERSRlEAMEREREMMRQIVESEKARAE 590
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1166-1981 |
3.04e-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: 70.48 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1166 DVKEVETYRTKLKKMRAEAEGEQPVFDSLEAELKKataVSDKMSRVHSERDaELDHYRQLLSSLQD-RWKAVFSQIDLRQ 1244
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEELEEVEENIERLDLIIDE---KRQQLERLRRERE-KAERYQALLKEKREyEGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1245 RELEQLGRQLGYYRESYDWLIRWINDAKQRQEKIQAVTITDSKTLK-----EQLAQEKKLLE---EVEGNKDKVDECQKY 1316
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeEQLRVKEKIGEleaEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1317 AKAYIDTIKDYELQLVAYKAQVEPLASPLKKTKLDSASdnIIQEYVTLRTKYSELmtltsqyikfitdsQRRLEDEEKAA 1396
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK--LTEEYAELKEELEDL--------------RAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1397 EKLKAEeqkkmammqaeldkqkqlaevhakaIAKAEKEAQELKLRMqEEVNRREDAVVDAEKQKHNIQLELH-ELKNLSE 1475
Cdd:TIGR02169 381 AETRDE-------------------------LKDYREKLEKLKREI-NELKRELDRLQEELQRLSEELADLNaAIAGIEA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1476 QQimdkskqvdDALQSRVK-IEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKL--RKQVNEET 1552
Cdd:TIGR02169 435 KI---------NELEEEKEdKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAeaQARASEER 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1553 QKKRMAEEELKRKAEAEKEAAKQKQKALED-----LE-----NLKRQAEEAERQVKQA-EIEKERQ-----------IQV 1610
Cdd:TIGR02169 506 VRGGRAVEEVLKASIQGVHGTVAQLGSVGEryataIEvaagnRLNNVVVEDDAVAKEAiELLKRRKagratflplnkMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1611 AHVAAQKSAAAELQSKHMSFVEKTSKLE-------------ESL------------------------------------ 1641
Cdd:TIGR02169 586 ERRDLSILSEDGVIGFAVDLVEFDPKYEpafkyvfgdtlvvEDIeaarrlmgkyrmvtlegelfeksgamtggsraprgg 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1642 ----KQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRL---------RLQAEEEAHKKSLAQEDAE 1708
Cdd:TIGR02169 666 ilfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiekeieQLEQEEEKLKERLEELEED 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1709 KQKEEAEREAKKRAKAEDSA--------LKQKEMAENELER---QRKVAESTAQ-QKLTAEQELIRLRADFDNAEQQRSL 1776
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEArieeleedLHKLEEALNDLEArlsHSRIPEIQAElSKLEEEVSRIEARLREIEQKLNRLT 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1777 LEDELyrLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKEtmsnserskqlLEVEATKMRDLAEEASKLRAIAE 1856
Cdd:TIGR02169 826 LEKEY--LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-----------LEELEAALRDLESRLGDLKKERD 892
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1857 EAKHQRQVAEEEaaRQRAEAERILKEKLAAisdatRLKTEAEiALKEKEAENERLRRQAEDEAYQRKALEDQAnQHKQQI 1936
Cdd:TIGR02169 893 ELEAQLRELERK--IEELEAQIEKKRKRLS-----ELKAKLE-ALEEELSEIEDPKGEDEEIPEEELSLEDVQ-AELQRV 963
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 1927222982 1937 EEKIVLLKK---SSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEK 1981
Cdd:TIGR02169 964 EEEIRALEPvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1510-1926 |
3.23e-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: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1510 VKQKSTAESELKQLRDRAAEAEKL--RKAAQEEAEKLRKQVNEETQK---KRMAEEEL--KRKAEAEKEAAKQKQKALED 1582
Cdd:pfam17380 213 IQMSTVAPKEVQGMPHTLAPYEKMerRKESFNLAEDVTTMTPEYTVRyngQTMTENEFlnQLLHIVQHQKAVSERQQQEK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1583 LENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQ----KSAAAELQSKHMSfVEKTSKLEESLKQEHgavlqlQHEAAAL 1658
Cdd:pfam17380 293 FEKMEQERLRQEKEEKAREVERRRKLEEAEKARQaemdRQAAIYAEQERMA-MERERELERIRQEER------KRELERI 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1659 KKQQEDAERAREEAEKELEKWRQKANEALRLRLQAeeeAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSAlKQKEMAENE 1738
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQELEA---ARKVKILEEERQRKIQQQKVEMEQIRAEQEEA-RQREVRRLE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1739 LERQRKVaESTAQQKLTAEQELIRLRADfdnaeqqrslledelyrlknevvAAQQQRKQLEDElakvrsemdvliqlksK 1818
Cdd:pfam17380 442 EERAREM-ERVRLEEQERQQQVERLRQQ-----------------------EEERKRKKLELE----------------K 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1819 AEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVA-EEEAARQRAEAER---ILKEKLAAISDATRLK 1894
Cdd:pfam17380 482 EKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAiYEEERRREAEEERrkqQEMEERRRIQEQMRKA 561
|
410 420 430
....*....|....*....|....*....|..
gi 1927222982 1895 TEAEIALKEKEAENERLRRQAEDEAyQRKALE 1926
Cdd:pfam17380 562 TEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
199-299 |
3.38e-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: 62.75 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 199 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED 278
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 1927222982 279 VdVPHPDEKSIITYVSSLYDA 299
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3833-3870 |
3.73e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.42 E-value: 3.73e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1927222982 3833 LEAQTATGGIIDPEFQFHLPADVAMQRGYINKETNEKL 3870
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3093-3130 |
5.30e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.03 E-value: 5.30e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1927222982 3093 LEAQAGTGYVVDPVDNKKYTVDEAVKAGVVGPELHEKL 3130
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1956-2516 |
5.38e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1956 AIVDDTLKQRRVVEEEIRILKlnFEKASSGKLDLELELNKLKniaeETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKV 2035
Cdd:PRK03918 139 AILESDESREKVVRQILGLDD--YENAYKNLGEVIKEIKRRI----ERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2036 KKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQ--- 2112
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKeka 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2113 ---TKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAE-FEAAKRAQA 2188
Cdd:PRK03918 293 eeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHElYEEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2189 ENAALKqKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEE--- 2265
Cdd:PRK03918 373 ELERLK-KRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrk 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2266 --LLKVKVQMEELLKLKLRIEEENQRLiKKDKDNTQKFLAKE---------ADNMKKLAE-----DAARLSVEAQEAARL 2329
Cdd:PRK03918 452 elLEEYTAELKRIEKELKEIEEKERKL-RKELRELEKVLKKEseliklkelAEQLKELEEklkkyNLEELEKKAEEYEKL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2330 RQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAER- 2408
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDa 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2409 KRQLEIIAES-EKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEA-----D 2482
Cdd:PRK03918 611 EKELEREEKElKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEElekrrE 690
|
570 580 590
....*....|....*....|....*....|....
gi 1927222982 2483 DLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQ 2516
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2061-2233 |
6.03e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 67.91 E-value: 6.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2061 KKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREA 2140
Cdd:PRK09510 95 KQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2141 ALLRQQAEEAERQKAAAEQEAANQAKAQEDAERlRKEAEFEAAKRAQAENAALKQKQQADAemakhKKLAEQTLKQKFQV 2220
Cdd:PRK09510 175 AAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA-KKKAAAEAKKKAAAEAKAAAAKAAAEA-----KAAAEKAAAAKAAE 248
|
170
....*....|...
gi 1927222982 2221 EQELTKVKLKLDE 2233
Cdd:PRK09510 249 KAAAAKAAAEVDD 261
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
199-294 |
6.83e-11 |
|
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: 62.02 E-value: 6.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 199 KEKLLLWSQRMtdgYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLV-DMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPE 277
Cdd:cd21229 5 KKLMLAWLQAV---LPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1927222982 278 DVDVPHPDEKSIITYVS 294
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2221-2648 |
7.50e-11 |
|
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: 68.89 E-value: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2221 EQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEEnqrlIKKDKDNTQK 2300
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE----IKKKEKELEK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2301 fLAKEADNMKKLAEDaarlsVEAQEAARLRQIAE-----DDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLA 2375
Cdd:TIGR04523 157 -LNNKYNDLKKQKEE-----LENELNLLEKEKLNiqkniDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2376 QEQAQKLLEDKQLMQQRLDEETEEYQ--KSLEAERKRQL-EIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASR 2452
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNqlKDEQNKIKKQLsEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2453 LHETELATQEKmtvveKLEVARltssKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMadaqQKQIEhEKTVLQQTFL 2532
Cdd:TIGR04523 311 ELKSELKNQEK-----KLEEIQ----NQISQNNKIISQLNEQISQLKKELTNSESENSEK----QRELE-EKQNEIEKLK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2533 SEKEMLLKKEKLIEEEKKRLESQFEEeVKKAKALKDEQ----ERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKE 2608
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQN-QEKLNQQKDEQikklQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1927222982 2609 MKELERKRLEQERILAEENQKLREKLQQLEEAQKDQPDKE 2648
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE 495
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2348-2649 |
9.03e-11 |
|
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: 68.84 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2348 LKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIiaESEKLKLQVSQ 2427
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDL--LQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2428 LSEAQAKAQEEAKKFKKQadsiaSRLHETELATQEKMTVVEK-LEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQ 2506
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQV-----LKENKEEEKEKKLQEEELKlLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2507 nKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQA 2586
Cdd:pfam02463 328 -KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927222982 2587 tmdAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQPDKEV 2649
Cdd:pfam02463 407 ---AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE 466
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1581-2216 |
1.04e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1581 EDLENLKRQAEEAERQVKQ-AEIEKERQiQVAHVAAQKSAAAELQSKHmsfvektskleeslkqehgAVLQLQHEAAALK 1659
Cdd:COG4913 235 DDLERAHEALEDAREQIELlEPIRELAE-RYAAARERLAELEYLRAAL-------------------RLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1660 KqqedaerareeaekelekwRQKANEALRLRLQAEEEAHKkslAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENEL 1739
Cdd:COG4913 295 A-------------------ELEELRAELARLEAELERLE---ARLDALREELDELEAQIRGNGGDRLEQLEREIERLER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1740 ERQRKVAESTAQQKLTA---------EQELIRLRADF----DNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAkvr 1806
Cdd:COG4913 353 ELEERERRRARLEALLAalglplpasAEEFAALRAEAaallEALEEELEALEEALAEAEAALRDLRRELRELEAEIA--- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1807 semdvliqlkskaeketmsNSERSKQLLEVEATKMRDLAEEA-----SKLRAIAEEAkhqrQVAEEEAARQRAeAERIL- 1880
Cdd:COG4913 430 -------------------SLERRKSNIPARLLALRDALAEAlgldeAELPFVGELI----EVRPEEERWRGA-IERVLg 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1881 ---------KEKLAAIS---DATRLKTEAEIaLKEKEAENERLRRQAEDEAYQRKaLEDQANQH----KQQIEEKIVLLK 1944
Cdd:COG4913 486 gfaltllvpPEHYAAALrwvNRLHLRGRLVY-ERVRTGLPDPERPRLDPDSLAGK-LDFKPHPFrawlEAELGRRFDYVC 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1945 KSSEAEMER-QRAIVDD-TLKQRRVVeeeirilklnFEKASSGKLDLELEL-----NKLKNIAEETQQSKLRAEEEAEKL 2017
Cdd:COG4913 564 VDSPEELRRhPRAITRAgQVKGNGTR----------HEKDDRRRIRSRYVLgfdnrAKLAALEAELAELEEELAEAEERL 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2018 RKLAleeekrrreaeekvkkiaaaeeeaarqrqaaqDELDRLKKKAEEARKQKDDADKEaekqiLMAQQAAQKCSAAEQQ 2097
Cdd:COG4913 634 EALE--------------------------------AELDALQERREALQRLAEYSWDE-----IDVASAEREIAELEAE 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2098 VQSVLAQQkeDTIMQtkLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKE 2177
Cdd:COG4913 677 LERLDASS--DDLAA--LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1927222982 2178 AEFEAAKRAQAENAALK----QKQQADAEMAKHKKLAEQTLKQ 2216
Cdd:COG4913 753 ERFAAALGDAVERELREnleeRIDALRARLNRAEEELERAMRA 795
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2054-2660 |
1.29e-10 |
|
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: 68.28 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2054 DELDRLKKKAEEARKQKDDADK-----EAEKQILMAQ-QAAQKCSAAEQQVQSVLAQQKED-----TIMQTKLKEEYEKA 2122
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKkhqqlCEEKNALQEQlQAETELCAEAEEMRARLAARKQEleeilHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2123 KKLakQAEaaKEKAEREAALLRQQ--AEEAERQKAAAEQ--EAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQ 2198
Cdd:pfam01576 92 QQL--QNE--KKKMQQHIQDLEEQldEEEAARQKLQLEKvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2199 ADAEMAKHKKLAEQTLKQKF---QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDavkQRGQVEEELLKVKVQMEE 2275
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAmisDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAE---LQAQIAELRAQLAKKEEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2276 LLKLKLRIEEENqrlikkdkdntqkflAKEADNMKKLAEDAARLSvEAQEaarlrqiaedDLNQQRALADKMLKEKMQAI 2355
Cdd:pfam01576 245 LQAALARLEEET---------------AQKNNALKKIRELEAQIS-ELQE----------DLESERAARNKAEKQRRDLG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2356 QEASRLRAEAEmlqrqKDLAQEQAQKLLEDKQlmqqrlDEETEEYQKSLEAERKRQleiiaeseklKLQVSQLSEAQAKA 2435
Cdd:pfam01576 299 EELEALKTELE-----DTLDTTAAQQELRSKR------EQEVTELKKALEEETRSH----------EAQLQEMRQKHTQA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2436 QEEAKKFKKQADSIASRLHETELAtqekmtvvekLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEmaDA 2515
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQA----------LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE--SE 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2516 QQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQK-------QQMEDEKKKLQATM 2588
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKlnlstrlRQLEDERNSLQEQL 505
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222982 2589 DAALNKQKEAEKEMHNKQKEMKELeRKRLEQERILAEENQKLREKLQQLEEAQKDQPDKEVIHVTMVETTKN 2660
Cdd:pfam01576 506 EEEEEAKRNVERQLSTLQAQLSDM-KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKN 576
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2169-2643 |
1.71e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2169 EDAERLRKEaeFEAAKRAqaENAALKQKQQAD------AEMAKHKKLAEQ-----TLKQKFQVEQELTKVKLKLDETDKq 2237
Cdd:COG4913 225 EAADALVEH--FDDLERA--HEALEDAREQIEllepirELAERYAAARERlaeleYLRAALRLWFAQRRLELLEAELEE- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2238 ksvLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQM-----EELLKLKLRIEEENQRLikKDKDNTQKFLAKEADNMK-K 2311
Cdd:COG4913 300 ---LRAELARLEAELERLEARLDALREELDELEAQIrgnggDRLEQLEREIERLEREL--EERERRRARLEALLAALGlP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2312 LAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQK---DLAQEQAQKLLEDK-- 2386
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRDALAEAlg 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2387 ----------QLMQQRLDEEteEYQKSLE-------------AERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFK 2443
Cdd:COG4913 455 ldeaelpfvgELIEVRPEEE--RWRGAIErvlggfaltllvpPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2444 kqADSIASRLH----------ETELATQEKMTVVEKLE----------VARLTSSK----EADDL-------------RK 2486
Cdd:COG4913 533 --PDSLAGKLDfkphpfrawlEAELGRRFDYVCVDSPEelrrhpraitRAGQVKGNgtrhEKDDRrrirsryvlgfdnRA 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2487 AIADLEKEKSRLKKEAEDLQNKSKEmADAQQKQIEHEKTVLQQtfLSEKEMLLKKEKLIEEEKKRLESQ----------- 2555
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEA-LEAELDALQERREALQR--LAEYSWDEIDVASAEREIAELEAElerldassddl 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2556 --FEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLREK 2633
Cdd:COG4913 688 aaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
570
....*....|
gi 1927222982 2634 LQQLEEAQKD 2643
Cdd:COG4913 768 RENLEERIDA 777
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3500-3537 |
1.87e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.49 E-value: 1.87e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1927222982 3500 LEAQMVSGGIIDPVNSHRVPIDVAYQKNIFNQKTAKNL 3537
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2208-2643 |
1.95e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2208 KLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAvkqrgqveEELLKVKVQMEELLKLKLRIEEEN 2287
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL--------EKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2288 QRLikkdkdntqKFLAKEADNMKKLAEDAARLSVEAQEAarlrqiaeddlnqQRALADKMLKEKMQAIQEASRLRAEAEM 2367
Cdd:COG4717 146 ERL---------EELEERLEELRELEEELEELEAELAEL-------------QEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2368 LQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAES----------------------EKLKLQV 2425
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIaaallallglggsllsliltiaGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2426 SQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDL 2505
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2506 QnkskemadaqQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEE-EVKKAKALKDEQERQKQQMEDEkkkL 2584
Cdd:COG4717 364 Q----------LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEElEEQLEELLGELEELLEALDEEE---L 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222982 2585 QATMDAALNKQKEAEKEMHNKQKEMKELER--KRLEQERILAEENQKLREKLQQLEEAQKD 2643
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAelEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1765-2626 |
2.57e-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: 67.28 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1765 ADF-DNAEQQRSLLEDELyRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERskqlLEVEATKMR- 1842
Cdd:COG3096 271 ADYmRHANERRELSERAL-ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDH----LNLVQTALRq 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1843 ---------DLAEEASKLRA---IAEEAKHQRQVAEEEAARQRAEAERiLKEKLA---------------------AISD 1889
Cdd:COG3096 346 qekieryqeDLEELTERLEEqeeVVEEAAEQLAEAEARLEAAEEEVDS-LKSQLAdyqqaldvqqtraiqyqqavqALEK 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1890 ATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQ---ANQHKQQIEEKIVLLKKSSeAEMERQRAivDDTLKQrr 1966
Cdd:COG3096 425 ARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKlsvADAARRQFEKAYELVCKIA-GEVERSQA--WQTARE-- 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1967 vVEEEIRILKLNFEKASSgkldLELELNKLKNIAEETQqsklRAEEEAEKLRKLAleeekrrreaeekvkkiaaaeeeaa 2046
Cdd:COG3096 500 -LLRRYRSQQALAQRLQQ----LRAQLAELEQRLRQQQ----NAERLLEEFCQRI------------------------- 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2047 RQRQAAQDELDRLKkkaEEARKQKDDADKEAEkqilmaqQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLA 2126
Cdd:COG3096 546 GQQLDAAEELEELL---AELEAQLEELEEQAA-------EAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2127 KQAEAAKEKAErEAALLRQQAEEAERQkaaaeqeaanqakaqedAERLRKEAefeAAKRAQAENAALKQKQQADAEMAKH 2206
Cdd:COG3096 616 EQSGEALADSQ-EVTAAMQQLLERERE-----------------ATVERDEL---AARKQALESQIERLSQPGGAEDPRL 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2207 KKLAEQ----TLKQKFQ---------------------VEQELTKVKLKLDETDKqksvLDEEL---QRLKDEVDDAVKQ 2258
Cdd:COG3096 675 LALAERlggvLLSEIYDdvtledapyfsalygparhaiVVPDLSAVKEQLAGLED----CPEDLyliEGDPDSFDDSVFD 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2259 rgqVEEELLKVKVQMEELLKLKLRIEEEnQRLIKKDKDNTQKFLAKEADnmkKLAEDAARLSVEAQEAARLRQIAEDDLN 2338
Cdd:COG3096 751 ---AEELEDAVVVKLSDRQWRYSRFPEV-PLFGRAAREKRLEELRAERD---ELAEQYAKASFDVQKLQRLHQAFSQFVG 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2339 QQRALA-----DKMLKEKMQAIQEASRLRAEAE----MLQRQKDLAQEQAQ---------KLLEDKQLmQQRLDEETEEY 2400
Cdd:COG3096 824 GHLAVAfapdpEAELAALRQRRSELERELAQHRaqeqQLRQQLDQLKEQLQllnkllpqaNLLADETL-ADRLEELREEL 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2401 QKSLEAER--KRQLEIIAESEKL-------KLQVSQLSEAQAKAQEEAKKFKKQADSIasrlheTELatqekmtvvekle 2471
Cdd:COG3096 903 DAAQEAQAfiQQHGKALAQLEPLvavlqsdPEQFEQLQADYLQAKEQQRRLKQQIFAL------SEV------------- 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2472 VARLT--SSKEADDLRKAIADL-EKEKSRLKkEAEDLQNKSKEMADAQQKQIEHEKTVLQQ---TFLSEKEMLLKKEKLI 2545
Cdd:COG3096 964 VQRRPhfSYEDAVGLLGENSDLnEKLRARLE-QAEEARREAREQLRQAQAQYSQYNQVLASlksSRDAKQQTLQELEQEL 1042
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2546 EEEKKRLESQFEEevkKAKALKDEQERQKQQMEDEKkklqatmdAALNKQKEA-EKEMHNKQKEMKELERKrLEQERILA 2624
Cdd:COG3096 1043 EELGVQADAEAEE---RARIRRDELHEELSQNRSRR--------SQLEKQLTRcEAEMDSLQKRLRKAERD-YKQEREQV 1110
|
..
gi 1927222982 2625 EE 2626
Cdd:COG3096 1111 VQ 1112
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1272-2022 |
3.04e-10 |
|
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: 67.12 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1272 KQRQEKIQAVTITDSKTLKEQLAQEKKLLEEVEGNKDKvdecqkyakayidtiKDYELQlvaykaqveplasplkkTKLD 1351
Cdd:pfam01576 203 RQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK---------------KEEELQ-----------------AALA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1352 SASDNIIQEYVTLRtKYSELMTLtsqyikfITDSQRRLEDEEKA---AEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAI 1428
Cdd:pfam01576 251 RLEEETAQKNNALK-KIRELEAQ-------ISELQEDLESERAArnkAEKQRRDLGEELEALKTELEDTLDTTAAQQELR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1429 AKAEKEAQELKLRMQEEVnRREDAVVDAEKQKHNIQLElhELKNLSEQ-----QIMDKSKQvddALQSRVK-IEEEIRLI 1502
Cdd:pfam01576 323 SKREQEVTELKKALEEET-RSHEAQLQEMRQKHTQALE--ELTEQLEQakrnkANLEKAKQ---ALESENAeLQAELRTL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1503 RLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALED 1582
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1583 LENLKRQAEEAERQVKQAEIEKE--RQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEE---SLKQEHGAVLQLQHEAAA 1657
Cdd:pfam01576 477 LQEETRQKLNLSTRLRQLEDERNslQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEdagTLEALEEGKKRLQRELEA 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1658 LKKQQEDAERAREEAEKELEKWRQKANEAL------RLRLQAEEEAHKK---SLAQEDA-------EKQKEEAE-REAKK 1720
Cdd:pfam01576 557 LTQQLEEKAAAYDKLEKTKNRLQQELDDLLvdldhqRQLVSNLEKKQKKfdqMLAEEKAisaryaeERDRAEAEaREKET 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1721 RAKAEDSALKQKEMAENELERQRKvaestaqqKLTAEQEliRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLED 1800
Cdd:pfam01576 637 RALSLARALEEALEAKEELERTNK--------QLRAEME--DLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELED 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1801 EL-----AKVRSEMDvLIQLKSKAEKETMSNSERSKQlleveatKMRDLAEEASKLRAIAEEAKHQRQVAeeEAARQRAE 1875
Cdd:pfam01576 707 ELqatedAKLRLEVN-MQALKAQFERDLQARDEQGEE-------KRRQLVKQVRELEAELEDERKQRAQA--VAAKKKLE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1876 AEriLKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIeekivllkKSSEAEMERQR 1955
Cdd:pfam01576 777 LD--LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKL--------KNLEAELLQLQ 846
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222982 1956 AIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLK----NIAEETQQSKLRAEEEAEKLRKLAL 2022
Cdd:pfam01576 847 EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEariaQLEEELEEEQSNTELLNDRLRKSTL 917
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1272-1616 |
3.14e-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: 66.69 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1272 KQRQEKIQavtitdsKTLKEQLAQEKK-LLEEVEgNKDKVDECQKYAKAYIDtikdyelQLVAYKAQVEPLASPLKKTkl 1350
Cdd:pfam17380 287 RQQQEKFE-------KMEQERLRQEKEeKAREVE-RRRKLEEAEKARQAEMD-------RQAAIYAEQERMAMERERE-- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1351 dsasdniiQEYVTLRTKYSELMTLTSQYIKFITDSQRRLEdeekaaeKLKAEEQKKMAMMQAELD---KQKQLAEVHAKA 1427
Cdd:pfam17380 350 --------LERIRQEERKRELERIRQEEIAMEISRMRELE-------RLQMERQQKNERVRQELEaarKVKILEEERQRK 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1428 IAKAEKEAQELKlRMQEEVNRREDAVVDAEKQKhniQLELHELKNLSEQQIMDKSKQvDDALQSRVKIEEEiRLIRLQLE 1507
Cdd:pfam17380 415 IQQQKVEMEQIR-AEQEEARQREVRRLEEERAR---EMERVRLEEQERQQQVERLRQ-QEEERKRKKLELE-KEKRDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1508 TTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEEtQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLK 1587
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-ERRREAEEERRKQQEMEERRRIQEQMRKATEERSR 567
|
330 340
....*....|....*....|....*....
gi 1927222982 1588 RQAEEAERQVKQAEIEKERQIQVAHVAAQ 1616
Cdd:pfam17380 568 LEAMEREREMMRQIVESEKARAEYEATTP 596
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2194-2642 |
3.46e-10 |
|
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: 66.58 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2194 KQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQM 2273
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2274 EELLKLKLRIEEENQRlikkdkdntQKFLAKEADNMKK----LAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKM-- 2347
Cdd:TIGR04523 197 LKLELLLSNLKKKIQK---------NKSLESQISELKKqnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIkk 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2348 -LKEKMQAIQEASR-----------LRAEAEMLQRQK----------DLAQEQAQKLLEDKQLMQ-----QRLDEETEEY 2400
Cdd:TIGR04523 268 qLSEKQKELEQNNKkikelekqlnqLKSEISDLNNQKeqdwnkelksELKNQEKKLEEIQNQISQnnkiiSQLNEQISQL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2401 QKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKE 2480
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2481 ADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMadaqQKQIEHEKTVLQQTFLSEKEMLLKKEKlieeekkrLESQFEEEV 2560
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNQDSVKELIIKNL----DNTRESLETQLKVLSRSINKIKQNLEQ--------KQKELKSKE 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2561 KKAKALKdeqeRQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQE-----RILAEENQKLREKLQ 2635
Cdd:TIGR04523 496 KELKKLN----EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfelkkENLEKEIDEKNKEIE 571
|
....*..
gi 1927222982 2636 QLEEAQK 2642
Cdd:TIGR04523 572 ELKQTQK 578
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1168-2005 |
3.48e-10 |
|
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: 66.99 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1168 KEVETYRTKLKKMRAEAEGEQPVFDSLEAELKKATAVSDKMSRVHSE------RDAELDHYRQLLSSLQDRWKAvfsqID 1241
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENEldplknRLKEIEHNLSKIMKLDNEIKA----LK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1242 LRQRELEQLGRQLGYYRES----YDWLIRWINDAKQRQEKIQAVTITDSKTLKEQLAQEKKLLEEvegNKDKVDECQKYA 1317
Cdd:TIGR00606 276 SRKKQMEKDNSELELKMEKvfqgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQ---EKTELLVEQGRL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1318 KAYIDTIKDyelQLVAYKAQVEPLASPLKKTKLDSASDNIIQeyvtlrtkyselmtltsqYIKFITDSQRRLEDEEKAAE 1397
Cdd:TIGR00606 353 QLQADRHQE---HIRARDSLIQSLATRLELDGFERGPFSERQ------------------IKNFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1398 KLKAEEQKKMAMMQAELDK----QKQLAEVHAKAIAKAEKEAQELKLRMQeEVNRREDAVVDAEKQKHNIQLELHELKNL 1473
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEirdeKKGLGRTIELKKEILEKKQEELKFVIK-ELQQLEGSSDRILELDQELRKAERELSKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1474 SEQQIMDKSKQVDDALQS-RVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEET 1552
Cdd:TIGR00606 491 EKNSLTETLKKEVKSLQNeKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFP 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1553 QKKRMAEeelkrkaeaekeaakqkqkALEDLENLKRQAEEAERQVkQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVE 1632
Cdd:TIGR00606 571 NKKQLED-------------------WLHSKSKEINQTRDRLAKL-NKELASLEQNKNHINNELESKEEQLSSYEDKLFD 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1633 KTSKLEESLKQEhgavlQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRL---RLQAEEEAHKKSLAQED--- 1706
Cdd:TIGR00606 631 VCGSQDEESDLE-----RLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVcqrVFQTEAELQEFISDLQSklr 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1707 -AEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLK 1785
Cdd:TIGR00606 706 lAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1786 ---NEVVAAQQQRKQLEDELAKVR--------SEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAI 1854
Cdd:TIGR00606 786 vclTDVTIMERFQMELKDVERKIAqqaaklqgSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1855 AEEAKHQRQVAEEEAARQRAEAERI------LKEKLAAISDATRLKTEAEIALKEKEAENERL-------RRQAEDEAYQ 1921
Cdd:TIGR00606 866 TNELKSEKLQIGTNLQRRQQFEEQLvelsteVQSLIREIKDAKEQDSPLETFLEKDQQEKEELissketsNKKAQDKVND 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1922 RKALEDQANQHKQQIEEKIV----LLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNF------EKASSGKLDLEL 1991
Cdd:TIGR00606 946 IKEKVKNIHGYMKDIENKIQdgkdDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIdtqkiqERWLQDNLTLRK 1025
|
890
....*....|....
gi 1927222982 1992 ELNKLKNIAEETQQ 2005
Cdd:TIGR00606 1026 RENELKEVEEELKQ 1039
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
559-748 |
3.48e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 62.85 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 559 LRYIQDLLAWVEENQHRIDEAQWGSDLPSVESQLGSHRGLHQTVEDFRSKIERARADETQL---SPVSKGAYRDYLGKLD 635
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 636 LQYGKLLNSSKSRLRNLD---SLHAFVSAATKELMWLNDKEEEEVNFDWSDRNSNMTAKKDNYSGLMRELELREKKVNDI 712
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1927222982 713 QATGDKLVRDGHPGK-KTVESFTAALQTQWSWILQLC 748
Cdd:cd00176 166 NELAEELLEEGHPDAdEEIEEKLEELNERWEELLELA 202
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1802-2278 |
3.58e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.33 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1802 LAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEakhqrqVAEEEAARQRAEAERILK 1881
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE------LEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1882 EKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHkQQIEEKIVLLKKSSEAEMERQraiVDDT 1961
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL-AELQEELEELLEQLSLATEEE---LQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1962 LKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAekLRKLALEEEKRRREAEEKVKKIAAA 2041
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL--LLLIAAALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2042 EEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILmaqqaaqkcsaAEQQVQSVLAQQKEDTIMQTKLKEEYEK 2121
Cdd:COG4717 276 AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL-----------EEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2122 AKKLAKQAEAAKEKAEREAALLRQQAEEAErqkaaaeqeaANQAKAQEDAERLRkeaefEAAKRAQAENAALKQKQQADA 2201
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELEQEIAA----------LLAEAGVEDEEELR-----AALEQAEEYQELKEELEELEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2202 EMAKHKKLAEQTLKQ--KFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQR--GQVEEELLKVKVQMEELL 2277
Cdd:COG4717 410 QLEELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELA 489
|
.
gi 1927222982 2278 K 2278
Cdd:COG4717 490 E 490
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1444-1935 |
4.41e-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: 66.19 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1444 EEVNRREDAVV----DAEKQKHNIQLELHELKNLSE-QQIMDKSKQVDDAlqSRVKIEEEIRLIRLQLETTVKQKSTAES 1518
Cdd:NF033838 38 EEVRGGNNPTVtssgNESQKEHAKEVESHLEKILSEiQKSLDKRKHTQNV--ALNKKLSDIKTEYLYELNVLKEKSEAEL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1519 ELKQLRDRAAEAEKLRKAAQEEAEK---LRKQVNEETQKKRMAEEELKRKAEAEKeaakqkqkaledLENLKRQAEEAER 1595
Cdd:NF033838 116 TSKTKKELDAAFEQFKKDTLEPGKKvaeATKKVEEAEKKAKDQKEEDRRNYPTNT------------YKTLELEIAESDV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1596 QVKQAEIEkerqiqvahvAAQKSAaaelqskhmsfveKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREeaeke 1675
Cdd:NF033838 184 EVKKAELE----------LVKEEA-------------KEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEE----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1676 lekwrqkanEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREA--------KKR--AKAEDSALKQKEMAENELERQRKV 1745
Cdd:NF033838 236 ---------EAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVlgepatpdKKEndAKSSDSSVGEETLPSPSLKPEKKV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1746 AEstAQQKLTAEQElirlRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAkvrsemdvliqlksKAEKETMS 1825
Cdd:NF033838 307 AE--AEKKVEEAKK----KAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELELV--------------KEEAKEPR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1826 NSERSKQL-LEVEATKmrdlaEEASKLraiaEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEK 1904
Cdd:NF033838 367 NEEKIKQAkAKVESKK-----AEATRL----EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEK 437
|
490 500 510
....*....|....*....|....*....|....
gi 1927222982 1905 EAEN---ERLRRQAEDEAYQRKAlEDQANQHKQQ 1935
Cdd:NF033838 438 PAEQpkaEKPADQQAEEDYARRS-EEEYNRLTQQ 470
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2205-2642 |
4.54e-10 |
|
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: 66.20 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2205 KHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVL---DEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKL 2281
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsntQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2282 RIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDaarlsVEAQEAARLRQIaeDDLNQQRAladKMLKEKMQAIQEASRL 2361
Cdd:TIGR04523 292 QLKSEISDLNNQKEQDWNKELKSELKNQEKKLEE-----IQNQISQNNKII--SQLNEQIS---QLKKELTNSESENSEK 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2362 RAEAEMLQRQ-KDLAQEQAQKLLEDKQLMQQRLDEETE-EYQKSLEAERKRQLEIIaESEKLKL--QVSQLSEAQAKAQE 2437
Cdd:TIGR04523 362 QRELEEKQNEiEKLKKENQSYKQEIKNLESQINDLESKiQNQEKLNQQKDEQIKKL-QQEKELLekEIERLKETIIKNNS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2438 EAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQ 2517
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2518 KQIEHektvlQQTFLSEKemllkkeklieeekKRLESQFEEevKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKE 2597
Cdd:TIGR04523 521 SLKEK-----IEKLESEK--------------KEKESKISD--LEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKS 579
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1927222982 2598 AEKEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQK 2642
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2102-2534 |
4.66e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2102 LAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFE 2181
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2182 AAKRAQAENAALKQKQQADAEMAKhKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQ 2261
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQ-EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2262 VEEELLKVKVQmEELLKLKLRIEEENQRLIKKDKDNTQK---------------FLAKEADNMKKLAEDAARLSVEAQEA 2326
Cdd:COG4717 232 LENELEAAALE-ERLKEARLLLLIAAALLALLGLGGSLLsliltiagvlflvlgLLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2327 ARLRQIAEDDLNQQRA-------LADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKlledKQLMQQRLDEETEE 2399
Cdd:COG4717 311 PALEELEEEELEELLAalglppdLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI----AALLAEAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2400 YQKSLEAERKRQlEIIAESEKLKLQVSQLSEAQAKAQEEAKKfkkqaDSIASRLHETELATQEKMTVVEKL--EVARLTS 2477
Cdd:COG4717 387 LRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEELEELreELAELEA 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222982 2478 SKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKqIEHEKTVLQQTFLSE 2534
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALEL-LEEAREEYREERLPP 516
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2177-2644 |
5.48e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 66.02 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2177 EAEFEAAKRAQAENAALKQKQQAD--AEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDD 2254
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDetLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2255 AVKQRGQVEEE-LLKVKVQMEELLKLKLRIEEENQR---LIKKDKDNTQKFLAKEA----DNMKKLAEDAARLSVEAQEA 2326
Cdd:pfam12128 327 LEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERlkaLTGKHQDVTAKYNRRRSkikeQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2327 ARLRQIAEDDLNQQ-RALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQeqaqklLEDKQLMQQRL-DEETEEYQKSL 2404
Cdd:pfam12128 407 DRQLAVAEDDLQALeSELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQAT------ATPELLLQLENfDERIERAREEQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2405 EAERKRQLeiiaeseklklqvsqlseaqaKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADD- 2483
Cdd:pfam12128 481 EAANAEVE---------------------RLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHf 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2484 LRKAIADLEKEKSRLKKEAE----DLQnksKEMADAQQKQiehEKTVLQQTfLSEKEMLLKKEKLIEEEKKRLESQFEEE 2559
Cdd:pfam12128 540 LRKEAPDWEQSIGKVISPELlhrtDLD---PEVWDGSVGG---ELNLYGVK-LDLKRIDVPEWAASEEELRERLDKAEEA 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2560 VKKAKALKDEQERQKQQMEDEKKKLQATMDAA-------------LNKQKEAEKEMHNKQKEmkelERKRLEQERI--LA 2624
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEKASREETFArtalknarldlrrLFDEKQSEKDKKNKALA----ERKDSANERLnsLE 688
|
490 500
....*....|....*....|
gi 1927222982 2625 EENQKLREKLQQLEEAQKDQ 2644
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEQKEQ 708
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2055-2399 |
6.52e-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: 65.30 E-value: 6.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2055 ELDRLKKKAEEARKQKDDADKEAEKQilmaQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKA---KKLAKQAEA 2131
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEK----YKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTltqRVLERETEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2132 AKEKAEREAALLRQQAEEAERQKAAAEQEaanqakaQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKklae 2211
Cdd:pfam07888 153 ERMKERAKKAGAQRKEEEAERKQLQAKLQ-------QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK---- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2212 qtLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEEL------LKLKLRiee 2285
Cdd:pfam07888 222 --LTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLtlqladASLALR--- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2286 ENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEasrLRAEA 2365
Cdd:pfam07888 297 EGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQE---LKASL 373
|
330 340 350
....*....|....*....|....*....|....
gi 1927222982 2366 EMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEE 2399
Cdd:pfam07888 374 RVAQKEKEQLQAEKQELLEYIRQLEQRLETVADA 407
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1867-2422 |
6.63e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 6.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1867 EEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAE-----------NERLRRQAEDEAYQRKALEDqANQHKQQ 1935
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKEleevlreineiSSELPELREELEKLEKEVKE-LEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1936 IEEKiVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKlDLELELNKLKNIAEETQQSKLRAEEEAE 2015
Cdd:PRK03918 240 IEEL-EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2016 KLRKLALEEEKRRREAEEKVKKIaaaeEEAARQRQAAQDELDRLKKKA---EEARKQKDDADK-EAEKQILMAQQAAQKC 2091
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERL----EELKKKLKELEKRLEELEERHelyEEAKAKKEELERlKKRLTGLTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2092 SAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKA---------EREAALLRQQAEEAERQKAAAEQEAA 2162
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelteEHRKELLEEYTAELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2163 NQAKAQEDAERLRKEAEfeaakraqAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLD 2242
Cdd:PRK03918 474 KERKLRKELRELEKVLK--------KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2243 EELQRLKD----------EVDDAVKQRGQVEEELLKVKVQMEELLKLKLR-IEEENQRLI-----KKDKDNTQKFLAKEA 2306
Cdd:PRK03918 546 KELEKLEElkkklaelekKLDELEEELAELLKELEELGFESVEELEERLKeLEPFYNEYLelkdaEKELEREEKELKKLE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2307 DNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRalADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDK 2386
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEE--YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
570 580 590
....*....|....*....|....*....|....*.
gi 1927222982 2387 qlmqqrldEETEEYQKSLEAERKRQLEIIAESEKLK 2422
Cdd:PRK03918 704 --------EEREKAKKELEKLEKALERVEELREKVK 731
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1734-2199 |
9.95e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 9.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1734 MAENELERQRKVAES-TAQQKLTAEQELIRLRADFDNAEQQRSL---LEDELYRLKNEVVAAQQQRKQLEDELAKVRSEM 1809
Cdd:COG4717 46 MLLERLEKEADELFKpQGRKPELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1810 DV--LIQLKSKAEKETMSNSERSKQLLEveatKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAI 1887
Cdd:COG4717 126 QLlpLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1888 SDATRLKTEAEIALKEKEAENERLRRQAEdeayqRKALEDQANQHKQQIEEKIVLLKksSEAEMERQRAIVDDTLKQRRV 1967
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELE-----QLENELEAAALEERLKEARLLLL--IAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1968 VEE----EIRILKLNFEKASSGKLDLELELNKLKNIAEetqQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEE 2043
Cdd:COG4717 275 IAGvlflVLGLLALLFLLLAREKASLGKEAEELQALPA---LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2044 EAARQRQAAQD-ELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKA 2122
Cdd:COG4717 352 LLREAEELEEElQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE 431
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222982 2123 KKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQA 2199
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2060-2217 |
1.27e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 63.33 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2060 KKKAEEARKQKDDADKEAE--KQILMAQQAAQKCSAAEQQVQSVLAQQKEdtimQTKLKEEYEKAKKlakQAEAAKEKAE 2137
Cdd:TIGR02794 104 AKQAEQAAKQAEEKQKQAEeaKAKQAAEAKAKAEAEAERKAKEEAAKQAE----EEAKAKAAAEAKK---KAEEAKKKAE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2138 REAallrQQAEEAERQKaaaeqeaaNQAKAQEDAERLRKEAEFEAAKRAQAE----NAALKQKQQADAEMAKHKKLAEQT 2213
Cdd:TIGR02794 177 AEA----KAKAEAEAKA--------KAEEAKAKAEAAKAKAAAEAAAKAEAEaaaaAAAEAERKADEAELGDIFGLASGS 244
|
....
gi 1927222982 2214 LKQK 2217
Cdd:TIGR02794 245 NAEK 248
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1727-1949 |
1.32e-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: 63.63 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1727 SALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVR 1806
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1807 SEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQR---QVAEEEAARQRAEAERILKEK 1883
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAeelRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222982 1884 LAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSSEA 1949
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2416-2629 |
1.98e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2416 AESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEvarltssKEADDLRKAIADLEKEK 2495
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE-------QELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2496 SRLKKEAEDLQNKSKEMADAQQKQIEHEKTVL----------------QQTFLSEKEMLLKKEKLIEEEKKRLESQFEEE 2559
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2560 VKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQK 2629
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1709-2479 |
2.33e-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: 63.97 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1709 KQKEEAEREAKKRAKAEdSALKQKEmaeNELERQRKV--AESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYR--- 1783
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIE-AELKQKE---NKLQENRKIieAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlc 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1784 --LKNEVVAAQQQRKQLEDELAKVRSemdVLIQLKSKAEKETMSNSErskqlLEVEATKMRdlAEEASKLRAIAEEAKHQ 1861
Cdd:pfam05483 158 nlLKETCARSAEKTKKYEYEREETRQ---VYMDLNNNIEKMILAFEE-----LRVQAENAR--LEMHFKLKEDHEKIQHL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1862 RQVAEEEAARQRAEAERIL---KEKLAAISDATRLKTEAEIALKEKEaenERLRRQAEDEayqrkaleDQANQHKQQIEE 1938
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLiqiTEKENKMKDLTFLLEESRDKANQLE---EKTKLQDENL--------KELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1939 KIVLLKKSSEAEMERQRAIVDDTLKQRRVV-----EEEIRILKLNFEKASSGKLDLELELN--KLKNIAEeTQQSKLRAE 2011
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLQIATKTIcqlteEKEAQMEELNKAKAAHSFVVTEFEATtcSLEELLR-TEQQRLEKN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2012 EEAEKLRKLALEEEKRRREAEEKVKKiaaaeeeaarqrqAAQDELDRLKKKAEEARKQKDDaDKEAEKqilmaqqAAQKC 2091
Cdd:pfam05483 376 EDQLKIITMELQKKSSELEEMTKFKN-------------NKEVELEELKKILAEDEKLLDE-KKQFEK-------IAEEL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2092 SAAEQQVQSVLaqqkedtimQTKLKEEYEkakkLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDA 2171
Cdd:pfam05483 435 KGKEQELIFLL---------QAREKEIHD----LEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2172 ERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDE 2251
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2252 VDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKklaedaarlsVEAQEAARLRQ 2331
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNK----------LELELASAKQK 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2332 IAEDDLNQQRALADKMLKEK--MQAIQEASRLRAEAEMLQRQKDLAQEqaQKLLEDKQLMQQrldeETEEYQKSLEaERK 2409
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKISEEklLEEVEKAKAIADEAVKLQKEIDKRCQ--HKIAEMVALMEK----HKHQYDKIIE-ERD 724
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2410 RQLEIIAESEKlklqvsQLSEAQAKAQEEAKKFKKQADSIASRLhETELATQEKMTVVEKLEVARLTSSK 2479
Cdd:pfam05483 725 SELGLYKNKEQ------EQSSAKAALEIELSNIKAELLSLKKQL-EIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2064-2211 |
2.41e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 62.97 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2064 EEARKQKDDADKEAEKQILMA-QQAAQKCSAAEQQVQS--VLAQQKEDTIMQTKLKEEYEKAKKLAKQA-EAAKEKAERE 2139
Cdd:COG2268 199 RDARIAEAEAERETEIAIAQAnREAEEAELEQEREIETarIAEAEAELAKKKAEERREAETARAEAEAAyEIAEANAERE 278
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222982 2140 aalLRQQAEEAERQKAAAEqeaanqakAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAE 2211
Cdd:COG2268 279 ---VQRQLEIAEREREIEL--------QEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAE 339
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2057-2442 |
2.79e-09 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 63.92 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2057 DRLKKKAEEARKQKDDADKEaekqILMAQQAAQKcSAAEQQVQSVLAQQKEDTI---------MQTKLKEEYEKAKKLAK 2127
Cdd:PRK10929 26 KQITQELEQAKAAKTPAQAE----IVEALQSALN-WLEERKGSLERAKQYQQVIdnfpklsaeLRQQLNNERDEPRSVPP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2128 Q---AEAAKEKAEREAALL---RQQAEEAERQKAAAEQEAANQAKaQEDAERLRKEAEfeaaKRAQAE---NAALKQKQ- 2197
Cdd:PRK10929 101 NmstDALEQEILQVSSQLLeksRQAQQEQDRAREISDSLSQLPQQ-QTEARRQLNEIE----RRLQTLgtpNTPLAQAQl 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2198 -QADAEMAKHK-KLAEQTLKQ-KFQVEQELTKVKLKLDEtdKQKSVLDEELQRLKDEVDDavkQRGQVEEELLkvkvqme 2274
Cdd:PRK10929 176 tALQAESAALKaLVDELELAQlSANNRQELARLRSELAK--KRSQQLDAYLQALRNQLNS---QRQREAERAL------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2275 ellklklrieeENQRLIKKDKDNTQKFLAKEadnMKKLAEDAARLSVEAQE----AARLRQIAEDDLNQQRALAdkMLKE 2350
Cdd:PRK10929 244 -----------ESTELLAEQSGDLPKSIVAQ---FKINRELSQALNQQAQRmdliASQQRQAASQTLQVRQALN--TLRE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2351 KMQ------AIQEAsrLRAEA----EMLQRQK---DLAQEQAQKLLEDKQLMQQRLDEE---------TEEYQKSLEAER 2408
Cdd:PRK10929 308 QSQwlgvsnALGEA--LRAQVarlpEMPKPQQldtEMAQLRVQRLRYEDLLNKQPQLRQirqadgqplTAEQNRILDAQL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1927222982 2409 KRQLEI-----------IAESEKLKLQVSQLSEAQAKAQEEAKKF 2442
Cdd:PRK10929 386 RTQRELlnsllsggdtlILELTKLKVANSQLEDALKEVNEATHRY 430
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1195-1868 |
3.21e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 63.53 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1195 EAELKKATAVSDKMSRVHSERDAELDHYR----QLLSSLQDRWKAVFSQIDLRQRELEQLGRQLGYY---RESYDWLIRW 1267
Cdd:TIGR00606 503 VKSLQNEKADLDRKLRKLDQEMEQLNHHTttrtQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnkKQLEDWLHSK 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1268 INDAKQRQEKIQAVT--ITDSKTLKEQLAQEKKLLEEVEgnkdkvdecQKYAKAYIDTI--KDYELQLVAYKAQVEPLAs 1343
Cdd:TIGR00606 583 SKEINQTRDRLAKLNkeLASLEQNKNHINNELESKEEQL---------SSYEDKLFDVCgsQDEESDLERLKEEIEKSS- 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1344 plKKTKLDSASDNIIQEYVTLRTKYSE----LMTLTSQYIKFITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQ 1419
Cdd:TIGR00606 653 --KQRAMLAGATAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLG 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1420 LAEVHAKAIAKAEKEAQELKLRMQEeVNRredavvDAEKQKHNIQLELHELknlseQQIMDKSKQVDDaLQSRVKIEEei 1499
Cdd:TIGR00606 731 LAPGRQSIIDLKEKEIPELRNKLQK-VNR------DIQRLKNDIEEQETLL-----GTIMPEEESAKV-CLTDVTIME-- 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1500 rliRLQLETTVKQKSTAESELK-QLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEelkrkaeaekeaakqkqk 1578
Cdd:TIGR00606 796 ---RFQMELKDVERKIAQQAAKlQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQD------------------ 854
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1579 aledlenlkRQAEEAERQVKQAEIEKERqIQVAHVAAQKSAAAElqskhmSFVEKTSKLEESLKQEHGAVLQLQHEAAAL 1658
Cdd:TIGR00606 855 ---------QQEQIQHLKSKTNELKSEK-LQIGTNLQRRQQFEE------QLVELSTEVQSLIREIKDAKEQDSPLETFL 918
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1659 KKQQEDAERAREEAEKELEKWRQKANEAlrlrlqaEEEAHKKSLAQEDAEKqkeeaereakkraKAEDSALKQKEMAENE 1738
Cdd:TIGR00606 919 EKDQQEKEELISSKETSNKKAQDKVNDI-------KEKVKNIHGYMKDIEN-------------KIQDGKDDYLKQKETE 978
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1739 LERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEvvaaqQQRKQLEDELAKVRSEMDVLIQLKSK 1818
Cdd:TIGR00606 979 LNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRE-----NELKEVEEELKQHLKEMGQMQVLQMK 1053
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1927222982 1819 AEKETMSNSERSKQLLEVEA-TKMRDLAEEasKLRAIAEEAKHQRQVAEEE 1868
Cdd:TIGR00606 1054 QEHQKLEENIDLIKRNHVLAlGRQKGYEKE--IKHFKKELREPQFRDAEEK 1102
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
71-179 |
3.36e-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: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 71 KKTFTKWVNKHLIKSQ---------RQVTDLYEDLRDGHNLISLLEVLSGETLPrERdvvrsvRLPREKGRMRFHKLQNV 141
Cdd:cd21217 3 KEAFVEHINSLLADDPdlkhllpidPDGDDLFEALRDGVLLCKLINKIVPGTID-ER------KLNKKKPKNIFEATENL 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1927222982 142 QIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 179
Cdd:cd21217 76 NLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
63-182 |
3.58e-09 |
|
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: 57.60 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 63 ADERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRERDVvrsvrlprEKGRMRFHKLQNVQ 142
Cdd:cd21222 10 APEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPLHEYH--------LTPSTDDEKLHNVK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1927222982 143 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 182
Cdd:cd21222 82 LALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1735-1956 |
3.79e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 62.15 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1735 AENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQ 1814
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1815 lkskaekeTMSNSERSKQLLEV--EATKMRDLAEEASKLRAIAEEAK---HQRQVAEEEAARQRAEAERILKEKLAAISD 1889
Cdd:COG3883 94 --------ALYRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADAdllEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222982 1890 ATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRA 1956
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2841-2878 |
3.88e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 54.64 E-value: 3.88e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1927222982 2841 VLEAQCATGGIIDPINSHRVPNEIAYKQGQYDHEMNKI 2878
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2115-2643 |
3.98e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.21 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2115 LKEEYEKAKKLAKQAEAAKEKAEREAALLRQ-------QAEEAERQKAAAEQEAANQAKAQEDAERLRKEA--EFEAAKR 2185
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidlqtKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTvhELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2186 AQAE-----NAALKQKQQ----------------ADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVL--- 2241
Cdd:pfam15921 160 LKEDmledsNTQIEQLRKmmlshegvlqeirsilVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLkgr 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2242 ----DEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADN-----MKKL 2312
Cdd:pfam15921 240 ifpvEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNqnsmyMRQL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2313 AE---DAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKE----KMQAIQEASRLRAE-----AEMLQRQKDLAQEQAQ 2380
Cdd:pfam15921 320 SDlesTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEarteRDQFSQESGNLDDQlqkllADLHKREKELSLEKEQ 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2381 -------------------KLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKK 2441
Cdd:pfam15921 400 nkrlwdrdtgnsitidhlrRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2442 FKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIE 2521
Cdd:pfam15921 480 VVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAE 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2522 HEKT--VLQQTFLSEKEMLLK---KEKLIEEEKKRLESQFEE---EVKKAKALKDEQERQKQQMED-------EKKKL-- 2584
Cdd:pfam15921 560 KDKVieILRQQIENMTQLVGQhgrTAGAMQVEKAQLEKEINDrrlELQEFKILKDKKDAKIRELEArvsdlelEKVKLvn 639
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222982 2585 ------------QATMDAALNKQKEAEKEMHNKQKEMKELERKRleqeRILAEENQKLREKLQ-QLEEAQKD 2643
Cdd:pfam15921 640 agserlravkdiKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF----RNKSEEMETTTNKLKmQLKSAQSE 707
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4342-4376 |
4.35e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.41 E-value: 4.35e-09
10 20 30
....*....|....*....|....*....|....*
gi 1927222982 4342 QRLLEAQACTGGIIDPTTGERFSVTDATEKGLVDK 4376
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDP 35
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
65-184 |
5.28e-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: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 65 ERDRVQKKTFTKWVNKHLIKSQrqVTDLYEDLRDGHNLISLLEVLSgetLPRERDVVRSVRLPREKGRMRfhKLQNVQIA 144
Cdd:cd21331 18 EGETREERTFRNWMNSLGVNPH--VNHLYGDLQDALVILQLYEKIK---VPVDWNKVNKPPYPKLGANMK--KLENCNYA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1927222982 145 LDFLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 184
Cdd:cd21331 91 VELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1632-2021 |
5.42e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1632 EKTSKLEEsLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANealRLRLQAEEEAHKKSLAQEDAEKQk 1711
Cdd:COG4717 75 ELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ---LLPLYQELEALEAELAELPERLE- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1712 eeaerEAKKRAKAEDSALKQKEMAENELER-QRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVA 1790
Cdd:COG4717 150 -----ELEERLEELRELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1791 AQQQRKQLEDE---------------LAKVRSEMDVLIQLKSKAEKET-----------------MSNSERSKQLLEVEA 1838
Cdd:COG4717 225 LEEELEQLENEleaaaleerlkearlLLLIAAALLALLGLGGSLLSLIltiagvlflvlgllallFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1839 TKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDE 1918
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1919 A--YQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQR-RVVEEEIRILKLNFEKASSGKLDLELELNK 1995
Cdd:COG4717 385 EelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420
....*....|....*....|....*.
gi 1927222982 1996 LKNiAEETQQSKLRAEEEAEKLRKLA 2021
Cdd:COG4717 465 LEE-DGELAELLQELEELKAELRELA 489
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2198-2439 |
5.63e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.77 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2198 QADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELlkvkVQMEELL 2277
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----EERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2278 KLKLRIEEENQRLIKK-----DKDNTQKFLAKeADNMKKLAEDAARLsVEAQEAARlrqiaeDDLNQQRALADKMLKEKM 2352
Cdd:COG3883 89 GERARALYRSGGSVSYldvllGSESFSDFLDR-LSALSKIADADADL-LEELKADK------AELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2353 QAIQEASRLRAEaemLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQ 2432
Cdd:COG3883 161 ALKAELEAAKAE---LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
....*..
gi 1927222982 2433 AKAQEEA 2439
Cdd:COG3883 238 AAAAAAA 244
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1821-2154 |
6.91e-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: 62.45 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1821 KETMSNSERSKQLLEVEATKMRDLAEEasklraIAEEAKHQRQVAEEEAARQrAEAERilkeKLAAISDATRLKTEAE-- 1898
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEE------KAREVERRRKLEEAEKARQ-AEMDR----QAAIYAEQERMAMEREre 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1899 ---IALKEKEAENERLRRQAEDEAYQR----KALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEE- 1970
Cdd:pfam17380 350 lerIRQEERKRELERIRQEEIAMEISRmrelERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEq 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1971 ----EIRILKLNFEKASsgkldlELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAa 2046
Cdd:pfam17380 430 eearQREVRRLEEERAR------EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELE- 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2047 rqrqaaqdelDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEdtiMQTKLKEEYEKAKKLa 2126
Cdd:pfam17380 503 ----------ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRR---IQEQMRKATEERSRL- 568
|
330 340
....*....|....*....|....*...
gi 1927222982 2127 kqaeaakEKAEREAALLRQQAEEAERQK 2154
Cdd:pfam17380 569 -------EAMEREREMMRQIVESEKARA 589
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1263-1939 |
7.25e-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: 62.43 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1263 WLIRWINDAKQRQEKIQ---AVTITDSKTLKE-QLAQEK---KLLEEVEGNKDKVDEcQKYAKAYIDTIKdyelQLVAYK 1335
Cdd:pfam05483 93 WKVSIEAELKQKENKLQenrKIIEAQRKAIQElQFENEKvslKLEEEIQENKDLIKE-NNATRHLCNLLK----ETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1336 AQveplasplKKTKLDSASDNIIQEYVTLRTKYsELMTLTSQYIKFITDSQR-----RLEDEEKAAEKLKAEEQKKMAmm 1410
Cdd:pfam05483 168 AE--------KTKKYEYEREETRQVYMDLNNNI-EKMILAFEELRVQAENARlemhfKLKEDHEKIQHLEEEYKKEIN-- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1411 qaelDKQKQLAEVHAKAIAKAEK---------EAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELKnLSEQQIMDK 1481
Cdd:pfam05483 237 ----DKEKQVSLLLIQITEKENKmkdltflleESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIK-MSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1482 SKQVDDALQSRVK-IEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQ---VNEETQKKRM 1557
Cdd:pfam05483 312 QKALEEDLQIATKtICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQlkiITMELQKKSS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1558 AEEELKRKAEAEKEAAKQKQKALEDLENL---KRQAEEAERQVKQAEIE-----KERQIQVAHVAAQ------------- 1616
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKILAEDEKLldeKKQFEKIAEELKGKEQElifllQAREKEIHDLEIQltaiktseehylk 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1617 --KSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAE 1694
Cdd:pfam05483 472 evEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELE 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1695 EEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQR 1774
Cdd:pfam05483 552 SVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQL 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1775 SLLEDELYRLKNEVVAAQQQRKQLEDELAKVrsemdvlIQLKSKAEKETMSNSERSKQLLEvEATKMRD-----LAEEAS 1849
Cdd:pfam05483 632 NAYEIKVNKLELELASAKQKFEEIIDNYQKE-------IEDKKISEEKLLEEVEKAKAIAD-EAVKLQKeidkrCQHKIA 703
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1850 KLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKlaaisdaTRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQA 1929
Cdd:pfam05483 704 EMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQ-------SSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEA 776
|
730
....*....|
gi 1927222982 1930 NQHKQQIEEK 1939
Cdd:pfam05483 777 KENTAILKDK 786
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
72-178 |
8.52e-09 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 56.19 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 72 KTFTKWVNKHLIKS--QRQVTDLYEDLRDGHNLISLLEVLSGETLPRERDVvrsvrlPREKGRMrfhkLQNVQIALDFLK 149
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGC------PRSQSQM----IENVDVCLSFLA 72
|
90 100
....*....|....*....|....*....
gi 1927222982 150 HRQVKLVNIRNDDIADGNPKLTLGLIWTI 178
Cdd:cd21286 73 ARGVNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1330-1882 |
8.71e-09 |
|
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: 62.15 E-value: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1330 QLVAYKAQveplaSPLKKTKLDSASDNIIQ---EYVTLRTKyseLMTLTSQYikfiTDSQRRLEdeeKAAEKLKAEEQKK 1406
Cdd:pfam10174 276 QMEVYKSH-----SKFMKNKIDQLKQELSKkesELLALQTK---LETLTNQN----SDCKQHIE---VLKESLTAKEQRA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1407 mAMMQAELDKQKQLAEVHAKAIAKAEKEAQEL---KLRMQEEVNRREDaVVDAEKQKHNIqleLHE-LKNLSEQqIMDKS 1482
Cdd:pfam10174 341 -AILQTEVDALRLRLEEKESFLNKKTKQLQDLteeKSTLAGEIRDLKD-MLDVKERKINV---LQKkIENLQEQ-LRDKD 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1483 KQVDDaLQSRVKieeeirliRLQLETtvkqkSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQvneetqkkrmaeeel 1562
Cdd:pfam10174 415 KQLAG-LKERVK--------SLQTDS-----SNTDTALTTLEEALSEKERIIERLKEQREREDRE--------------- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1563 krkaeaekeaakqkqkALEDLENLKRQAEEAERQVKQAEIEKerqiqvahvAAQKSAAAELQSKHMSFVEKTSKLEESLK 1642
Cdd:pfam10174 466 ----------------RLEELESLKKENKDLKEKVSALQPEL---------TEKESSLIDLKEHASSLASSGLKKDSKLK 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1643 QEHGAVLQLQHEAAALKKQQEDAERAREEAekelekwRQKANEALRLRLQAEEEAHKKslaqEDAEKQKEEAEREAkkra 1722
Cdd:pfam10174 521 SLEIAVEQKKEECSKLENQLKKAHNAEEAV-------RTNPEINDRIRLLEQEVARYK----EESGKAQAEVERLL---- 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1723 kaedSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLED-- 1800
Cdd:pfam10174 586 ----GILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEElm 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1801 -ELAKVRSEMDVLIQ-----LKSKAEKETMSNS---ERSKQLLEVEATKMRDLAEEASKLRA-IA--EEAKHQRQVAEEE 1868
Cdd:pfam10174 662 gALEKTRQELDATKArlsstQQSLAEKDGHLTNlraERRKQLEEILEMKQEALLAAISEKDAnIAllELSSSKKKKTQEE 741
|
570
....*....|....
gi 1927222982 1869 AARQRAEAERILKE 1882
Cdd:pfam10174 742 VMALKREKDRLVHQ 755
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2004-2205 |
9.25e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.98 E-value: 9.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2004 QQSKLRAEEEAEKLRKlaleeekRRREAEEKVKKIAAAEEEAARQrqaaqdeldrlKKKAEEARKQKDDADKEAEKQILM 2083
Cdd:PRK09510 79 EQRKKKEQQQAEELQQ-------KQAAEQERLKQLEKERLAAQEQ-----------KKQAEEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2084 AQQAAQKCSAAEQQVQSVLAQQKEDtimQTKLKEEYEKAKklaKQAEAAKEKAEREAAlLRQQAEEAERQKAAAEQEAAN 2163
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAAKKAAA---EAKKKAEAEAAK---KAAAEAKKKAEAEAA-AKAAAEAKKKAEAEAKKKAAA 213
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1927222982 2164 QAKAQEDAERLRKEAEFEAAKRAQAENAAlKQKQQADAEMAK 2205
Cdd:PRK09510 214 EAKKKAAAEAKAAAAKAAAEAKAAAEKAA-AAKAAEKAAAAK 254
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1588-1938 |
1.23e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.89 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1588 RQAEEAERQVKQA-EIEKERQIQVAHVAAQKSAAAELQSKhmsfVEKTSKLEESLKQEH-GAVLQLQHEAAALKKQQEda 1665
Cdd:COG3096 275 RHANERRELSERAlELRRELFGARRQLAEEQYRLVEMARE----LEELSARESDLEQDYqAASDHLNLVQTALRQQEK-- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1666 erareeaekeLEKWRQKANEA-LRLRLQAE--EEAHKKslaQEDAEKQKEEAEREAKkRAKaedSALKQKEMAENELERq 1742
Cdd:COG3096 349 ----------IERYQEDLEELtERLEEQEEvvEEAAEQ---LAEAEARLEAAEEEVD-SLK---SQLADYQQALDVQQT- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1743 RKVAESTAQQKLTAEQELIRLRA-DFDNAEQQRSLLEDELYRLkNEVVAAQQQRKQLEDElakVRSEMDVLIQLKSK--A 1819
Cdd:COG3096 411 RAIQYQQAVQALEKARALCGLPDlTPENAEDYLAAFRAKEQQA-TEEVLELEQKLSVADA---ARRQFEKAYELVCKiaG 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1820 EKETMSNSERSKQLLEvEATKMRDLAEEASKLRAiaeeakhqrQVAE-EEAARQRAEAERILKEKLAAISDATRLKTEAE 1898
Cdd:COG3096 487 EVERSQAWQTARELLR-RYRSQQALAQRLQQLRA---------QLAElEQRLRQQQNAERLLEEFCQRIGQQLDAAEELE 556
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1927222982 1899 IALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEE 1938
Cdd:COG3096 557 ELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE 596
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2078-2659 |
1.28e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 61.74 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2078 EKQILMAQQAAQkcsaaeqqvqsvlaQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALL------RQQAEEAE 2151
Cdd:PRK10246 232 EKQLLTAQQQQQ--------------QSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALslaqpaRQLRPHWE 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2152 RQKAAAEQEAANQAKAQEDAERLRKEAefeaAKRAQAENAALKQKQQADAEMAKHKK-LAEQ---------------TLK 2215
Cdd:PRK10246 298 RIQEQSAALAHTRQQIEEVNTRLQSTM----ALRARIRHHAAKQSAELQAQQQSLNTwLAEHdrfrqwnnelagwraQFS 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2216 QKFQVEQELTKVKLKLDETDKQKSVL-DEELQRLKDEVDDAVKQRGQ---VEEELLKVKVQMEELLKLKLRIEEENQRLI 2291
Cdd:PRK10246 374 QQTSDREQLRQWQQQLTHAEQKLNALpAITLTLTADEVAAALAQHAEqrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVT 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2292 KKDKDNTQKFLAKEAD---------NMKKLAEDAARLSVEAQEAARLR-------------------QIAEDDLNQQRAl 2343
Cdd:PRK10246 454 QEQTQRNAALNEMRQRykektqqlaDVKTICEQEARIKDLEAQRAQLQagqpcplcgstshpaveayQALEPGVNQSRL- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2344 aDKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDkqlmQQRLDEETEEYQKSLEAERKRQLEI---IAESEK 2420
Cdd:PRK10246 533 -DALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQE----EQALTQQWQAVCASLNITLQPQDDIqpwLDAQEE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2421 LKLQVSQLSEAQ------AKAQEEAKKFKKQADsiasrlhetelatQEKMTVVEKLEVARLTSSKEADdlrkaiadleke 2494
Cdd:PRK10246 608 HERQLRLLSQRHelqgqiAAHNQQIIQYQQQIE-------------QRQQQLLTALAGYALTLPQEDE------------ 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2495 ksrlkkEAEDLQNKSKEMADAQQKQIEHekTVLQQTfLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAK----ALKDEQ 2570
Cdd:PRK10246 663 ------EASWLATRQQEAQSWQQRQNEL--TALQNR-IQQLTPLLETLPQSDDLPHSEETVALDNWRQVHeqclSLHSQL 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2571 ERQKQQMEDEKKKL---QATMDAALNKQKEAEKE-----------MHNKQKEMKELERKRLEQERILAEENQKLREKLQQ 2636
Cdd:PRK10246 734 QTLQQQDVLEAQRLqkaQAQFDTALQASVFDDQQaflaalldeetLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQH 813
|
650 660
....*....|....*....|...
gi 1927222982 2637 LEEAQKDQPDKEVIHVTMVETTK 2659
Cdd:PRK10246 814 RPDGLDLTVTVEQIQQELAQLAQ 836
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1505-1753 |
1.43e-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: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1505 QLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAeaekeaakqkqkalEDLE 1584
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE--------------AELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1585 NLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKhmsfvEKTSKLEESLKQEHGAVLQLQHEAAALKKQQED 1664
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSP-----EDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1665 AERAREEAEKELEKWRQ--KANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQ 1742
Cdd:COG4942 162 LAALRAELEAERAELEAllAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
250
....*....|.
gi 1927222982 1743 RKVAESTAQQK 1753
Cdd:COG4942 242 RTPAAGFAALK 252
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
192-294 |
1.67e-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: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 192 QSEDMTAKEKLLLWSQ-RMTDgyqgIRCDNFTTSWRDGKLFNAVIHKHYPRLV-DMGRVYRQTNLENLEQAFGVAERDLG 269
Cdd:cd21315 11 DGKGPTPKQRLLGWIQsKVPD----LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLD 86
|
90 100
....*....|....*....|....*
gi 1927222982 270 VTRLLDPEDVDVPHPDEKSIITYVS 294
Cdd:cd21315 87 VPQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2242-2451 |
1.91e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2242 DEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLiKKDKDNTQKFLAKEADNMKKLAEDAARLSV 2321
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2322 EAQEAARLRQIAE--------DDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRL 2393
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 2394 DEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIAS 2451
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2282-2518 |
2.00e-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: 59.78 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2282 RIEEENQRL--IKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEAS 2359
Cdd:COG4942 21 AAAEAEAELeqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2360 RLRAE-AEMLQRQKDLAQEQAQKLL---EDKQLMQQRLdeeteEYQKSLEAERKRQLEiiaeseKLKLQVSQLSEAQAKA 2435
Cdd:COG4942 101 AQKEElAELLRALYRLGRQPPLALLlspEDFLDAVRRL-----QYLKYLAPARREQAE------ELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2436 QEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADA 2515
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 1927222982 2516 QQK 2518
Cdd:COG4942 250 ALK 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1388-2147 |
2.03e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1388 RLEDEEKAAEKLKaEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKlrmqEEVNRREDAVVDAEKQKHNIQLEL 1467
Cdd:PRK03918 156 GLDDYENAYKNLG-EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVL----REINEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1468 HELKNLSEQqIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKqkstaesELKQLRDRAAEAEKLRKAAqEEAEKLRKQ 1547
Cdd:PRK03918 231 KELEELKEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKK-------EIEELEEKVKELKELKEKA-EEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1548 VNEETQKKRMAEEELkrkaeaekeaakqkqkaledlENLKRQAEEAERQVKQAEIEKERqiqvahvaaqksaaaelqskh 1627
Cdd:PRK03918 302 YEEYLDELREIEKRL---------------------SRLEEEINGIEERIKELEEKEER--------------------- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1628 msfVEKTSKLEESLKQEHGAvlqlqheaaalkkqqedaerareeaekeLEKWRQKANEALRLrlQAEEEAHKKSLAQEDA 1707
Cdd:PRK03918 340 ---LEELKKKLKELEKRLEE----------------------------LEERHELYEEAKAK--KEELERLKKRLTGLTP 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1708 EKQKEEAEREAKKRAKAEDsalkqkemAENELERQRKVAESTAQQKLTAEQELirLRADFDNAEQQRSLLEDELYRLKNE 1787
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEE--------EISKITARIGELKKEIKELKKAIEEL--KKAKGKCPVCGRELTEEHRKELLEE 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1788 VVAaqqqrkqledELAKVRSEMDVLIQLKSKAEKEtmsnserskqllEVEATKMRDLAEEASKLRAIAEEAKHqrqvaee 1867
Cdd:PRK03918 457 YTA----------ELKRIEKELKEIEEKERKLRKE------------LRELEKVLKKESELIKLKELAEQLKE------- 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1868 eaarqraeaeriLKEKLAAISDATrlkteaeiaLKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSS 1947
Cdd:PRK03918 508 ------------LEEKLKKYNLEE---------LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1948 EAEMERQ---RAIVDDTLKQRRVVEEEIRILKLNFEK---ASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLa 2021
Cdd:PRK03918 567 ELEEELAellKELEELGFESVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL- 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2022 leeekRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKqilmaqqaaqkcsaaeqqvqsv 2101
Cdd:PRK03918 646 -----RKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK---------------------- 698
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1927222982 2102 LAQQKEDtimQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQA 2147
Cdd:PRK03918 699 LKEELEE---REKAKKELEKLEKALERVEELREKVKKYKALLKERA 741
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1677-2428 |
2.17e-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: 61.01 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1677 EKWRQKAN--EALRLRLQAEEEAHKKSLAQEdAEKQKEEAEREAKKRakaedsalkqKEMAENELERQRKVAESTaqqkl 1754
Cdd:pfam12128 244 TKLQQEFNtlESAELRLSHLHFGYKSDETLI-ASRQEERQETSAELN----------QLLRTLDDQWKEKRDELN----- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1755 taeQELIRLRADFDNAEQQRSLLEDELYRLKNEVVaaqQQRKQLEDELAKVRSEMdvliqlkskaeketmSNSERSKQLL 1834
Cdd:pfam12128 308 ---GELSAADAAVAKDRSELEALEDQHGAFLDADI---ETAAADQEQLPSWQSEL---------------ENLEERLKAL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1835 EveaTKMRDLAEEASKLRA-IAEEAKHQRQVAEEEAARQRAEAERilkeKLAAISDA-----TRLKTEAEIALKEKEAEN 1908
Cdd:pfam12128 367 T---GKHQDVTAKYNRRRSkIKEQNNRDIAGIKDKLAKIREARDR----QLAVAEDDlqaleSELREQLEAGKLEFNEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1909 ERLRRQAEDEayqrKALEDQAnqhkqQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLD 1988
Cdd:pfam12128 440 YRLKSRLGEL----KLRLNQA-----TATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQ 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1989 LELELNKLKNIAEETQQ----------SKLRAEEE--AEKLRKLALEEEKRRREAEEKVKKIAAAEEE------------ 2044
Cdd:pfam12128 511 ASRRLEERQSALDELELqlfpqagtllHFLRKEAPdwEQSIGKVISPELLHRTDLDPEVWDGSVGGELnlygvkldlkri 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2045 AARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTI--------MQTKLK 2116
Cdd:pfam12128 591 DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRrlfdekqsEKDKKN 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2117 EEYEKAKK--------LAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQA 2188
Cdd:pfam12128 671 KALAERKDsanerlnsLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELK 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2189 --------ENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQksvldeELQRLKDEVDDavkqrg 2260
Cdd:pfam12128 751 aletwykrDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQ------RRPRLATQLSN------ 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2261 qVEEELLKVKVQMEellklklRIEEENQRLIKKdkdntqkfLAKEADNMKKLA----EDAARLSVEAQEAARLRQIAEDD 2336
Cdd:pfam12128 819 -IERAISELQQQLA-------RLIADTKLRRAK--------LEMERKASEKQQvrlsENLRGLRCEMSKLATLKEDANSE 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2337 lnqqraladkmlkekmQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLED-----KQLMQQRLDEETEEYQKSLEAERKRQ 2411
Cdd:pfam12128 883 ----------------QAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREEDHYQNDKG 946
|
810
....*....|....*..
gi 1927222982 2412 LEIIAESEKLKlQVSQL 2428
Cdd:pfam12128 947 IRLLDYRKLVP-YLEQW 962
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1582-1997 |
2.39e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 60.84 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1582 DLENLKRQAEEAE--RQVKQAEIEKERQIQVAHVAAQKSAAAELQsKHMSFVEKTSKLEESLKQEhgaVLQLQHEAAALK 1659
Cdd:PRK10929 24 DEKQITQELEQAKaaKTPAQAEIVEALQSALNWLEERKGSLERAK-QYQQVIDNFPKLSAELRQQ---LNNERDEPRSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1660 KQQEDAERARE---EAEKELEKWRQKANEALRLRLQAEeeahkkSLAQedAEKQKEEAER---EAKKRAKAEDSALKQKE 1733
Cdd:PRK10929 100 PNMSTDALEQEilqVSSQLLEKSRQAQQEQDRAREISD------SLSQ--LPQQQTEARRqlnEIERRLQTLGTPNTPLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1734 MAENELeRQrkvAESTAQQKLTAEQELIRLRAdfdNAEQqrslledELYRLKNEVvaAQQQRKQLEDELAKVRSemdvli 1813
Cdd:PRK10929 172 QAQLTA-LQ---AESAALKALVDELELAQLSA---NNRQ-------ELARLRSEL--AKKRSQQLDAYLQALRN------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1814 QLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAaisdatrL 1893
Cdd:PRK10929 230 QLNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQA-------L 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1894 KTEAEIA--LKEKEAENERLRRQA----EDEAYQRkaLEDQANQ---HKQQIEEkivLLKKSSEAEMERQRAIVDDTLKQ 1964
Cdd:PRK10929 303 NTLREQSqwLGVSNALGEALRAQVarlpEMPKPQQ--LDTEMAQlrvQRLRYED---LLNKQPQLRQIRQADGQPLTAEQ 377
|
410 420 430
....*....|....*....|....*....|...
gi 1927222982 1965 RRVVEEEIRILKLNFEKASSGKLDLELELNKLK 1997
Cdd:PRK10929 378 NRILDAQLRTQRELLNSLLSGGDTLILELTKLK 410
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2046-2254 |
2.45e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.82 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2046 ARQRQAAQDELDRLKKKAEEARKQKDD-ADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEdtimqtkLKEEYEKAKK 2124
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQRKKKEQQQAEElQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQA-------ALKQKQAEEA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2125 LAKQAEAAKEKAEREAALLRQQAEEAERQKaAAEQEAANQAKAQEDAerlRKEAEFEAAKRAQAE---NAALKQKQQADA 2201
Cdd:PRK09510 138 AAKAAAAAKAKAEAEAKRAAAAAKKAAAEA-KKKAEAEAAKKAAAEA---KKKAEAEAAAKAAAEakkKAEAEAKKKAAA 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1927222982 2202 EmAKHKKLAEqtlkQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDD 2254
Cdd:PRK09510 214 E-AKKKAAAE----AKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4420-4458 |
2.46e-08 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 52.33 E-value: 2.46e-08
10 20 30
....*....|....*....|....*....|....*....
gi 1927222982 4420 FLEIQYLTGGLIEPDVEGRVSLDESIRKGTIDARTAQKL 4458
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2056-2451 |
2.64e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2056 LDRLKKKAEEARKQK-------DDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQ 2128
Cdd:COG4717 48 LERLEKEADELFKPQgrkpelnLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2129 AEAAKE--KAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKH 2206
Cdd:COG4717 128 LPLYQEleALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2207 KKLAEQTLKQKfQVEQELTKVKLKLDETDKQKSVLDEELQRLK----------------DEVDDAVKQRGQV-------- 2262
Cdd:COG4717 208 LAELEEELEEA-QEELEELEEELEQLENELEAAALEERLKEARlllliaaallallglgGSLLSLILTIAGVlflvlgll 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2263 ---------EEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIA 2333
Cdd:COG4717 287 allflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2334 EDDLNQQRALA------DKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLmqQRLDEETEEYQKSLEAE 2407
Cdd:COG4717 367 ELEQEIAALLAeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEEL 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2408 RKRQLEIIAESEKLKLQVSQL------SEAQAKAQEEAKKFKKQADSIAS 2451
Cdd:COG4717 445 EEELEELREELAELEAELEQLeedgelAELLQELEELKAELRELAEEWAA 494
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2009-2453 |
2.85e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2009 RAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEK--QILMAQQ 2086
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2087 AAQKCSAAEQQVQSVlaqqkedtimQTKLKEEYEKAKKLaKQAEAAKEKAEREAALLRQQAEEAERQkaAAEQEAANQAK 2166
Cdd:COG4717 130 LYQELEALEAELAEL----------PERLEELEERLEEL-RELEEELEELEAELAELQEELEELLEQ--LSLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2167 AQEDAERLRKEAEF--EAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKF-------------------------- 2218
Cdd:COG4717 197 LAEELEELQQRLAEleEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaallallglggsllsliltia 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2219 ------------------QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRgqvEEELLKVKVQMEELLKLK 2280
Cdd:COG4717 277 gvlflvlgllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS---PEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2281 LRIEEENQRLIKKDKDNTQKFLAKEADnmkklAEDAARLSVEAQEAARLRQIAE--DDLNQQRALADKMLKEKMQAIQEA 2358
Cdd:COG4717 354 REAEELEEELQLEELEQEIAALLAEAG-----VEDEEELRAALEQAEEYQELKEelEELEEQLEELLGELEELLEALDEE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2359 sRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLD--EETEEYQKsLEAERKRQLEIIAESEK----LKLQVSQLSEAQ 2432
Cdd:COG4717 429 -ELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAE-LLQELEELKAELRELAEewaaLKLALELLEEAR 506
|
490 500
....*....|....*....|..
gi 1927222982 2433 AKAQEE-AKKFKKQADSIASRL 2453
Cdd:COG4717 507 EEYREErLPPVLERASEYFSRL 528
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1294-1609 |
3.53e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1294 AQEKKLLEEV----EGNKDKVDECQKYAKAyidTIKDYELQLVAYKAQVEPLASPLKKTKLDSASDNIIQEYVTLRTKYS 1369
Cdd:PTZ00121 1479 AEEAKKADEAkkkaEEAKKKADEAKKAAEA---KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1370 ELmtltsqyikfitdsqRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQ---KQLAEVHAKAIAKAEKEAQELK------- 1439
Cdd:PTZ00121 1556 EL---------------KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeeARIEEVMKLYEEEKKMKAEEAKkaeeaki 1620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1440 ----LRMQEEVNRREDAVV--DAEKQKHNIQLELHELKN-LSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQ 1512
Cdd:PTZ00121 1621 kaeeLKKAEEEKKKVEQLKkkEAEEKKKAEELKKAEEENkIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1513 KSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEE 1592
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
330
....*....|....*..
gi 1927222982 1593 AERQVKQAEIEKERQIQ 1609
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVD 1797
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1727-1939 |
4.09e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.07 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1727 SALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAK-- 1804
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1805 --------VRSEMDVLiqLKSKAEKETMSNSERSKQLLEveatKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEA 1876
Cdd:COG3883 93 ralyrsggSVSYLDVL--LGSESFSDFLDRLSALSKIAD----ADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927222982 1877 ERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEK 1939
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1588-2021 |
4.63e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1588 RQAEEAERQVKQA-EIEKERQIQVAHVAAQKSAAAELQSKhmsfVEKTSKLEESLKQEHGAV---LQLQHEAAALKKQqe 1663
Cdd:PRK04863 276 RHANERRVHLEEAlELRRELYTSRRQLAAEQYRLVEMARE----LAELNEAESDLEQDYQAAsdhLNLVQTALRQQEK-- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1664 daerareeaekeLEKWRQ---KANEALRLRLQAEEEAHKKslaQEDAEKQKEEAEREAKkRAKAEDSALKQkemAENELE 1740
Cdd:PRK04863 350 ------------IERYQAdleELEERLEEQNEVVEEADEQ---QEENEARAEAAEEEVD-ELKSQLADYQQ---ALDVQQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1741 RqRKVAESTAQQKLTAEQELIRLRA-DFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKA 1819
Cdd:PRK04863 411 T-RAIQYQQAVQALERAKQLCGLPDlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEV 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1820 EKETMSNSERSkqlLEVEATKMRDLAEEASKLRAIAEEAKhQRQVAEEEAARQRAEAERILKEKLAAISDATRLkteaei 1899
Cdd:PRK04863 490 SRSEAWDVARE---LLRRLREQRHLAEQLQQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQL------ 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1900 aLKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEkivLLKKSSE-----AEMERQRAIVDDTLKQRRVVEEEIRI 1974
Cdd:PRK04863 560 -QEELEARLESLSESVSEARERRMALRQQLEQLQARIQR---LAARAPAwlaaqDALARLREQSGEEFEDSQDVTEYMQQ 635
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1927222982 1975 LKLNFEKASSGKLDLELELNKLKNIAEETQQsklRAEEEAEKLRKLA 2021
Cdd:PRK04863 636 LLERERELTVERDELAARKQALDEEIERLSQ---PGGSEDPRLNALA 679
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1581-1814 |
4.98e-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: 58.32 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1581 EDLENLKRQAEEAERQvKQAEIEKERQIQVAHVAAQKSAAAELQSKHmsfVEKTSKLEESLKQEHGAVLQLQHEAAALKK 1660
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQ-RAAEQARQKELEQRAAAEKAAKQAEQAAKQ---AEEKQKQAEEAKAKQAAEAKAKAEAEAERK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1661 QQEdaerareeaekelekwrqkanealRLRLQAEEEAHKKslAQEDAEKQKEEAEREAKKRAKAEDSALKQK--EMAENE 1738
Cdd:TIGR02794 144 AKE------------------------EAAKQAEEEAKAK--AAAEAKKKAEEAKKKAEAEAKAKAEAEAKAkaEEAKAK 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222982 1739 LERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQ 1814
Cdd:TIGR02794 198 AEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQ 273
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2417-2645 |
5.05e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2417 ESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETElatqekmtvveklevarltssKEADDLRKAIADLEKEKS 2496
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ---------------------AELEALQAEIDKLQAEIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2497 RLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQ-------QTFLSEKEMLLkkeklieeekkRLESQFEEEVKKAKALKDE 2569
Cdd:COG3883 76 EAEAEIEERREELGERARALYRSGGSVSYLDVllgsesfSDFLDRLSALS-----------KIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222982 2570 QERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQP 2645
Cdd:COG3883 145 LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1783-2529 |
5.51e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.26 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1783 RLKNEVVAAQQQRKQLEDELAKVRSEM--------DVLIQLKSKAEKETMSNSE------RSKQL---LEVEATKMRDLA 1845
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEKKLKTIKNELknkekelkNLDKNLNKDEEKINNSNNKikileqQIKDLndkLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1846 EEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEaeiaLKEKEAENERLRRQAEDeayqrkaL 1925
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE----LEKLNNKYNDLKKQKEE-------L 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1926 EDQANQHKQQIEEKivllkksseaemerqRAIVDDTLKQRRVVEEEIRILKLNFEK---ASSGKLDLELELNKLKNIAEE 2002
Cdd:TIGR04523 172 ENELNLLEKEKLNI---------------QKNIDKIKNKLLKLELLLSNLKKKIQKnksLESQISELKKQNNQLKDNIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2003 TQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKD-DADKEAEKQI 2081
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqDWNKELKSEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2082 lmAQQAAQKcsaaeQQVQSVLAQQKEDTimqTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEA 2161
Cdd:TIGR04523 317 --KNQEKKL-----EEIQNQISQNNKII---SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2162 ANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEmakHKKLAEQTLKQKFQV---EQELTKVKLKLDETDKQK 2238
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE---IERLKETIIKNNSEIkdlTNQDSVKELIIKNLDNTR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2239 SVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKlaedaar 2318
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK------- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2319 lsvEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEasrLRAEAEMLQRqkdlAQEQAQKLLEDKQLMQQRLDEETE 2398
Cdd:TIGR04523 537 ---ESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEE---LKQTQKSLKK----KQEEKQELIDQKEKEKKDLIKEIE 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2399 EYQKSLEaERKRQLEII-AESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVeklevarlts 2477
Cdd:TIGR04523 607 EKEKKIS-SLEKELEKAkKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI---------- 675
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1927222982 2478 skeaDDLRKAIADLEKEKSRLKKEA--EDLQNKSKEMADAQQKQIEHEKTVLQQ 2529
Cdd:TIGR04523 676 ----DDIIELMKDWLKELSLHYKKYitRMIRIKDLPKLEEKYKEIEKELKKLDE 725
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
70-181 |
6.67e-08 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 53.66 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 70 QKKTFTKWVNKHLIKSQrqVTDLYEDLRDGHNLISLLEVLSGETLPRERDVVRSVRLPrekgrmrFHKLQNVQIALDFLK 149
Cdd:cd21299 5 EERCFRLWINSLGIDTY--VNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMP-------FKKVENCNQVVKIGK 75
|
90 100 110
....*....|....*....|....*....|..
gi 1927222982 150 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 181
Cdd:cd21299 76 QLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1440-2348 |
6.94e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1440 LRMQEEVNRREDAVVDAEKQKHNIQLELHElknlSEQQIMDKSKQVDDALQSRVKIEEEIRLI--RLQLETTV----KQK 1513
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTSRRQLAA----EQYRLVEMARELAELNEAESDLEQDYQAAsdHLNLVQTAlrqqEKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1514 STAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQvneetqkKRMAEEELKRKAEAekeaakqkqkaLED----LENLKRQ 1589
Cdd:PRK04863 351 ERYQADLEELEERLEEQNEVVEEADEQQEENEAR-------AEAAEEEVDELKSQ-----------LADyqqaLDVQQTR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1590 AEeAERQVKQAEIEKERQIQVAHVAAQKSAA--AELQSKhmsfvektsklEESLKQEhgaVLQLQHE---AAALKKQQEd 1664
Cdd:PRK04863 413 AI-QYQQAVQALERAKQLCGLPDLTADNAEDwlEEFQAK-----------EQEATEE---LLSLEQKlsvAQAAHSQFE- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1665 aerareeaekelekwrqKANEALRlRLQAE---EEAHKKslAQE---DAEKQKEEAEREAKKRAKAedSALKQKEMAENE 1738
Cdd:PRK04863 477 -----------------QAYQLVR-KIAGEvsrSEAWDV--AREllrRLREQRHLAEQLQQLRMRL--SELEQRLRQQQR 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1739 LERQRKVAESTAQQKLTAEQELIRLRADfdnAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSK 1818
Cdd:PRK04863 535 AERLLAEFCKRLGKNLDDEDELEQLQEE---LEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1819 AEK------ETMSNSERSKQLLEVEATKMRDLAEE----ASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAIS 1888
Cdd:PRK04863 612 LARlreqsgEEFEDSQDVTEYMQQLLERERELTVErdelAARKQALDEEIERLSQPGGSEDPRLNALAERFGGVLLSEIY 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1889 DATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDqanqhkqqIEEKIVLLK--------KSSEAEmERQRAIVDd 1960
Cdd:PRK04863 692 DDVSLEDAPYFSALYGPARHAIVVPDLSDAAEQLAGLED--------CPEDLYLIEgdpdsfddSVFSVE-ELEKAVVV- 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1961 tlkqrRVVEEEIRILKLNfekassgkldlelELNKLKNIAEETQQSKLRAE--EEAEKLRKLAleeekrrreaeEKVKKI 2038
Cdd:PRK04863 762 -----KIADRQWRYSRFP-------------EVPLFGRAAREKRIEQLRAEreELAERYATLS-----------FDVQKL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2039 AAAEEEAARQRQAA-----QDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQK--EDTIM 2111
Cdd:PRK04863 813 QRLHQAFSRFIGSHlavafEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNllADETL 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2112 QTKLKE------EYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAE--RQKAAAEQEAANQAKAQEDA--ERLRKEAEF- 2180
Cdd:PRK04863 893 ADRVEEireqldEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEqlKQDYQQAQQTQRDAKQQAFAltEVVQRRAHFs 972
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2181 -EAAKRAQAENAALKQKQQADAEMAKHKKL-AEQTLKQKFQVEQELTKVKLKLDETdkqKSVLDEELQRLKDEVDD---- 2254
Cdd:PRK04863 973 yEDAAEMLAKNSDLNEKLRQRLEQAEQERTrAREQLRQAQAQLAQYNQVLASLKSS---YDAKRQMLQELKQELQDlgvp 1049
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2255 --------AVKQRGQVEEELLKVKVQMEELLKLKLRIEEE----NQRLIKKDKDNTQkfLAKEADNMKKLAEDAARLSVE 2322
Cdd:PRK04863 1050 adsgaeerARARRDELHARLSANRSRRNQLEKQLTFCEAEmdnlTKKLRKLERDYHE--MREQVVNAKAGWCAVLRLVKD 1127
|
970 980
....*....|....*....|....*...
gi 1927222982 2323 AQEAARL--RQIAEDDLNQQRALADKML 2348
Cdd:PRK04863 1128 NGVERRLhrRELAYLSADELRSMSDKAL 1155
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1533-2011 |
7.64e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1533 LRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERqiqvah 1612
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK------ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1613 vaaqksaaAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAErareEAEKELEKWRQKANEALRLRLQ 1692
Cdd:COG4717 121 --------LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE----ELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1693 AEEEAHKKSLAQ-EDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELER---QRKVAESTAQQKLTAEQELIRLRADFD 1768
Cdd:COG4717 189 ATEEELQDLAEElEELQQRLAELEEELEEAQEELEELEEELEQLENELEAaalEERLKEARLLLLIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1769 NAEQQRS----------LLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEA 1838
Cdd:COG4717 269 LSLILTIagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1839 TK--MRDLAEEASKLRAIAEEAK-----HQRQVAEEEAARQRAEAERI---LKEKLAAISDATRLKTEAEIALKEKEAEn 1908
Cdd:COG4717 349 LQelLREAEELEEELQLEELEQEiaallAEAGVEDEEELRAALEQAEEyqeLKEELEELEEQLEELLGELEELLEALDE- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1909 ERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKksseaEMERQRAIvDDTLKQRRVVEEEIRILklnFEKASSGKLD 1988
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELE-----QLEEDGEL-AELLQELEELKAELREL---AEEWAALKLA 498
|
490 500
....*....|....*....|...
gi 1927222982 1989 LELeLNKLKNIAEETQQSKLRAE 2011
Cdd:COG4717 499 LEL-LEEAREEYREERLPPVLER 520
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2123-2644 |
8.92e-08 |
|
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: 58.60 E-value: 8.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2123 KKLAKQAEAAKEKAEREA-ALLRQQAEEAERQKAAaeqeaanqakaQEDAERLRK-EAEFEAAKRAQAENAalKQKQQAD 2200
Cdd:pfam05557 19 KQMELEHKRARIELEKKAsALKRQLDRESDRNQEL-----------QKRIRLLEKrEAEAEEALREQAELN--RLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2201 AEMAKHKKLAEQTLKQKFQV----EQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEEL 2276
Cdd:pfam05557 86 EALNKKLNEKESQLADAREVisclKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2277 LKLKLRIEEENQRLIKKDKDntqkflAKEADNMKKLAEDAARLSVEAQ----EAARLRQIAEDDLNQQRALADkmLKEKM 2352
Cdd:pfam05557 166 AEAEQRIKELEFEIQSQEQD------SEIVKNSKSELARIPELEKELErlreHNKHLNENIENKLLLKEEVED--LKRKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2353 QAIQEAsrlRAEAEMLQRQKDLAQeqaQKLLEDKQLMQQRLDE--ETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSE 2430
Cdd:pfam05557 238 EREEKY---REEAATLELEKEKLE---QELQSWVKLAQDTGLNlrSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2431 AQAKAQEEAKKFKKQADSIASRLHETElatqekmTVVEKLEVARLTSSKEADDLRKAIADLEKE---------KSRLKKE 2501
Cdd:pfam05557 312 ARRELEQELAQYLKKIEDLNKKLKRHK-------ALVRRLQRRVLLLTKERDGYRAILESYDKEltmsnyspqLLERIEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2502 AEDLQNKSKemadAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLE----SQFEEEVKKAKALKDEQERQKQQM 2577
Cdd:pfam05557 385 AEDMTQKMQ----AHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESladpSYSKEEVDSLRRKLETLELERQRL 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222982 2578 EDEKKKLQATMdAALNKQKEAE----KEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQ 2644
Cdd:pfam05557 461 REQKNELEMEL-ERRCLQGDYDpkktKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQV 530
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1861-2640 |
1.02e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1861 QRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEiALKEKEAENERLRRQAEDeayqRKALEDQANQHKQQIEEKI 1940
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELA-ELNEAESDLEQDYQAASD----HLNLVQTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1941 VLLKKSSEAeMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKlRAEEEAEKLRKL 2020
Cdd:PRK04863 355 ADLEELEER-LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAV-QALERAKQLCGL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2021 AleeekrrreaeekvkkiaaaeeeaarqrqaaQDELDRLKKKAEEARKQKDDADKE---AEKQILMAQQAAQKCSAAEQQ 2097
Cdd:PRK04863 433 P-------------------------------DLTADNAEDWLEEFQAKEQEATEEllsLEQKLSVAQAAHSQFEQAYQL 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2098 VQSVLAQqkedtimqTKLKEEYEKAKKLAKQAEAAKEKAEREAALlRQQAEEAERQkaaaeqeaanqAKAQEDAERLRKE 2177
Cdd:PRK04863 482 VRKIAGE--------VSRSEAWDVARELLRRLREQRHLAEQLQQL-RMRLSELEQR-----------LRQQQRAERLLAE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2178 AEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSV---LDEELQRLKDEVDD 2254
Cdd:PRK04863 542 FCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2255 AVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLiKKDKDNTQKFLAKEADNMKKLAED--AARLS-----VEAQEAA 2327
Cdd:PRK04863 622 EFEDSQDVTEYMQQLLERERELTVERDELAARKQAL-DEEIERLSQPGGSEDPRLNALAERfgGVLLSeiyddVSLEDAP 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2328 -------RLRQ-IAEDDLNQ-QRALA------------------------DKMLKEKMQAIQEA------SRLRAE---- 2364
Cdd:PRK04863 701 yfsalygPARHaIVVPDLSDaAEQLAgledcpedlyliegdpdsfddsvfSVEELEKAVVVKIAdrqwrySRFPEVplfg 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2365 -------AEMLQRQKDLAQEQAQKLLEDKQLMQqRLDEETEEY-------------QKSLEAERKRQLEIIAESEKLKLQ 2424
Cdd:PRK04863 781 raarekrIEQLRAEREELAERYATLSFDVQKLQ-RLHQAFSRFigshlavafeadpEAELRQLNRRRVELERALADHESQ 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2425 VSQLSEAQAKAQEEAKKFKKQADSIAsrLHETELATQEKMTVVEKLEVArltsSKEADDLR---KAIADLEKEKSRLKKE 2501
Cdd:PRK04863 860 EQQQRSQLEQAKEGLSALNRLLPRLN--LLADETLADRVEEIREQLDEA----EEAKRFVQqhgNALAQLEPIVSVLQSD 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2502 AEDLQNKSKEMADAQQKQieheKTVLQQTF-LSE-------------KEMLLKKEKLIEEEKKRLEsQFEEEVKKAKalk 2567
Cdd:PRK04863 934 PEQFEQLKQDYQQAQQTQ----RDAKQQAFaLTEvvqrrahfsyedaAEMLAKNSDLNEKLRQRLE-QAEQERTRAR--- 1005
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2568 dEQERQKQQMEDEKKKLQATMDAALN-KQ---KEAEKEMHN---------------KQKEMKE-----------LERKRL 2617
Cdd:PRK04863 1006 -EQLRQAQAQLAQYNQVLASLKSSYDaKRqmlQELKQELQDlgvpadsgaeeraraRRDELHArlsanrsrrnqLEKQLT 1084
|
890 900
....*....|....*....|....*.
gi 1927222982 2618 EQERILAEENQKLR---EKLQQLEEA 2640
Cdd:PRK04863 1085 FCEAEMDNLTKKLRkleRDYHEMREQ 1110
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
197-299 |
1.14e-07 |
|
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: 53.15 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 197 TAKEKLLLWSQRMTdgyQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTN-LENLEQAFGVAERDLGVTRLLD 275
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQpVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 1927222982 276 PEDVDVPHPDEKSIITYVSSLYDA 299
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1872-2228 |
1.16e-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: 58.21 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1872 QRAEAERILKEKLAAIsDATRLKTEAEialkEKEAENERLRRQAEDEAYQRKALEDQANQHKQQieekivllkksSEAEM 1951
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAEQ-----------ERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1952 ERQRAIVDDTLKQRRVVEEEIRILKLNFEKAssgkldlelELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREA 2031
Cdd:pfam17380 345 ERERELERIRQEERKRELERIRQEEIAMEIS---------RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2032 EEKVKKIAAAEEEAARQRQaaqDELDRLKKkaEEARKQKDDADKEAEKQilmaqqaaqkcsaaeQQVQsVLAQQKEDtim 2111
Cdd:pfam17380 416 QQQKVEMEQIRAEQEEARQ---REVRRLEE--ERAREMERVRLEEQERQ---------------QQVE-RLRQQEEE--- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2112 QTKLKEEYEKAKKLAKQAEAAKEKA-EREAALLRQQAEEAERQKAAAEQEAANQAKA-------QEDAERLRKEAEFEAA 2183
Cdd:pfam17380 472 RKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEERQKAiyeeerrREAEEERRKQQEMEER 551
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2184 KRAQAENAALKQKQQADAEMAKHKKLAEQTL-----KQKFQVEQELTKVK 2228
Cdd:pfam17380 552 RRIQEQMRKATEERSRLEAMEREREMMRQIVesekaRAEYEATTPITTIK 601
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1409-1564 |
1.65e-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: 55.32 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1409 MMQAELDKQKQLAEVHAKaIAKAEKEAQELKLR---MQEEVNRREDAVVDAEKQKHNIQLELHELKNLSEQqiMDKSKQV 1485
Cdd:COG1579 1 AMPEDLRALLDLQELDSE-LDRLEHRLKELPAElaeLEDELAALEARLEAAKTELEDLEKEIKRLELEIEE--VEARIKK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222982 1486 DDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKR 1564
Cdd:COG1579 78 YEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2177-2491 |
1.73e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 58.00 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2177 EAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTL---KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVD 2253
Cdd:PRK11281 32 NGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2254 DAVKQR------GQVEEELLKVKVQMEELLKlklRIEEENQRLI--KKDKDNTQKFLakeADNMKKLAEDAARLSVEAQE 2325
Cdd:PRK11281 112 EETRETlstlslRQLESRLAQTLDQLQNAQN---DLAEYNSQLVslQTQPERAQAAL---YANSQRLQQIRNLLKGGKVG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2326 AARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRaeaEMLQRQKDLAQEQAQKLLEDKQLMQ-----QRLD--EET- 2397
Cdd:PRK11281 186 GKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQ---DLLQKQRDYLTARIQRLEHQLQLLQeainsKRLTlsEKTv 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2398 EEYQKSLEAERKRQLEIIAESEKLKLQVSQ-LSEAQAKAQE---EAKKFKKQADsiasRLHETELATQEKMTVVE-KLEV 2472
Cdd:PRK11281 263 QEAQSQDEAARIQANPLVAQELEINLQLSQrLLKATEKLNTltqQNLRVKNWLD----RLTQSERNIKEQISVLKgSLLL 338
|
330 340
....*....|....*....|....*..
gi 1927222982 2473 AR--------LTSSKEADDLRKAIADL 2491
Cdd:PRK11281 339 SRilyqqqqaLPSADLIEGLADRIADL 365
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4068-4104 |
1.92e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 49.79 E-value: 1.92e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1927222982 4068 IRLLEAQIATGGIIDPEESHRVPVEVAYKRGFFDEEM 4104
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1534-2153 |
2.02e-07 |
|
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: 57.35 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1534 RKAAQEEAEKLRKQVNEETQKKRMAEEElkrkaeaekeaakqKQKALEDLENLKRQAEEAERQVKQAEIEkERQiqvahv 1613
Cdd:pfam05701 37 RKLVELELEKVQEEIPEYKKQSEAAEAA--------------KAQVLEELESTKRLIEELKLNLERAQTE-EAQ------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1614 AAQKSAAAELQSKHMsfvektsklEESLKQEHGAVLQLQHEAAalKKQQEDAERAREEAEKELEKWRQKANEALRLRLQA 1693
Cdd:pfam05701 96 AKQDSELAKLRVEEM---------EQGIADEASVAAKAQLEVA--KARHAAAVAELKSVKEELESLRKEYASLVSERDIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1694 EEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAEnelERQRKVAESTAQQKLTAEQELirlradfdnaEQq 1773
Cdd:pfam05701 165 IKRAEEAVSASKEIEKTVEELTIELIATKESLESAHAAHLEAE---EHRIGAALAREQDKLNWEKEL----------KQ- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1774 rslLEDELYRLKNEVVAAQQQRKQLE---DELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEask 1850
Cdd:pfam05701 231 ---AEEELQRLNQQLLSAKDLKSKLEtasALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAALASAKKELEE--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1851 LRAIAEEAKHQRQVAEEEAARQRAEAERiLKEKLAAISdatRLKTEAEIALKEKEAENERLRrqAEDEAYQRKALEDQan 1930
Cdd:pfam05701 305 VKANIEKAKDEVNCLRVAAASLRSELEK-EKAELASLR---QREGMASIAVSSLEAELNRTK--SEIALVQAKEKEAR-- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1931 qhkqqiEEKIVLLKKSSEAEMErqraiVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELnklkniaeetqQSKLRA 2010
Cdd:pfam05701 377 ------EKMVELPKQLQQAAQE-----AEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRL-----------EAVLKE 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2011 EEEAEKLRKLALEEEKRRREAEEKVKKiaAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQK 2090
Cdd:pfam05701 435 IEAAKASEKLALAAIKALQESESSAES--TNQEDSPRGVTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELR 512
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927222982 2091 CSAAEQQVQSVLAQQKEDtimqtkLKEEYEKAKKlakqAEAAKEKAEREaalLRQQAEEAERQ 2153
Cdd:pfam05701 513 SLEKLEEVNREMEERKEA------LKIALEKAEK----AKEGKLAAEQE---LRKWRAEHEQR 562
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1527-1740 |
2.48e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.35 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1527 AAEAEKLRK--AAQEEAEKLRKQVNEETQKKRMAEEELKRKAEaekeaakqkqkaledlenlKRQAEEAER----QVKQA 1600
Cdd:PRK09510 74 AKRAEEQRKkkEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ-------------------KKQAEEAAKqaalKQKQA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1601 EIEKERQIQVAHVAA--QKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEdaerareeaekelek 1678
Cdd:PRK09510 135 EEAAAKAAAAAKAKAeaEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA--------------- 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222982 1679 wRQKANEALRLRlqAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELE 1740
Cdd:PRK09510 200 -KKKAEAEAKKK--AAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
192-299 |
2.58e-07 |
|
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: 52.02 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 192 QSEDMTAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLV-DMGRVYRQTNLENLEQAFGVAERDLGV 270
Cdd:cd21313 3 DAKKQTPKQRLLGWIQ---NKIPYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1927222982 271 TRLLDPEDVDVPHPDEKSIITYVSSLYDA 299
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1189-1974 |
2.62e-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: 57.44 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1189 PVFDSLEAELKKATAVSDKMSRVHSERdaELDHYRQLLSSLQDRWKavfsqidlRQRELEQlgRQLGYYRESYDWLIRWI 1268
Cdd:pfam15921 52 PIFPKYEVELDSPRKIIAYPGKEHIER--VLEEYSHQVKDLQRRLN--------ESNELHE--KQKFYLRQSVIDLQTKL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1269 NDAKQRQEKIQAVTITDSKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDyelQLVAYKAQVEPLASPLkkT 1348
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRK---MMLSHEGVLQEIRSIL--V 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1349 KLDSASDNIIQEYVTLRT-KYSELMTLTSQYIKF----ITDSQRRLEDEEKAAEKLKAEEQKKMAMM-QAELDKQKQLAE 1422
Cdd:pfam15921 195 DFEEASGKKIYEHDSMSTmHFRSLGSAISKILREldteISYLKGRIFPVEDQLEALKSESQNKIELLlQQHQDRIEQLIS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1423 VHakaiakaekeaqelklrmqeEVnrredavvdaekqkhniqlelhELKNLSEQQIMDKSKQvdDALQSRVKIEEEirLI 1502
Cdd:pfam15921 275 EH--------------------EV----------------------EITGLTEKASSARSQA--NSIQSQLEIIQE--QA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1503 RLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKL--------------RKQVNEET-----QKKRMAEEELK 1563
Cdd:pfam15921 309 RNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvlanseltearteRDQFSQESgnlddQLQKLLADLHK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1564 RKAEAEKEAAKQKQKALEDLEN------LKRQAEEAERQVKQAEI-----------EKERQI-----------QVAHVAA 1615
Cdd:pfam15921 389 REKELSLEKEQNKRLWDRDTGNsitidhLRRELDDRNMEVQRLEAllkamksecqgQMERQMaaiqgknesleKVSSLTA 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1616 QKSAAAELQSKHM-SFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLR-LQA 1693
Cdd:pfam15921 469 QLESTKEMLRKVVeELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnVQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1694 EEEAHKKSLAQEDA-----EKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFD 1768
Cdd:pfam15921 549 ECEALKLQMAEKDKvieilRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVS 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1769 NAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQ--------LKSKAEKETMSNSERSKQL----LEV 1836
Cdd:pfam15921 629 DLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEdyevlkrnFRNKSEEMETTTNKLKMQLksaqSEL 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1837 EATKMRDLAEEASKLRAIAEEAKHQRQVAeeeAARQRAEAeriLKEKLAAISDA-TRLKTEAEIALKEKEAENERLRRQA 1915
Cdd:pfam15921 709 EQTRNTLKSMEGSDGHAMKVAMGMQKQIT---AKRGQIDA---LQSKIQFLEEAmTNANKEKHFLKEEKNKLSQELSTVA 782
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222982 1916 EDE---AYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIvddtlkqRRVVEEEIRI 1974
Cdd:pfam15921 783 TEKnkmAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDII-------QRQEQESVRL 837
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1436-2005 |
2.76e-07 |
|
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: 56.96 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1436 QELKlRMQEEVNRREDAVVDAEKQKHNIQLELHELKNLSEQQIMDKSKQVDDALQSRVKIE-EEIRLIRLQLETTVKQKS 1514
Cdd:pfam05701 42 LELE-KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSElAKLRVEEMEQGIADEASV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1515 TAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAekeaakqkqkaledlenlkrqAEEAE 1594
Cdd:pfam05701 121 AAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSA---------------------SKEIE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1595 RQVKQAEIE----KE--RQIQVAHVAA--QKSAAAelqskhMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAe 1666
Cdd:pfam05701 180 KTVEELTIEliatKEslESAHAAHLEAeeHRIGAA------LAREQDKLNWEKELKQAEEELQRLNQQLLSAKDLKSKL- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1667 rareeaekelekwrqKANEALRLRLQAEEEAHKKSlaqedaeKQKEEAEREAKKRaKAEDSALKQKEMAENELERQRKVA 1746
Cdd:pfam05701 253 ---------------ETASALLLDLKAELAAYMES-------KLKEEADGEGNEK-KTSTSIQAALASAKKELEEVKANI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1747 EstaqqKLTAEQELIRLRAdfdnaeqqrSLLEDELYRLKNEVVAAQQQR-------KQLEDELAKVRSEMdVLIQLKSKA 1819
Cdd:pfam05701 310 E-----KAKDEVNCLRVAA---------ASLRSELEKEKAELASLRQREgmasiavSSLEAELNRTKSEI-ALVQAKEKE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1820 EKETMsnSERSKQLLEV--EATKMRDLA----EEASKLRAIAEEAKHQRQVAEE--EAARQRAEAERIlKEKLAAISDAT 1891
Cdd:pfam05701 375 AREKM--VELPKQLQQAaqEAEEAKSLAqaarEELRKAKEEAEQAKAAASTVESrlEAVLKEIEAAKA-SEKLALAAIKA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1892 RLKTEAEIALKEKEA----------ENERLRRQAEDEayqrkalEDQANqhkQQIEEKIVLLKKSSEAEMeRQRAIVDDT 1961
Cdd:pfam05701 452 LQESESSAESTNQEDsprgvtlsleEYYELSKRAHEA-------EELAN---KRVAEAVSQIEEAKESEL-RSLEKLEEV 520
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1927222982 1962 LKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKniAEETQQ 2005
Cdd:pfam05701 521 NREMEERKEALKIALEKAEKAKEGKLAAEQELRKWR--AEHEQR 562
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2279-2600 |
2.79e-07 |
|
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: 57.54 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2279 LKLRIEEENQRLIKKDKDNTQKfLAKEADNMKKLAEdaarlsvEAQEAARLRQIAEDDLNQQRALADKmlkekmqAIQEA 2358
Cdd:NF012221 1505 LKLTAKAGSNRLEFKGTGHNDG-LGYILDNVVATSE-------SSQQADAVSKHAKQDDAAQNALADK-------ERAEA 1569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2359 SRLRAEAEMLQRQKDLAQEQAQklLEDKQlmQQRLDEETEEYQKSLEAERKrqlEIIAESEKLKLQVSQLSEAQAKAQEE 2438
Cdd:NF012221 1570 DRQRLEQEKQQQLAAISGSQSQ--LESTD--QNALETNGQAQRDAILEESR---AVTKELTTLAQGLDALDSQATYAGES 1642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2439 AKKFKKQ-ADSIASRLHETELATqeKMTVVEKLEVARLTSSKEADDLRKAIAdleKEKSRLKKEAEDLQNKSKEMADAQQ 2517
Cdd:NF012221 1643 GDQWRNPfAGGLLDRVQEQLDDA--KKISGKQLADAKQRHVDNQQKVKDAVA---KSEAGVAQGEQNQANAEQDIDDAKA 1717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2518 KQIEHEKTVLQQtflsekemllkkeklieeekkRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKE 2597
Cdd:NF012221 1718 DAEKRKDDALAK---------------------QNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDE 1776
|
...
gi 1927222982 2598 AEK 2600
Cdd:NF012221 1777 SDK 1779
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2240-2490 |
2.85e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2240 VLDEelQRLKDEVDDAVKQRGQ---VEEELLKVKVQMEELLklklRIEEENQRLIKKDKDNTQKflakeadnmkklaeDA 2316
Cdd:COG4913 217 MLEE--PDTFEAADALVEHFDDlerAHEALEDAREQIELLE----PIRELAERYAAARERLAEL--------------EY 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2317 ARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQ----EQAQKLLEDKQLMQQR 2392
Cdd:COG4913 277 LRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgdrlEQLEREIERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2393 LDEETEEYQKSLeaeRKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEV 2472
Cdd:COG4913 357 RERRRARLEALL---AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
250
....*....|....*...
gi 1927222982 2473 ARLTSSKEADDLRKAIAD 2490
Cdd:COG4913 434 RKSNIPARLLALRDALAE 451
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1288-1772 |
3.06e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1288 TLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLASplKKTKLDSASDNIIQEYVTLRTK 1367
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRE--TIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1368 YSELmtltSQYIKFITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVN 1447
Cdd:PRK02224 288 LEEL----EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1448 RREDAVVDAEKQKHNIQLELHELKNLsEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRA 1527
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEEL-EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1528 AEAEKLRKAAQ--------EEAEKLrkqvnEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQ 1599
Cdd:PRK02224 443 EEAEALLEAGKcpecgqpvEGSPHV-----ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1600 AE-IEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQ-------------EDA 1665
Cdd:PRK02224 518 REdLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaelkeriesleriRTL 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1666 ERAREEAEKELEKWRQK------ANEALRLRLQAEEEaHKKSLAQ-------EDAEKQKEEAER-----EAKKRAKAE-- 1725
Cdd:PRK02224 598 LAAIADAEDEIERLREKrealaeLNDERRERLAEKRE-RKRELEAefdeariEEAREDKERAEEyleqvEEKLDELREer 676
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1927222982 1726 DSALKQKEMAENELERQRKVAEstaqqKLTA-EQELIRLRADFDNAEQ 1772
Cdd:PRK02224 677 DDLQAEIGAVENELEELEELRE-----RREAlENRVEALEALYDEAEE 719
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2056-2638 |
3.25e-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: 56.98 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2056 LDRLKKKAEEARKQKddadKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEK 2135
Cdd:TIGR00606 188 LETLRQVRQTQGQKV----QEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2136 -AEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAK-RAQAENAALKQKqqadaEMAKHKKLAEQT 2213
Cdd:TIGR00606 264 iMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTvREKERELVDCQR-----ELEKLNKERRLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2214 LKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEellkvkVQMEELLKLKLRIEEENQRLIKK 2293
Cdd:TIGR00606 339 NQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSE------RQIKNFHTLVIERQEDEAKTAAQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2294 DkdntqkfLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASR-LRAEAEMLQRQK 2372
Cdd:TIGR00606 413 L-------CADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRiLELDQELRKAER 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2373 DLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKlQVSQLSEAQAKAQEEAKKFKKQ-ADSIAS 2451
Cdd:TIGR00606 486 ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRT-QMEMLTKDKMDKDEQIRKIKSRhSDELTS 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2452 RLHETELATQEKMTVVEKLEVARLTSSKEADdLRKAIADLEKEKSRLKKEAE------------------------DLQN 2507
Cdd:TIGR00606 565 LLGYFPNKKQLEDWLHSKSKEINQTRDRLAK-LNKELASLEQNKNHINNELEskeeqlssyedklfdvcgsqdeesDLER 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2508 KSKEMADA-QQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQA 2586
Cdd:TIGR00606 644 LKEEIEKSsKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEK 723
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1927222982 2587 TMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLE 2638
Cdd:TIGR00606 724 RRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG 775
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2067-2504 |
3.36e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 56.69 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2067 RKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQK--EDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLR 2144
Cdd:pfam09731 77 GESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKaqLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2145 QQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRaQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQEL 2224
Cdd:pfam09731 157 QAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKE-VINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2225 TKVKLKLDETDKQKS-------VLDEELQRLKDEVDDAVKQRGQVEEELLKVKVqmeelLKLKLRIEEENQRLIKKDKDn 2297
Cdd:pfam09731 236 EKAQSLAKLVDQYKElvaseriVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLI-----AHAHREIDQLSKKLAELKKR- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2298 tqkflakeadnmkklAEDAARLSVEAQEAarlrqiaeddlnQQRALADKMLKekmqaiqeasrlRAEAEMLQRQKDLAQE 2377
Cdd:pfam09731 310 ---------------EEKHIERALEKQKE------------ELDKLAEELSA------------RLEEVRAADEAQLRLE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2378 QAQKLLEdkqlmqqrldeETEEYQKSLEAERKRQLEIIAE-------SEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIA 2450
Cdd:pfam09731 351 FEREREE-----------IRESYEEKLRTELERQAEAHEEhlkdvlvEQEIELQREFLQDIKEKVEEERAGRLLKLNELL 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222982 2451 SRLHETELATQEKMTVV-EKLEVARLTSSKEA--DDLRKAIAD-----LEKEKSRLKKEAED 2504
Cdd:pfam09731 420 ANLKGLEKATSSHSEVEdENRKAQQLWLAVEAlrSTLEDGSADsrprpLVRELKALKELASD 481
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1966-2210 |
4.21e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.49 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1966 RVVEEEIRILKLNFEKASSGKLDLELelnKLKNIAEETQQSKLRAEEEAEKLRKL------ALEEEKRRREAEEKVKKIA 2039
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARFEA---RQARLEREKAAREARHKKAAEARAAKdkdavaAALARVKAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2040 AAEEEAARQRQAAQDELDRLKKKAEEARKQKDDA--DKEAEKQILMAQQAAQKcsAAEQQVQSVLAQQKEDTIMQTKLKE 2117
Cdd:PRK05035 509 KAGARPDNSAVIAAREARKAQARARQAEKQAAAAadPKKAAVAAAIARAKAKK--AAQQAANAEAEEEVDPKKAAVAAAI 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2118 EYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQ 2197
Cdd:PRK05035 587 ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQAN 666
|
250
....*....|...
gi 1927222982 2198 QADAEMAKHKKLA 2210
Cdd:PRK05035 667 AEPEEAEDPKKAA 679
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1519-1758 |
4.36e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.49 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1519 ELKQLR---DRAAEAEKLRKAAQEEAEKLRKQVNE--ETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEA 1593
Cdd:PRK05035 456 EARQARlerEKAAREARHKKAAEARAAKDKDAVAAalARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQA 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1594 ERQVKQAEIEKERQIQ--VAHVAAQKSAAAElqskhmsfveKTSKLEESLKQEHGAVLQLQHEAAAlKKQQEDAERAREE 1671
Cdd:PRK05035 536 EKQAAAAADPKKAAVAaaIARAKAKKAAQQA----------ANAEAEEEVDPKKAAVAAAIARAKA-KKAAQQAASAEPE 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1672 AEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRK----VAE 1747
Cdd:PRK05035 605 EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKaavaAAI 684
|
250
....*....|.
gi 1927222982 1748 STAQQKLTAEQ 1758
Cdd:PRK05035 685 ARAKAKKAAQQ 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1420-1661 |
4.54e-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: 55.54 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1420 LAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELknlsEQQIMDKSKQVDdalqsrvKIEEEI 1499
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIR-------ALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1500 RLIRLQLETTVKQKSTAESELKQLRDRAAE-AEKLRKAAQEEAEKLRKQVNEETQKKRMAeEELKRKAEAEKEAAKQKQK 1578
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLDAVRRL-QYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1579 ALEDLENLKRQAEEAERQVKQ--AEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAA 1656
Cdd:COG4942 158 DLAELAALRAELEAERAELEAllAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....*
gi 1927222982 1657 ALKKQ 1661
Cdd:COG4942 238 AAAER 242
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3955-3991 |
4.83e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.63 E-value: 4.83e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1927222982 3955 RYLEGTSCIAGVFLETSKERLSIYQAMKKNMIRPGTA 3991
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2479-2651 |
5.73e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2479 KEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEE 2558
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2559 EVKKAKALKdEQERQKQQMEDEKKKLQATMDAALNK-QKEAEKEMHNKQKEMKELERKRLEQERILA---EENQKLREKL 2634
Cdd:COG4717 151 LEERLEELR-ELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEeaqEELEELEEEL 229
|
170
....*....|....*..
gi 1927222982 2635 QQLEEAQKDQPDKEVIH 2651
Cdd:COG4717 230 EQLENELEAAALEERLK 246
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3756-3790 |
6.17e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.63 E-value: 6.17e-07
10 20 30
....*....|....*....|....*....|....*
gi 1927222982 3756 LLEAQAATGFIVDPVKNETLTVDEAVRKGIVGPEI 3790
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4171-4199 |
6.36e-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: 6.36e-07
10 20
....*....|....*....|....*....
gi 1927222982 4171 IVDPETGKEMTVYEAYRKGLIDHQTYLEL 4199
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2167-2412 |
8.59e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 8.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2167 AQEDAERLRKEAEfEAAKRAQAENAALKQKQQAdaemakhkklAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQ 2246
Cdd:COG4942 18 QADAAAEAEAELE-QLQQEIAELEKELAALKKE----------EKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2247 RLKDEVDDAVKQRGQVEEEL---LKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEA 2323
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELaelLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2324 QEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKS 2403
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
....*....
gi 1927222982 2404 LEAERKRQL 2412
Cdd:COG4942 247 GFAALKGKL 255
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1676-1960 |
8.75e-07 |
|
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: 55.42 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1676 LEKWRQKANEALRLRLQAEEEAHKKSL--AQEDAEKQKEEAEREAKKRAKAEDSAL--KQKEMAENELERQRKVAESTAQ 1751
Cdd:pfam05667 245 RTKLLKRIAEQLRSAALAGTEATSGASrsAQDLAELLSSFSGSSTTDTGLTKGSRFthTEKLQFTNEAPAATSSPPTKVE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1752 Q----KLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVvaaqqqrKQLEDELAKVRSEMDVLIQLKSKAEK------ 1821
Cdd:pfam05667 325 TeeelQQQREEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNEELEKQYKVKKKtldllp 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1822 ETMSNSERSKQLLEVEATKMRDLAEEASKLRA--IAEEAKHQRQVAEEEAARQRAEAE-RILKEKLAAISDATRLKTEAe 1898
Cdd:pfam05667 398 DAEENIAKLQALVDASAQRLVELAGQWEKHRVplIEEYRALKEAKSNKEDESQRKLEEiKELREKIKEVAEEAKQKEEL- 476
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1899 iaLKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIE-EKIVLLKKSSEAEM-------ERQRAIVDD 1960
Cdd:pfam05667 477 --YKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEiTKILSDTKSLQKEInsltgklDRTFTVTDE 544
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1684-1960 |
9.86e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 54.69 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1684 NEALRLRLQA------EEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAEN--------ELERQRKVAE-- 1747
Cdd:pfam19220 5 NELLRVRLGEmadrleDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYgklrrelaGLTRRLSAAEge 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1748 -STAQQKLTAEQELIRlRADFDNAEQQRSLLEDE--LYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETM 1824
Cdd:pfam19220 85 lEELVARLAKLEAALR-EAEAAKEELRIELRDKTaqAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1825 SNSERSkQLLEVEATKMRDLAEEAS----------------------KLRAI-----AEEAKHQRQVAEEEAARQRAEAE 1877
Cdd:pfam19220 164 TARERL-ALLEQENRRLQALSEEQAaelaeltrrlaeletqldatraRLRALegqlaAEQAERERAEAQLEEAVEAHRAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1878 RI-LKEKLAAISD----ATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKksseaEME 1952
Cdd:pfam19220 243 RAsLRMKLEALTAraaaTEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQ-----EMQ 317
|
....*...
gi 1927222982 1953 RQRAIVDD 1960
Cdd:pfam19220 318 RARAELEE 325
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1515-1751 |
1.01e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1515 TAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAeaekeaakqkqkalEDLENLKRQAEEAE 1594
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ--------------AEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1595 RQVKQAEIEKERQIQVAHVAAQKSAAAE--LQSKHMS-FVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREE 1671
Cdd:COG3883 79 AEIEERREELGERARALYRSGGSVSYLDvlLGSESFSdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1672 AEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQ 1751
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1951-2303 |
1.06e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.13 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1951 MERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEE---AEKLRKLALEEEKR 2027
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQErmaMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2028 RREAEEKVKKiaaaeeEAARQRQAAQDELDRLKKKaeeaRKQKDdadkEAEKQILmaqQAAQKCSAAEQQVQSVLAQQKE 2107
Cdd:pfam17380 358 RKRELERIRQ------EEIAMEISRMRELERLQME----RQQKN----ERVRQEL---EAARKVKILEEERQRKIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2108 DTIMQTKLKEEyekakklAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEaanqakaQEDAERLRKEAEFEAAKRAQ 2187
Cdd:pfam17380 421 EMEQIRAEQEE-------ARQREVRRLEEERAREMERVRLEEQERQQQVERLR-------QQEEERKRKKLELEKEKRDR 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2188 AENAALKQKQQADAEMAKHKKLAEQTLKQKFqVEQELtkvklkldeTDKQKSVLDEELQRLKDE---VDDAVKQRGQVEE 2264
Cdd:pfam17380 487 KRAEEQRRKILEKELEERKQAMIEEERKRKL-LEKEM---------EERQKAIYEEERRREAEEerrKQQEMEERRRIQE 556
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1927222982 2265 ELLKVKvqmEELLKLK-LRIEEENQRLIKKDKDNTQKFLA 2303
Cdd:pfam17380 557 QMRKAT---EERSRLEaMEREREMMRQIVESEKARAEYEA 593
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2364-2644 |
1.13e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.15 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2364 EAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEyqksLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFK 2443
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEE----EEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2444 KQADSIASRLHETELA-TQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEH 2522
Cdd:pfam13868 101 EQMDEIVERIQEEDQAeAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2523 EKTVLQQTFLSEKEMLLKKEKLIEEEKKRLEsqfeEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEM 2602
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDELRAKLY----QEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEA 256
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1927222982 2603 HNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQ 2644
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2262-2621 |
1.26e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.77 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2262 VEEELLKVKVQMEELLKLKLRIEEENQRLIKKDkdntQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQR 2341
Cdd:pfam13868 1 LRENSDELRELNSKLLAAKCNKERDAQIAEKKR----IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2342 ALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQK-SLEAERKRQLEIIAESEK 2420
Cdd:pfam13868 77 ELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEeQAEWKELEKEEEREEDER 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2421 LKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEksrlkk 2500
Cdd:pfam13868 157 ILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKK------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2501 eaedlQNKSKEMADAQQKQIEHEKTVLQQtflsEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDE 2580
Cdd:pfam13868 231 -----ARQRQELQQAREEQIELKERRLAE----EAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1927222982 2581 KKKLQAtmdaalnKQKEAEKEMHNKQKEMKELERKRLEQER 2621
Cdd:pfam13868 302 REEQRA-------AEREEELEEGERLREEEAERRERIEEER 335
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2552-2710 |
1.31e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 54.83 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2552 LESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQ--------KEAEKEMHNKQKEMKELERKRLEQ--ER 2621
Cdd:PRK00409 528 LERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqqaiKEAKKEADEIIKELRQLQKGGYASvkAH 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2622 ILAEENQKLREKLQQLEEAQKDQPdkevihvtmvETTKNVYNGQNV--------GDVVDSAEKKPDPLAFNGIREKVPAS 2693
Cdd:PRK00409 608 ELIEARKRLNKANEKKEKKKKKQK----------EKQEELKVGDEVkylslgqkGEVLSIPDDKEAIVQAGIMKMKVPLS 677
|
170
....*....|....*..
gi 1927222982 2694 RLHDLGLLPKKDFDKLK 2710
Cdd:PRK00409 678 DLEKIQKPKKKKKKKPK 694
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1596-1976 |
1.41e-06 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 54.76 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1596 QVKQAEIEKERQIQVAHVAAQKSAAAELQSKHmsfveKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKE 1675
Cdd:pfam09731 98 SSEVAEEEKEATKDAAEAKAQLPKSEQEKEKA-----LEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDT 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1676 LEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQR------KVAEST 1749
Cdd:pfam09731 173 AEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSlaklvdQYKELV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1750 AQQKLTAEQELIRLRAD-FDNAEQQRSLLEDELYRLkneVVAAQQQRKQLEDELA--KVRSEMDVLIQLKSKAEKETMSN 1826
Cdd:pfam09731 253 ASERIVFQQELVSIFPDiIPVLKEDNLLSNDDLNSL---IAHAHREIDQLSKKLAelKKREEKHIERALEKQKEELDKLA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1827 SERSKQLLEVEATKMRDLAEEASklRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLaaISDATRLKTEAEIALKEKEA 1906
Cdd:pfam09731 330 EELSARLEEVRAADEAQLRLEFE--REREEIRESYEEKLRTELERQAEAHEEHLKDVL--VEQEIELQREFLQDIKEKVE 405
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222982 1907 ENERLRRQAEDEAYQR-KALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILK 1976
Cdd:pfam09731 406 EERAGRLLKLNELLANlKGLEKATSSHSEVEDENRKAQQLWLAVEALRSTLEDGSADSRPRPLVRELKALK 476
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2245-2643 |
1.55e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2245 LQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKdKDNTQKFLAKEADNMKKLAEDAARLSVEAQ 2324
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2325 EAARLRQIAEddLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLmqqrldeeteeyqksl 2404
Cdd:COG4717 127 LLPLYQELEA--LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL---------------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2405 eAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQ-EKMTVVEKLEVARLTSSKEADD 2483
Cdd:COG4717 189 -ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2484 LRKAIADLEK-----------EKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVlqQTFLSEKEMLLKKEKLIEEEKKRL 2552
Cdd:COG4717 268 LLSLILTIAGvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEEL--EELLAALGLPPDLSPEELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2553 ESQFEEEVKKAKALkdEQERQKQQMEDEKKKL----QATMDAALNKQKEAEKEMHNKQKEMKELER-----KRLEQERIL 2623
Cdd:COG4717 346 IEELQELLREAEEL--EEELQLEELEQEIAALlaeaGVEDEEELRAALEQAEEYQELKEELEELEEqleelLGELEELLE 423
|
410 420
....*....|....*....|
gi 1927222982 2624 AEENQKLREKLQQLEEAQKD 2643
Cdd:COG4717 424 ALDEEELEEELEELEEELEE 443
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1390-1736 |
1.56e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.10 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1390 EDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEvhakAIAKAEKEAQelkLRMQEEVNRREDAVVDAEKQKHNIQLElHE 1469
Cdd:pfam02029 34 ESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLD----RTAKREERRQ---KRLQEALERQKEFDPTIADEKESVAER-KE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1470 LKNLSEQQIMDKSKQVDDaLQSRVKIEEeirlirlqleTTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQV- 1548
Cdd:pfam02029 106 NNEEEENSSWEKEEKRDS-RLGRYKEEE----------TEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENf 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1549 NEETQKKRMAEEELKRKAeaekeaakqkqkalEDLENLKRQAEEAERQVKQAEIE-KERQIQVAHVAAQKSAAAELQSKH 1627
Cdd:pfam02029 175 AKEEVKDEKIKKEKKVKY--------------ESKVFLDQKRGHPEVKSQNGEEEvTKLKVTTKRRQGGLSQSQEREEEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1628 MSFVEKTSKLEEsLKQEHGAvlqLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLaQEDA 1707
Cdd:pfam02029 241 EVFLEAEQKLEE-LRRRRQE---KESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAERKLRE-EEEK 315
|
330 340
....*....|....*....|....*....
gi 1927222982 1708 EKQKEEAEReakKRAKAedsALKQKEMAE 1736
Cdd:pfam02029 316 RRMKEEIER---RRAEA---AEKRQKLPE 338
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1581-1920 |
1.78e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.57 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1581 EDLENLKRQAEEAERQVKQAE-IEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTskLEESLKQEHGAVLQLQhEAAALK 1659
Cdd:COG3096 836 AELAALRQRRSELERELAQHRaQEQQLRQQLDQLKEQLQLLNKLLPQANLLADET--LADRLEELREELDAAQ-EAQAFI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1660 KQQEDAERAREEAEKELEKWRQKaNEALRLRLQAEEEAHKKSLAQEDAEKQ----------KEEAEREAKKRAKAEdsAL 1729
Cdd:COG3096 913 QQHGKALAQLEPLVAVLQSDPEQ-FEQLQADYLQAKEQQRRLKQQIFALSEvvqrrphfsyEDAVGLLGENSDLNE--KL 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1730 KQK-EMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELY-------------------RLKNEVV 1789
Cdd:COG3096 990 RARlEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEelgvqadaeaeerarirrdELHEELS 1069
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1790 AAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETmsnserskqlleveaTKMRDLAEEASK----LRAIAEEAKHQRQVA 1865
Cdd:COG3096 1070 QNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDY---------------KQEREQVVQAKAgwcaVLRLARDNDVERRLH 1134
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 1866 EEEAARQRAeaerilkEKLAAISDatrlktEAEIALKEKEAENERLR---RQAEDEAY 1920
Cdd:COG3096 1135 RRELAYLSA-------DELRSMSD------KALGALRLAVADNEHLRdalRLSEDPRR 1179
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2302-2665 |
1.82e-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: 54.34 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2302 LAKEADNMKKLaedaaRLSVEAQeaarLRQiAEDDLNQQRALADKMLK--EKMQAIQEASRLRAEaEMLQRQKDLAQEQ- 2378
Cdd:pfam05483 83 LYKEAEKIKKW-----KVSIEAE----LKQ-KENKLQENRKIIEAQRKaiQELQFENEKVSLKLE-EEIQENKDLIKENn 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2379 -AQKLLEDKQLMQQRLDEETEEYQKSLEAERK----------------RQLEIIAESEKLKLQVsQLSEAQAKAQEEAKK 2441
Cdd:pfam05483 152 aTRHLCNLLKETCARSAEKTKKYEYEREETRQvymdlnnniekmilafEELRVQAENARLEMHF-KLKEDHEKIQHLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2442 FKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKA-------IADLEKEKSRLKKEAEDLQnKSKEMAD 2514
Cdd:pfam05483 231 YKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKtklqdenLKELIEKKDHLTKELEDIK-MSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2515 AQQKQIEHE-----KTVLQQTflSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMD 2589
Cdd:pfam05483 310 STQKALEEDlqiatKTICQLT--EEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQ 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2590 AALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQ--KLREKLQQLEEA--------QKDQPDKEvIHVTMVETTK 2659
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQElifllqarEKEIHDLE-IQLTAIKTSE 466
|
....*.
gi 1927222982 2660 NVYNGQ 2665
Cdd:pfam05483 467 EHYLKE 472
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1765-2216 |
2.25e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 53.76 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1765 ADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKE---TMSNSERSKQLLEveatKM 1841
Cdd:COG5278 79 EPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEaalALVRSGEGKALMD----EI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1842 RDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQ 1921
Cdd:COG5278 155 RARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALEL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1922 RKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAE 2001
Cdd:COG5278 235 LAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2002 ETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQI 2081
Cdd:COG5278 315 AAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2082 LMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEA 2161
Cdd:COG5278 395 IAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAAL 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 2162 ANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQ 2216
Cdd:COG5278 475 AALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAE 529
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1383-1606 |
2.89e-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: 52.84 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1383 TDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELklrmQEEVNRREDAVVDAEKQKHN 1462
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1463 IQLELHELKNLSEQQI--------------MDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAA 1528
Cdd:COG4942 95 LRAELEAQKEELAELLralyrlgrqpplalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 1529 EAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKER 1606
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2356-2648 |
3.52e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2356 QEASRLRAEAEMLQRQKDLAQEQ---AQKLLEDKQLMQQRLDEETEEYQKS----LEAERKRQlEIIAESEKLKLQVSQL 2428
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETrdeADEVLEEHEERREELETLEAEIEDLretiAETERERE-ELAEEVRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2429 SEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNK 2508
Cdd:PRK02224 292 EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2509 SKEMADA------QQKQIEHEKTVLQQTF----------LSEKEMLLKKEKLIEEEKKRLESQFEEE---VKKAKALK-- 2567
Cdd:PRK02224 372 LEEAREAvedrreEIEELEEEIEELRERFgdapvdlgnaEDFLEELREERDELREREAELEATLRTArerVEEAEALLea 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2568 -------------------DEQERQKQQMEDEKKKLQATMDaALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQ 2628
Cdd:PRK02224 452 gkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVE-EVEERLERAEDLVEAEDRIERLEERREDLEELIAERRE 530
|
330 340
....*....|....*....|
gi 1927222982 2629 KLREKLQQLEEAQKDQPDKE 2648
Cdd:PRK02224 531 TIEEKRERAEELRERAAELE 550
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2120-2272 |
3.52e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.95 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2120 EKAKKLAKQAEAAKEKAEREAALLRQQAE-EAERQKAAAEQEAANQAKAQEDAERLRKEAEFEA---AKRAQAENAALKQ 2195
Cdd:COG2268 192 RKIAEIIRDARIAEAEAERETEIAIAQANrEAEEAELEQEREIETARIAEAEAELAKKKAEERReaeTARAEAEAAYEIA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2196 KQQADAEMAKHKKLAEQT------LKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRlkdevdDAVKQRGQVEEELLKV 2269
Cdd:COG2268 272 EANAEREVQRQLEIAEREreielqEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEA------EAIRAKGLAEAEGKRA 345
|
...
gi 1927222982 2270 KVQ 2272
Cdd:COG2268 346 LAE 348
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1635-1959 |
3.54e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1635 SKLEESLkQEHGAVLQLQHeaaALKKQQEDAERAREEAEKELEKWRQkaneALRLRLQAEEEAHKKSLA-QEDAEKQKEE 1713
Cdd:pfam07888 34 NRLEECL-QERAELLQAQE---AANRQREKEKERYKRDREQWERQRR----ELESRVAELKEELRQSREkHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1714 AEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQ 1793
Cdd:pfam07888 106 LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1794 QRKQLEDELAKVRSEMD----VLIQLKSKAEKETMSNSERSKQLLEVEATK--MRDLAEEASKLRAIAEEAKhqRQVAEE 1867
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALLeeLRSLQERLNASERKVEGLG--EELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1868 EAARQRAEAErILKEKLAAISDATRLkTEAEIALKEKEA----ENERLRRQAEDEAYQRKALedqaNQHKQQIEEKIvll 1943
Cdd:pfam07888 264 AAQRDRTQAE-LHQARLQAAQLTLQL-ADASLALREGRArwaqERETLQQSAEADKDRIEKL----SAELQRLEERL--- 334
|
330
....*....|....*.
gi 1927222982 1944 kksSEAEMERQRAIVD 1959
Cdd:pfam07888 335 ---QEERMEREKLEVE 347
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1176-1603 |
3.75e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1176 KLKKMRAEAEGEQPVFDSLEAELKKATAVSDKMSRVHSERDAELDHYRQLLSSLQD--RWKAVFSQIDLRQRELEQLGRQ 1253
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1254 LGYYRESYDWLIRWINDAKQRQEKIQAVTITDSKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDyELQLVA 1333
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE-ELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1334 YKAQVEPLASPLKKTKLDSASDNIIqeyVTLRTKYSELMTLTSQYIKFITDSQ-------RRLEDEEKAAEKLKAEEQKK 1406
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIAAAL---LALLGLGGSLLSLILTIAGVLFLVLgllallfLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1407 MAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAvvDAEKQKHNIQLELHELKNLSEQQIMDKSKQVD 1486
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA--EELEEELQLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1487 DAL---QSRVKIEEEIRLIRLQLE--TTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEE 1561
Cdd:COG4717 389 AALeqaEEYQELKEELEELEEQLEelLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1927222982 1562 lkrkaeaekeaakqkqkalEDLENLKRQAEEAERQVKQAEIE 1603
Cdd:COG4717 469 -------------------GELAELLQELEELKAELRELAEE 491
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1474-1823 |
3.76e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1474 SEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVK----QKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVN 1549
Cdd:pfam07888 39 CLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRelesRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1550 EETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKErQIQVAHVAAQ---KSAAAELQSK 1626
Cdd:pfam07888 119 ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK-QLQAKLQQTEeelRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1627 HMSFVEKTSKLEE------SLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKK 1700
Cdd:pfam07888 198 RNSLAQRDTQVLQlqdtitTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1701 SLAQEDAEKQ--------KEEAEREAKKRAKAEDSALKQKEMAEN---ELERQRKVAESTAQQKLTAEQELIRLRadfDN 1769
Cdd:pfam07888 278 RLQAAQLTLQladaslalREGRARWAQERETLQQSAEADKDRIEKlsaELQRLEERLQEERMEREKLEVELGREK---DC 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1927222982 1770 AEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVrseMDVLIQLKSKAEKET 1823
Cdd:pfam07888 355 NRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL---LEYIRQLEQRLETVA 405
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1437-2128 |
3.94e-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: 53.49 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1437 ELKLRmQEEVNRREDAVVDAEKQKHNIQLELHELKNlSEQQIMDKSKQVDDALQsrvKIEEEIRLIRLQLETTVKQKSTA 1516
Cdd:TIGR04523 48 ELKNK-EKELKNLDKNLNKDEEKINNSNNKIKILEQ-QIKDLNDKLKKNKDKIN---KLNSDLSKINSEIKNDKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1517 ESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQ--AEEAE 1594
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKllKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1595 RQVKQAEIEKERqiqvahvaaqksaaaELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEK 1674
Cdd:TIGR04523 203 LSNLKKKIQKNK---------------SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1675 ELEKwrqkanealrlrLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEmaenELERQrkvaestaqqkl 1754
Cdd:TIGR04523 268 QLSE------------KQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS----ELKNQ------------ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1755 taEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKaEKETMSNSERSKQLL 1834
Cdd:TIGR04523 320 --EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS-YKQEIKNLESQINDL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1835 EveaTKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEaerILKEKlAAISDATRLKTEAEIALKEKEAENERLRRQ 1914
Cdd:TIGR04523 397 E---SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET---IIKNN-SEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1915 AEDEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDdtlkqrrvVEEEIRILKLNFEKASSGKLDLELELN 1994
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD--------LTKKISSLKEKIEKLESEKKEKESKIS 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1995 KLKNIAEETQQSKLRAEEEAEKLRKlaleeekrrreaeekVKKIAAAEEeaarqrqaaqdELDRLKKKAEEarKQKDDAD 2074
Cdd:TIGR04523 542 DLEDELNKDDFELKKENLEKEIDEK---------------NKEIEELKQ-----------TQKSLKKKQEE--KQELIDQ 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222982 2075 KEAEKQILMAQQAA--QKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQ 2128
Cdd:TIGR04523 594 KEKEKKDLIKEIEEkeKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
2321-2657 |
4.21e-06 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 53.41 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2321 VEAQEAARLRQIAEDDLNQQRAladkmlkekmQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLE--DKQLMQQR--LDEE 2396
Cdd:pfam15818 10 LEALEELRMRREAETQYEEQIG----------KIIVETQELKWQKETLQNQKETLAKQHKEAMAvfKKQLQMKMcaLEEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2397 TEEYQKSLEAERKrqlEIIAESEKLK-LQVSQ------LSEAQAKAQ------EEAKK----FKKQADSIASRL------ 2453
Cdd:pfam15818 80 KGKYQLATEIKEK---EIEGLKETLKaLQVSKyslqkkVSEMEQKLQlhllakEDHHKqlneIEKYYATITGQFglvken 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2454 -----HETELATQ--EKMTVVEKLEVARLTSSKEadDLRKAIADLEKEK----SRLKKEAEDLQNKSKEMADAQQ----- 2517
Cdd:pfam15818 157 hgkleQNVQEAIQlnKRLSALNKKQESEICSLKK--ELKKVTSDLIKSKvtcqYKMGEENINLTIKEQKFQELQErlnme 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2518 ----KQIEHEKTVLQ---QTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLqatmda 2590
Cdd:pfam15818 235 lelnKKINEEITHIQeekQDIIISFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKF------ 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2591 aLNKQKEAEKEMHNKQKEMKELERKRLE---QERILAEENQKLREKLQQLEEAQKDQPDKEVIHVTMVET 2657
Cdd:pfam15818 309 -LNLQNEHEKALGTWKKHVEELNGEINEiknELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNVPEVNN 377
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1913-2154 |
4.40e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1913 RQAEDEAYQRKALEDQANQHKQQIEEkivlLKKSSEAEMERQRAivddtLKQRRVVEEEIRIlklnfEKASSGKLDLELE 1992
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEE----LQQKQAAEQERLKQ-----LEKERLAAQEQKK-----QAEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1993 LNKLKNIAEETQQSKLRAEEEAEKLRKLAleeekrrreaeekvKKIAAAEEEAarqrqaaqDELDRLKKKAEEARKQkdd 2072
Cdd:PRK09510 132 KQAEEAAAKAAAAAKAKAEAEAKRAAAAA--------------KKAAAEAKKK--------AEAEAAKKAAAEAKKK--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2073 adKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTimqtklkeeyEKAKKLAKQAEAAKEKAEREAAllRQQAEEAER 2152
Cdd:PRK09510 187 --AEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA----------EAKAAAAKAAAEAKAAAEKAAA--AKAAEKAAA 252
|
..
gi 1927222982 2153 QK 2154
Cdd:PRK09510 253 AK 254
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1729-1962 |
4.48e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1729 LKQKEMAENELERQRKVAESTAQQKLTAEQElirlradfdnAEQQRsLLEDELYRLknevvAAQQQRKQLEDELAKVRSE 1808
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQA----------AEQER-LKQLEKERL-----AAQEQKKQAEEAAKQAALK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1809 mdvliqlKSKAEKETMSNSERSKQLLEVEATKMRDLAEEAsklraiAEEAKHQRQVAEEEAARQRAEAERILKEKLAAIS 1888
Cdd:PRK09510 131 -------QKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKA------AAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAA 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1927222982 1889 DAtrlKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDqanqhKQQIEEKIVLLKKSSEAEMERQRAIVDDTL 1962
Cdd:PRK09510 198 EA---KKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAE-----AKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2354-2615 |
4.50e-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: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2354 AIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLdeeteeyqKSLEAERKRQLEIIAESEK-LKLQVSQLSEAQ 2432
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL--------AALERRIAALARRIRALEQeLAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2433 AKAQEEAKKFKKQADSIASRLhetelATQEKMTVVEKLEVarLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEM 2512
Cdd:COG4942 90 KEIAELRAELEAQKEELAELL-----RALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2513 AdAQQKQIEHEKTVLQQtflsekemllkkeklieeekkrLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAAL 2592
Cdd:COG4942 163 A-ALRAELEAERAELEA----------------------LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
250 260
....*....|....*....|...
gi 1927222982 2593 NKQKEAEKEMHNKQKEMKELERK 2615
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAER 242
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1495-2348 |
4.76e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.42 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1495 IEEEIRLIRLQLEttVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKL-RKQVNEETQKKRMAEEElkrkaeaekeaa 1573
Cdd:COG3096 302 AEEQYRLVEMARE--LEELSARESDLEQDYQAASDHLNLVQTALRQQEKIeRYQEDLEELTERLEEQE------------ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1574 kqkqkalEDLENLKRQAEEAERQVKQAEIEKER--------------------QIQVAhVAAQKSAAAELQSKHMS---F 1630
Cdd:COG3096 368 -------EVVEEAAEQLAEAEARLEAAEEEVDSlksqladyqqaldvqqtraiQYQQA-VQALEKARALCGLPDLTpenA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1631 VEKTSKLEESLKQEHGAVLQLQHE---AAALKKQQEDAERAREEAEKELEKWR--QKANEALR----LRLQAEEEAH-KK 1700
Cdd:COG3096 440 EDYLAAFRAKEQQATEEVLELEQKlsvADAARRQFEKAYELVCKIAGEVERSQawQTARELLRryrsQQALAQRLQQlRA 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1701 SLAQ-EDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSlled 1779
Cdd:COG3096 520 QLAElEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIK---- 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1780 ELYRLKNEVVAAQQQRKQLEDEL-AKVRSEMDVLIQLKSKAEKETMSNSERS-----KQLLE-----------VEATKMR 1842
Cdd:COG3096 596 ELAARAPAWLAAQDALERLREQSgEALADSQEVTAAMQQLLEREREATVERDelaarKQALEsqierlsqpggAEDPRLL 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1843 DLAE-----------------EASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAIS-------DATRLKTEAE 1898
Cdd:COG3096 676 ALAErlggvllseiyddvtleDAPYFSALYGPARHAIVVPDLSAVKEQLAGLEDCPEDLYLIEgdpdsfdDSVFDAEELE 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1899 IALKEKEAENE-RLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVD--DTLKQRRVV------E 1969
Cdd:COG3096 756 DAVVVKLSDRQwRYSRFPEVPLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAfsQFVGGHLAVafapdpE 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1970 EEIRilKLNFEKAssgklDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRReaeekvkkiaaaeeeaarqr 2049
Cdd:COG3096 836 AELA--ALRQRRS-----ELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLAD-------------------- 888
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2050 qaaqdelDRLKKKAEEARKQKDDADKeaekqilmAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAK----KL 2125
Cdd:COG3096 889 -------ETLADRLEELREELDAAQE--------AQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKeqqrRL 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2126 AKQAEAAKEKAEREAALlrqQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEfEAAKRAQAEnaaLKQKQQADAEMAK 2205
Cdd:COG3096 954 KQQIFALSEVVQRRPHF---SYEDAVGLLGENSDLNEKLRARLEQAEEARREAR-EQLRQAQAQ---YSQYNQVLASLKS 1026
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2206 HKKLAEQTLKqkfQVEQELTKVKLKLDETDKQKSvlDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELlklklriee 2285
Cdd:COG3096 1027 SRDAKQQTLQ---ELEQELEELGVQADAEAEERA--RIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSL--------- 1092
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 2286 eNQRLIKKDKDNTQkfLAKEADNMKKLAEDAARLSVEAQEAARL--RQIAEDDLNQQRALADKML 2348
Cdd:COG3096 1093 -QKRLRKAERDYKQ--EREQVVQAKAGWCAVLRLARDNDVERRLhrRELAYLSADELRSMSDKAL 1154
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2168-2444 |
4.76e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.84 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2168 QEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQ---ELTKVKLKLDETDKQKSVLDEE 2244
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDElneKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2245 LQRLKDEVDDAVKQRGQVEeellKVKVQMEELLK----LKLRIEEENQrLIKKDKDntqkfLAKEADNMKKLAEDAARLS 2320
Cdd:COG1340 94 LDELRKELAELNKAGGSID----KLRKEIERLEWrqqtEVLSPEEEKE-LVEKIKE-----LEKELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2321 VEAQEAARLRQIAEDDLNQQRALADKM--LKEKMQAI-QEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLdeet 2397
Cdd:COG1340 164 ELRAELKELRKEAEEIHKKIKELAEEAqeLHEEMIELyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL---- 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1927222982 2398 EEYQKSLEAERKRQLEIIAESEKlklqvsqlSEAQAKAQEEAKKFKK 2444
Cdd:COG1340 240 RELRKELKKLRKKQRALKREKEK--------EELEEKAEEIFEKLKK 278
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1736-1959 |
4.90e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1736 ENELERQRKVAEsTAQQKLTA---EQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVL 1812
Cdd:COG3206 181 EEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1813 iqlkskaeketmSNSERSKQLLEVEATKMRDLAEEASKLRaiaeeAKH-QRQVAEEEAARQRAEAERILKEKLAAI-SDA 1890
Cdd:COG3206 260 ------------LQSPVIQQLRAQLAELEAELAELSARYT-----PNHpDVIALRAQIAALRAQLQQEAQRILASLeAEL 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222982 1891 TRLKTEAEIALKEKEAENERLRRQAEDEAyQRKALEDQANQHKQQIEEkivLLKKSSEAEMERQRAIVD 1959
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEA-ELRRLEREVEVARELYES---LLQRLEEARLAEALTVGN 387
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
70-189 |
4.94e-06 |
|
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: 49.27 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 70 QKKTFTKWVNK---------HLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPrERDVVRSVRLPrekgrmrFHKLQN 140
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTID-ERAINKKKLTP-------FTISEN 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1927222982 141 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQI 189
Cdd:cd21323 97 LNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
986-1605 |
5.06e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 986 DDRMQIEEDYTKSTQHFDSLIRSMEKGLMVVrhkgqqdetlcknyLSEIKDLRLRIEDCEaGTVARIRRpvEKEPLKECV 1065
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEV--------------LREINEISSELPELR-EELEKLEK--EVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1066 QKTTEQKKvqvELEGLKKDLNKVSAKTKEvlaspqqtasapvLRSELDLTVekmdhthmlssvylEKLKTVEMVIRNTQG 1145
Cdd:PRK03918 238 EEIEELEK---ELESLEGSKRKLEEKIRE-------------LEERIEELK--------------KEIEELEEKVKELKE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1146 AEGVLKQYEDClrevhtvpndVKEVETYRTKLKKMRAEAEGEQPVFDSLEAELKKAtavSDKMSRVhSERDAELDHYRQL 1225
Cdd:PRK03918 288 LKEKAEEYIKL----------SEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL---EEKEERL-EELKKKLKELEKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1226 LSSLQDRWKAvFSQIDLRQRELEQLGRQLGYYreSYDWLIRWINDAKQRQEKIQA--VTITDSK-TLKEQLAQEKKLLEE 1302
Cdd:PRK03918 354 LEELEERHEL-YEEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEeiSKITARIgELKKEIKELKKAIEE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1303 VEGNKDKVDECQKyakayiDTIKDYELQLVA-YKAQVEPLASPLKktKLDSASDNIIQEYVTLRTKYSElmtltsqyikf 1381
Cdd:PRK03918 431 LKKAKGKCPVCGR------ELTEEHRKELLEeYTAELKRIEKELK--EIEEKERKLRKELRELEKVLKK----------- 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1382 itdsQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMqEEVNRREDAVVDAEKQKH 1461
Cdd:PRK03918 492 ----ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL-EKLEELKKKLAELEKKLD 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1462 NIQLELHELKNlseqQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEA 1541
Cdd:PRK03918 567 ELEEELAELLK----ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1927222982 1542 EKLRKQVNEetQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKE 1605
Cdd:PRK03918 643 EELRKELEE--LEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1708-2070 |
5.16e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1708 EKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNE 1787
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1788 VVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIaeeakhQRQVAEE 1867
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL------EEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1868 EAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSS 1947
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1948 EAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKR 2027
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1927222982 2028 RREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQK 2070
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
65-185 |
5.26e-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: 48.44 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 65 ERDRVQKKTFTKWVNKHLIKSQrqVTDLYEDLRDGHNLISLLEVLSgetLPRERDVVRSVRLPREKGRMRfhKLQNVQIA 144
Cdd:cd21329 2 EGESSEERTFRNWMNSLGVNPY--VNHLYSDLCDALVIFQLYEMTR---VPVDWGHVNKPPYPALGGNMK--KIENCNYA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1927222982 145 LDFLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 185
Cdd:cd21329 75 VELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
656-748 |
5.43e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.71 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 656 HAFVSAATKELMWLNDKEEEEVNFDWSDRNSNMTAKKDNYSGLMRELELREKKVNDIQATGDKLVRDGHPGKKTVESFTA 735
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1927222982 736 ALQTQWSWILQLC 748
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2205-2522 |
5.46e-06 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 51.49 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2205 KHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIE 2284
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2285 EENQRLIkkdkdNTQKFLAKEadnmkklaEDAARLSVEAQEAARLRQIaEDDLNQQRALADKMLKEKMQaiqeasrLRAE 2364
Cdd:pfam09728 81 KQNKKLK-----EESKKLAKE--------EEEKRKELSEKFQSTLKDI-QDKMEEKSEKNNKLREENEE-------LREK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2365 AEMLQRQKDLAQEQAQKLLEDKQLMQQRLdeETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKK 2444
Cdd:pfam09728 140 LKSLIEQYELRELHFEKLLKTKELEVQLA--EAKLQQATEEEEKKAQEKEVAKARELKAQVQTLSETEKELREQLNLYVE 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 2445 QADSIASRLhetelatqekmtvvEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEH 2522
Cdd:pfam09728 218 KFEEFQDTL--------------NKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEE 281
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2181-2586 |
5.53e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2181 EAAKRAQAENAALKQKQQADAEmakhKKLAEQtlkqkfqvEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRG 2260
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSR----RQLAAE--------QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2261 QVEeellKVKVQMEELLKLKLRIEEenqrlikkdkdntQKFLAKEADNMKKLAEdaARLSVEAQEAARLR-QIAED---- 2335
Cdd:PRK04863 346 QQE----KIERYQADLEELEERLEE-------------QNEVVEEADEQQEENE--ARAEAAEEEVDELKsQLADYqqal 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2336 DLNQQRALAdkmlkekmqaIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETE--EYQKSLEAERKRQLE 2413
Cdd:PRK04863 407 DVQQTRAIQ----------YQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLslEQKLSVAQAAHSQFE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2414 IIAES-EKLKLQVSQlSEAQAKAQE---EAKKFKKQADS---IASRLHETELATQEKMTVVEKLEVARLTSSKEADDlrk 2486
Cdd:PRK04863 477 QAYQLvRKIAGEVSR-SEAWDVAREllrRLREQRHLAEQlqqLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD--- 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2487 aIADLEKEKSRLKKEAEDLqNKSKEMADAQQKQIEHEKTVLQQTFlSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKAL 2566
Cdd:PRK04863 553 -EDELEQLQEELEARLESL-SESVSEARERRMALRQQLEQLQARI-QRLAARAPAWLAAQDALARLREQSGEEFEDSQDV 629
|
410 420 430
....*....|....*....|....*....|....*..
gi 1927222982 2567 -----------------KDEQERQKQQMEDEKKKLQA 2586
Cdd:PRK04863 630 teymqqllerereltveRDELAARKQALDEEIERLSQ 666
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3956-3994 |
5.61e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.78 E-value: 5.61e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1927222982 3956 YLEGTSCIAGVFLETSKERLSIYQAMKKNMIRPGTAFEL 3994
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1475-1789 |
6.04e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1475 EQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQK 1554
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1555 KRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKT 1634
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1635 SKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEAlrlRLQAEEEAHKKSLAQEDAEKQKEEA 1714
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV---ILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 1715 EREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVV 1789
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDV 355
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1902-2218 |
6.29e-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: 51.77 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1902 KEKEAENERLRRQAEDEAyqrKALEDQANQHKQQIEEkivlLKKSSEAEMERQRAivddtLKQRRVVEEEIRilklNFEK 1981
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAA---KKEQERQKKLEQQAEE----AEKQRAAEQARQKE-----LEQRAAAEKAAK----QAEQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1982 ASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLAleeekrrreaeekvkkiaaaeeeaarqrqaAQDELDRLKK 2061
Cdd:TIGR02794 110 AAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAA------------------------------KQAEEEAKAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2062 KAEEARKQKDDADKEAEKQILMAQQAAQKCsaaeqqvqsvlaqqkedtimqtklkeeyeKAKKLAKQAEAAKEKAEREAA 2141
Cdd:TIGR02794 160 AAAEAKKKAEEAKKKAEAEAKAKAEAEAKA-----------------------------KAEEAKAKAEAAKAKAAAEAA 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222982 2142 LLRQQAEEAERQKAaaeqeaanqakAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKF 2218
Cdd:TIGR02794 211 AKAEAEAAAAAAAE-----------AERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQNL 276
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2116-2328 |
6.69e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 52.64 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2116 KEEYEKAKKLAKQAEAAKEKAE--REAALLRQQAEEA-ERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAA 2192
Cdd:PRK05035 464 REKAAREARHKKAAEARAAKDKdaVAAALARVKAKKAaATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAA 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2193 LKQKQQADAEM--AKHKKLAEQTLKQKFQVEQELTKVKL--KLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLK 2268
Cdd:PRK05035 544 DPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDPKKAAVaaAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIAR 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222982 2269 VKVQMEELLKLKLRIEEENQRL-----------IKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAAR 2328
Cdd:PRK05035 624 AKAKKAEQQANAEPEEPVDPRKaavaaaiarakARKAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQ 694
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2356-2524 |
6.79e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.73 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2356 QEASRLRAEaemlQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLE----AERKRQLEIIAESEKLKLQVSQLSEA 2431
Cdd:PRK09510 70 QQKSAKRAE----EQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEqkkqAEEAAKQAALKQKQAEEAAAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2432 QAKAQEEAKKF---KKQADSIASRLHETELA------TQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKS--RLKK 2500
Cdd:PRK09510 146 KAKAEAEAKRAaaaAKKAAAEAKKKAEAEAAkkaaaeAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAaaEAKA 225
|
170 180
....*....|....*....|....
gi 1927222982 2501 EAEDLQNKSKEMADAQQKQIEHEK 2524
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEK 249
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1716-2172 |
6.82e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 52.22 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1716 REAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQR 1795
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1796 KQLEDELAKVRSEmdvliqlkskAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAE 1875
Cdd:COG5278 162 ALALAALLLAAAA----------LLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1876 AERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQR 1955
Cdd:COG5278 232 LELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1956 AIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKV 2035
Cdd:COG5278 312 AAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELE 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2036 KKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKL 2115
Cdd:COG5278 392 VLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAV 471
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222982 2116 KEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAE 2172
Cdd:COG5278 472 AALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASA 528
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1705-2108 |
8.05e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1705 EDAEKQKEEAEREAKKRAKAEDsALKQKEMAENELERQRKVAEStAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRL 1784
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQE-ELEELEEELEELEAELEELRE-ELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1785 KN---EVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEveaTKMRDLAEEASKLRAIAEEAKHQ 1861
Cdd:COG4717 152 EErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ---QRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1862 RQVAEEEAARQrAEAERILKEKLAAISDATRLKTEAE-------------------------IALKEKEAENERLRRQAE 1916
Cdd:COG4717 229 LEQLENELEAA-ALEERLKEARLLLLIAAALLALLGLggsllsliltiagvlflvlgllallFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1917 DEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKAS---SGKLDLELEL 1993
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1994 NKLKNIAEETQQSKLRAEEEAEKLRKL-----ALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARK 2068
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELlgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1927222982 2069 QKDDADKEAEKQILMAQ-----QAAQKCSAAEQQVQSVLAQQKED 2108
Cdd:COG4717 468 DGELAELLQELEELKAElrelaEEWAALKLALELLEEAREEYREE 512
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1287-1822 |
1.02e-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: 51.94 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1287 KTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQveplasplkKTKLDSASDNIIQEYVTLRT 1366
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE---------KLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1367 KYSELMTLTSQYiKFITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDK-QKQLAEVhakaIAKAEKEAQELKlRMQEE 1445
Cdd:TIGR04523 202 LLSNLKKKIQKN-KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtQTQLNQL----KDEQNKIKKQLS-EKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1446 VNRREDAVVDAEKQKHNIQLELHELKNLSEQQIMDKSKqvddalqsrvkieEEIRLIRLQLETTVKQKSTAESELKQLRD 1525
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK-------------SELKNQEKKLEEIQNQISQNNKIISQLNE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1526 RAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEElkrkaeaekeaakqKQKALEDLENLKRQAEEAERQV-KQAEIEK 1604
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE--------------NQSYKQEIKNLESQINDLESKIqNQEKLNQ 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1605 ERQIQVAHVAAQKSaaaELQSKHMSFVEKTSKLEESLKqehgavlQLQHEAAALKKQQEDAERAREEAEKELEKWRQKAN 1684
Cdd:TIGR04523 409 QKDEQIKKLQQEKE---LLEKEIERLKETIIKNNSEIK-------DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1685 EalrlrLQAEEEAHKKSLAQEDAE-----KQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQE 1759
Cdd:TIGR04523 479 K-----IKQNLEQKQKELKSKEKElkklnEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 1760 LIR--LRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKE 1822
Cdd:TIGR04523 554 LKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE 618
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
2071-2279 |
1.15e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 50.88 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2071 DDADKEAEKQILMAQQAAQKcsAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEA 2150
Cdd:pfam00529 52 DPTDYQAALDSAEAQLAKAQ--AQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2151 ErqkaAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKH-KKLAEQTLKQKFQVEQELTKVKL 2229
Cdd:pfam00529 130 R----VLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEvRSELSGAQLQIAEAEAELKLAKL 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222982 2230 KLDETDkQKSVLDEELQRLKDEVDDAVKQRGQ-----------------VEEELLKVKVQMEELLKL 2279
Cdd:pfam00529 206 DLERTE-IRAPVDGTVAFLSVTVDGGTVSAGLrlmfvvpednllvpgmfVETQLDQVRVGQPVLIPF 271
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1358-1808 |
1.16e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1358 IQEYVTLRTKYSELMTLTSQYIKfITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHA--KAIAKAEKEA 1435
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1436 QELKLRMQEEVNRREDaVVDAEKQKHNIQLELHELKNLS----EQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLEttvk 1511
Cdd:COG4717 149 EELEERLEELRELEEE-LEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELE---- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1512 qksTAESELKQLRDRAAEAEKLRKAAQEEAEKL--RKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQ 1589
Cdd:COG4717 224 ---ELEEELEQLENELEAAALEERLKEARLLLLiaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1590 AEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKH-MSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQedaera 1668
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEElLELLDRIEELQELLREAEELEEELQLEELEQEIAA------ 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1669 reeaekELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAED-----SALKQKEMAENELERQR 1743
Cdd:COG4717 375 ------LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeeleEELEELEEELEELEEEL 448
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 1744 KVAeSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSE 1808
Cdd:COG4717 449 EEL-REELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2285-2485 |
1.25e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2285 EENQRLIKKDKDNTQKFLAKEADNMKKLAEDAAR-----------LSVEAQEAARLRQIAE------------DDLNQQR 2341
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAaleefrqknglVDLSEEAKLLLQQLSElesqlaearaelAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2342 ALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQA---QKLLEDKQLMQQrLDEETEEYQKSLEAERKRQL-EIIAE 2417
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAelsARYTPNHPDVIA-LRAQIAALRAQLQQEAQRILaSLEAE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 2418 SEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLR 2485
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1721-1896 |
1.38e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1721 RAKAEDSALKQKEMAENELERQRKVAESTAQQKLT-AEQELIRLRADFDNAEQQRsllEDELYRLKNEVvaaQQQRKQLE 1799
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELRER---RNELQKLEKRL---LQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1800 DELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDL-------AEEASK--LRAIAEEAKHQRQV----AE 1866
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELerisgltAEEAKEilLEKVEEEARHEAAVlikeIE 179
|
170 180 190
....*....|....*....|....*....|.
gi 1927222982 1867 EEAarqRAEAERILKEKLA-AIsdaTRLKTE 1896
Cdd:PRK12704 180 EEA---KEEADKKAKEILAqAI---QRCAAD 204
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1689-2011 |
1.42e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1689 LRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFD 1768
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1769 NAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQL-LEVEATKMRDLAEE 1847
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALeQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1848 ASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALED 1927
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1928 QANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSK 2007
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQ 344
|
....
gi 1927222982 2008 LRAE 2011
Cdd:COG4372 345 LLLV 348
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1951-2661 |
1.44e-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: 51.29 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1951 MERQRAIVDDTLKQRRVVEEEIRILKlnfekassgkldlelelnklkniaEETQQSKLRAEEEAEKLRKLALeeekrrre 2030
Cdd:pfam07111 61 LSQQAELISRQLQELRRLEEEVRLLR------------------------ETSLQQKMRLEAQAMELDALAV-------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2031 aeekvkkiaaaeeeAARQRQAAQDELDRLKKKAEEARKQKDDAD-KEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDt 2109
Cdd:pfam07111 109 --------------AEKAGQAEAEGLRAALAGAEMVRKNLEEGSqRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEG- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2110 iMQTKLKEEYEKAKKLAKQAeaakEKAEREAALLRQQaeeaerqkaaaeqeaanQAKAQEDAErlrkeaefeaAKRAQAE 2189
Cdd:pfam07111 174 -LEKSLNSLETKRAGEAKQL----AEAQKEAELLRKQ-----------------LSKTQEELE----------AQVTLVE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2190 NAalkqkqqadaemakhkklaeqtlkQKFQVEQELTKVKLKLDETDKQKsvLDEELQRLKDEVDDAvkqrgQVEEELLKV 2269
Cdd:pfam07111 222 SL------------------------RKYVGEQVPPEVHSQTWELERQE--LLDTMQHLQEDRADL-----QATVELLQV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2270 KVQ-MEELLKLKlriEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVeaqeaarlrQIAEDDLNQQRALadKML 2348
Cdd:pfam07111 271 RVQsLTHMLALQ---EEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMV---------QLKAQDLEHRDSV--KQL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2349 KEKMQAIQEasrlraeaemlqRQKDLAQEQA--QKLLEDK--QLMQQRLDEET--EEYQKSLEAERKRQLEIIAESEKLK 2422
Cdd:pfam07111 337 RGQVAELQE------------QVTSQSQEQAilQRALQDKaaEVEVERMSAKGlqMELSRAQEARRRQQQQTASAEEQLK 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2423 LQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTV----VEKLEVA--RLTSSKEADDLRKAIADLEKEKS 2496
Cdd:pfam07111 405 FVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIkglmARKVALAqlRQESCPPPPPAPPVDADLSLELE 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2497 RLKKEAEDLQ--------------NKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKK 2562
Cdd:pfam07111 485 QLREERNRLDaelqlsahliqqevGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASL 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2563 AKALKDEQERQKQQMEDEKKKLQATMDAALNKQK----EAEKEMHNKQKEMKELERKRLEQErilaEENQKLReKLQqlE 2638
Cdd:pfam07111 565 RQELTQQQEIYGQALQEKVAEVETRLREQLSDTKrrlnEARREQAKAVVSLRQIQHRATQEK----ERNQELR-RLQ--D 637
|
730 740
....*....|....*....|...
gi 1927222982 2639 EAQKDQPDKEVIHVTMVETTKNV 2661
Cdd:pfam07111 638 EARKEEGQRLARRVQELERDKNL 660
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2337-2659 |
1.48e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2337 LNQQRALADKMLKEKMQAIQEASRLRAEAEMLqrqKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIA 2416
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKSLHGKAELLTLRSQLL---TLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2417 ESEKLKLQvSQLSEAQAKAQE---EAKKFKKQADSIASRLHETELAT-QEKMTVVEKLEVARLTSSKEADDLRKAIadLE 2492
Cdd:TIGR00618 252 QEEQLKKQ-QLLKQLRARIEElraQEAVLEETQERINRARKAAPLAAhIKAVTQIEQQAQRIHTELQSKMRSRAKL--LM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2493 KEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFE-EEVKKAKALKDEQE 2571
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQkLQSLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2572 RQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEE-NQKLREKLQQLEeaqkdqpDKEVI 2650
Cdd:TIGR00618 409 QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsAQSLKEREQQLQ-------TKEQI 481
|
....*....
gi 1927222982 2651 HVTMVETTK 2659
Cdd:TIGR00618 482 HLQETRKKA 490
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2056-2505 |
1.57e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.99 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2056 LDRLKKKAEEARkqkDDADK----EAEKQIlmaQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKlaKQAEA 2131
Cdd:PRK04778 81 LPDIEEQLFEAE---ELNDKfrfrKAKHEI---NEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKD--LYREL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2132 AKEKAERE------AALLRQQAEEAERQKaaaeqeaanqakaqEDAERLRKEAEFEAAK----RAQAENAALKQKqqada 2201
Cdd:PRK04778 153 RKSLLANRfsfgpaLDELEKQLENLEEEF--------------SQFVELTESGDYVEAReildQLEEELAALEQI----- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2202 eMAKHKKLAEQtLKQKFQVE--------QELTKVKLKLDETDkqksvLDEELQRLKDEVDDAVKQRGQ-----VEEELLK 2268
Cdd:PRK04778 214 -MEEIPELLKE-LQTELPDQlqelkagyRELVEEGYHLDHLD-----IEKEIQDLKEQIDENLALLEEldldeAEEKNEE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2269 VKVQMEELLKLkLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEdaarlsveaqEAARLRQ---IAEDDLNQQRALad 2345
Cdd:PRK04778 287 IQERIDQLYDI-LEREVKARKYVEKNSDTLPDFLEHAKEQNKELKE----------EIDRVKQsytLNESELESVRQL-- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2346 kmlKEKMQAIqeasrlraEAEMLQRQKDLA-QEQAQKLLEDKQlmqqrldeetEEYQKSLEaerkrqlEIIAESEKLKLQ 2424
Cdd:PRK04778 354 ---EKQLESL--------EKQYDEITERIAeQEIAYSELQEEL----------EEILKQLE-------EIEKEQEKLSEM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2425 VSQLSEAQAKAQEEAKKFKKQADSI-------------ASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADL 2491
Cdd:PRK04778 406 LQGLRKDELEAREKLERYRNKLHEIkryleksnlpglpEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDV 485
|
490
....*....|....
gi 1927222982 2492 EkeksRLKKEAEDL 2505
Cdd:PRK04778 486 E----TLEEETEEL 495
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1392-1554 |
1.77e-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: 50.77 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1392 EEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELK 1471
Cdd:pfam05262 179 DKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1472 NLSEQQIMdKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTaESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEE 1551
Cdd:pfam05262 259 NLPKPADT-SSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAK-DHKAFDLKQESKASEKEAEDKELEAQKKREPVAED 336
|
...
gi 1927222982 1552 TQK 1554
Cdd:pfam05262 337 LQK 339
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2282-2450 |
1.85e-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: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2282 RIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQiAEDDLNQQRaladkmlkeKMQAIQEASRL 2361
Cdd:pfam15709 354 RREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQ-EEEERKQRL---------QLQAAQERARQ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2362 RAEA---EMLQRQKDLAQEQAQKLLEDKqlmqQRLDEETEEyqksLEAERKRQLEiIAESEKLKLQvSQLSEAQAKAQEE 2438
Cdd:pfam15709 424 QQEEfrrKLQELQRKKQQEEAERAEAEK----QRQKELEMQ----LAEEQKRLME-MAEEERLEYQ-RQKQEAEEKARLE 493
|
170
....*....|..
gi 1927222982 2439 AKKFKKQADSIA 2450
Cdd:pfam15709 494 AEERRQKEEEAA 505
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2054-2644 |
1.85e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2054 DELDRLK--------------KKA----------EEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSvlAQQKEDt 2109
Cdd:PRK04863 390 EEVDELKsqladyqqaldvqqTRAiqyqqavqalERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLS--LEQKLS- 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2110 iMQTKLKEEYEKAKKLAKQA------EAAKEKA---EREAALLRQQAEEAErQKAAAEQEAANQAKAQEDAERLRKEAEF 2180
Cdd:PRK04863 467 -VAQAAHSQFEQAYQLVRKIagevsrSEAWDVArelLRRLREQRHLAEQLQ-QLRMRLSELEQRLRQQQRAERLLAEFCK 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2181 EAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSV---LDEELQRLKDEVDDAVK 2257
Cdd:PRK04863 545 RLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFE 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2258 QRGQVEEELLKVKVQMEELLKLKLRIEEENQRLiKKDKDNTQKFLAKEADNMKKLAED--AARLS-----VEAQEAA--- 2327
Cdd:PRK04863 625 DSQDVTEYMQQLLERERELTVERDELAARKQAL-DEEIERLSQPGGSEDPRLNALAERfgGVLLSeiyddVSLEDAPyfs 703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2328 ----RLRQ-IAEDDLNQ-QRALA------------------------DKMLKEKMQAIQEA------SRLRAE------- 2364
Cdd:PRK04863 704 alygPARHaIVVPDLSDaAEQLAgledcpedlyliegdpdsfddsvfSVEELEKAVVVKIAdrqwrySRFPEVplfgraa 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2365 ----AEMLQRQKDLAQEQAQKLLEDKQLMqQRLDEETEEY-------------QKSLEAERKRQLEIIAESEKLKLQVSQ 2427
Cdd:PRK04863 784 rekrIEQLRAEREELAERYATLSFDVQKL-QRLHQAFSRFigshlavafeadpEAELRQLNRRRVELERALADHESQEQQ 862
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2428 LSEAQAKAQEEAKKFKKQADSIAsrLHETELATQEKMTVVEKLEVArltsSKEADDLR---KAIADLEKEKSRLKKEAED 2504
Cdd:PRK04863 863 QRSQLEQAKEGLSALNRLLPRLN--LLADETLADRVEEIREQLDEA----EEAKRFVQqhgNALAQLEPIVSVLQSDPEQ 936
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2505 LQNKSKEMADAQQKQieheKTVLQQTF-LSE-------------KEMLLKKEKLIEEEKKRLEsQFEEEVKKAKalkdEQ 2570
Cdd:PRK04863 937 FEQLKQDYQQAQQTQ----RDAKQQAFaLTEvvqrrahfsyedaAEMLAKNSDLNEKLRQRLE-QAEQERTRAR----EQ 1007
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2571 ERQKQQMEDEKKKLQATMDAALNKQKEAEKEMhnkQKEMKEL---------ERKRLEQERIlaeeNQKLREKLQQLEEAQ 2641
Cdd:PRK04863 1008 LRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL---KQELQDLgvpadsgaeERARARRDEL----HARLSANRSRRNQLE 1080
|
...
gi 1927222982 2642 KDQ 2644
Cdd:PRK04863 1081 KQL 1083
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1386-1562 |
1.86e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1386 QRRLEDEEKaaEKLKAEEQKKMAMMQA--ELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDavvDAEKQKHNI 1463
Cdd:PRK09510 100 QERLKQLEK--ERLAAQEQKKQAEEAAkqAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAA---EAKKKAEAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1464 QLELHELKNLSEQQIMDKSKQVDDAlqsRVKIEEEirlirlqlettVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEK 1543
Cdd:PRK09510 175 AAKKAAAEAKKKAEAEAAAKAAAEA---KKKAEAE-----------AKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEK 240
|
170
....*....|....*....
gi 1927222982 1544 LRKQVNEETQKKRMAEEEL 1562
Cdd:PRK09510 241 AAAAKAAEKAAAAKAAAEV 259
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1692-1924 |
1.87e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 51.10 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1692 QAEEEAHKKSLAQE--DAEKQ---KEEAEREAKKRAKAEDSALKQKEMaeneleRQRKVAESTAQQKLTAEQELIRLRAD 1766
Cdd:PRK05035 440 AIEQEKKKAEEAKArfEARQArleREKAAREARHKKAAEARAAKDKDA------VAAALARVKAKKAAATQPIVIKAGAR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1767 FDNAE-----QQRSLLEDELYRLKNEVVAAQQQRKQLEDELAkvRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKM 1841
Cdd:PRK05035 514 PDNSAviaarEARKAQARARQAEKQAAAAADPKKAAVAAAIA--RAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKA 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1842 RDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKT---EAEIA-LKEKEAENERLRRQAED 1917
Cdd:PRK05035 592 KKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKaavAAAIArAKARKAAQQQANAEPEE 671
|
....*..
gi 1927222982 1918 EAYQRKA 1924
Cdd:PRK05035 672 AEDPKKA 678
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2095-2496 |
1.93e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.45 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2095 EQQVQSVLAQQKEDTIMQTKLKEE---YEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERqkaaaeqeaaNQAKAQEDA 2171
Cdd:pfam19220 37 EAILRELPQAKSRLLELEALLAQEraaYGKLRRELAGLTRRLSAAEGELEELVARLAKLEA----------ALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2172 ERLRKEaefEAAKRAQAENaaLKQKQQADAEMAKHKKLAEQTLKQKFQVeqeltkvklkldetdkqksvLDEELQRLKDE 2251
Cdd:pfam19220 107 EELRIE---LRDKTAQAEA--LERQLAAETEQNRALEEENKALREEAQA--------------------AEKALQRAEGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2252 VDDAVKQRGQVEEELLKVKVQMEE----LLKLKLRIEEENQRLikkdkdntqkflakeADNMKKLAEDAARLSVEAQEAA 2327
Cdd:pfam19220 162 LATARERLALLEQENRRLQALSEEqaaeLAELTRRLAELETQL---------------DATRARLRALEGQLAAEQAERE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2328 RLRQIAEDDLNQQRAlADKMLKEKMQAIQE----ASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEyqks 2403
Cdd:pfam19220 227 RAEAQLEEAVEAHRA-ERASLRMKLEALTAraaaTEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAG---- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2404 LEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLhETELATQEKmtvveKLEVARLTSSKEADD 2483
Cdd:pfam19220 302 LEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASL-SDRIAELTK-----RFEVERAALEQANRR 375
|
410
....*....|...
gi 1927222982 2484 LRkaiADLEKEKS 2496
Cdd:pfam19220 376 LK---EELQRERA 385
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1289-1754 |
2.00e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1289 LKEQLAQEKKLLEEVEGNKDKVDecqkyakayIDTIKDYELQLVAYKAQVEPLASPLKK-TKLDSASDNIIQEYVTLRTK 1367
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELN---------LKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1368 YSELMTLTSQY--IKFITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHakaiAKAEKEAQELKLRMQEE 1445
Cdd:COG4717 118 LEKLEKLLQLLplYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQ----EELEELLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1446 VNRREDAVVDAEKQKHNIQLELHELknlsEQQIMDKSKQVDDALQSRVKIEEEIRL----IRLQLETTVKQKSTAESELK 1521
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEA----QEELEELEEELEQLENELEAAALEERLkearLLLLIAAALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1522 QLRDRAAEA---------------EKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENL 1586
Cdd:COG4717 270 SLILTIAGVlflvlgllallflllAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1587 K---RQAEEAERQVKQAEIEKERQIQVAHVAAQK----SAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQL--QHEAAA 1657
Cdd:COG4717 350 QellREAEELEEELQLEELEQEIAALLAEAGVEDeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELleALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1658 LKKQQEDAERAREEAEKELEKWRQKANEaLRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAedsalkqkEMAEN 1737
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAE-LEAELEQLEEDGELAELLQELEELKAELRELAEEWAAL--------KLALE 500
|
490
....*....|....*..
gi 1927222982 1738 ELERQRKVAESTAQQKL 1754
Cdd:COG4717 501 LLEEAREEYREERLPPV 517
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
65-185 |
2.02e-05 |
|
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: 46.91 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 65 ERDRVQKKTFTKWVNKhlIKSQRQVTDLYEDLRDGHNLISLLEVLSgetLPRERDVVRSVRLPREKGRMRfhKLQNVQIA 144
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIK---VPVDWNRVNKPPYPKLGENMK--KLENCNYA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1927222982 145 LDFLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 185
Cdd:cd21330 82 VELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1503-1754 |
2.03e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 50.36 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1503 RLQLETTVKQKST---AESELKQLRDRAAEAEKLRKAAqeeaekLRKQVNEETQKkrMAEEELKRKAEAEKEAAKQKQKA 1579
Cdd:PRK07735 36 KLEEENREKEKALpknDDMTIEEAKRRAAAAAKAKAAA------LAKQKREGTEE--VTEEEKAKAKAKAAAAAKAKAAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1580 LedlenlKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALK 1659
Cdd:PRK07735 108 L------AKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1660 KQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKK-SLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENE 1738
Cdd:PRK07735 182 KQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKaSQGNGDSGDEDAKAKAIAAAKAKAAAAARAKTKGAEGK 261
|
250
....*....|....*.
gi 1927222982 1739 LERQRKVAESTAQQKL 1754
Cdd:PRK07735 262 KEEEPKQEEPSVNQPY 277
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1505-1928 |
2.22e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.68 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1505 QLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLE 1584
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1585 NLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQED 1664
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1665 AERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRK 1744
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1745 VAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDElyrlkNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETM 1824
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAE-----AVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELA 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1825 SNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEK 1904
Cdd:COG5278 426 EALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALAL 505
|
410 420
....*....|....*....|....
gi 1927222982 1905 EAENERLRRQAEDEAYQRKALEDQ 1928
Cdd:COG5278 506 AALLLAAAEAALAAALAAALASAE 529
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1826-2177 |
2.29e-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: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1826 NSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEA-EIALKEK 1904
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEyEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1905 EAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRaivddtlkqrrvvEEEIRILKLNFEKAss 1984
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEER-------------EEDERILEYLKEKA-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1985 GKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALeeekrrreaeekvkkiaaaeeeaarqrqaaqDELDRLKKKAE 2064
Cdd:pfam13868 166 EREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAER-------------------------------DELRAKLYQEE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2065 EARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIM--QTKLKEEYEKAKKLAKQAEAAKEKAEREAAL 2142
Cdd:pfam13868 215 QERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEefERMLRKQAEDEEIEQEEAEKRRMKRLEHRRE 294
|
330 340 350
....*....|....*....|....*....|....*
gi 1927222982 2143 LRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKE 2177
Cdd:pfam13868 295 LEKQIEEREEQRAAEREEELEEGERLREEEAERRE 329
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2059-2402 |
2.35e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 50.78 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2059 LKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQ----QKEDTIMQTKLKEEYEKAKKLAKQAEAA-- 2132
Cdd:NF033838 144 ATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAElelvKEEAKEPRDEEKIKQAKAKVESKKAEATrl 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2133 -KEKAEREAAllrqqAEEAERQKAAAEQEAANQAKAQEDAERLRKEaefeaAKRAQAENAALKQKQQADAEmAKHKKLAE 2211
Cdd:NF033838 224 eKIKTDREKA-----EEEAKRRADAKLKEAVEKNVATSEQDKPKRR-----AKRGVLGEPATPDKKENDAK-SSDSSVGE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2212 QTLKQ-KFQVEQELTKVKLKLDETDKQKSVLDEELQRlkdevDDAVKQRGQVEEELLKVKVQMEElLKLKLRIEEenqrl 2290
Cdd:NF033838 293 ETLPSpSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRR-----NYPTNTYKTLELEIAESDVKVKE-AELELVKEE----- 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2291 ikkdkdntqkflAKEADNMKKLAEDAARLSVEAQEAARLRQI------AEDDLNQQRALADKMLKEKMQAIQEASRLRAE 2364
Cdd:NF033838 362 ------------AKEPRNEEKIKQAKAKVESKKAEATRLEKIktdrkkAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPE 429
|
330 340 350
....*....|....*....|....*....|....*...
gi 1927222982 2365 AEMLQRQKDLAQEQAQKlLEDKQLMQQRLDEETEEYQK 2402
Cdd:NF033838 430 KPAPKPEKPAEQPKAEK-PADQQAEEDYARRSEEEYNR 466
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1464-1824 |
2.43e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1464 QLELHELKNLSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRaaeaeklRKAAQEEAEK 1543
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE-------LEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1544 LRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAEL 1623
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1624 QSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLA 1703
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1704 QEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYR 1783
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1927222982 1784 LKNEVVAAQQQ---RKQLEDELAKVRSEMDVLIQLKSKAEKETM 1824
Cdd:COG4372 325 AKKLELALAILlaeLADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2082-2328 |
2.50e-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: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2082 LMAQQAAQKCSAAEQQVQSVLAQQKEdtimqtkLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAaaeQEA 2161
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAE-------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA---ALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2162 ANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQkfqveqeLTKVKLKLDETDKQKSVL 2241
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR-------LQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2242 DEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLiKKDKDNTQKFLAKEADNMKKLAEDAARLSV 2321
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL-EKELAELAAELAELQQEAEELEALIARLEA 234
|
....*..
gi 1927222982 2322 EAQEAAR 2328
Cdd:COG4942 235 EAAAAAE 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2344-2641 |
2.58e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2344 ADKMLKEKMQAIQEASRLRAEAEMLQRQkDLAQEQAQKLLEDKQLMQQRLDEET--EEYQKSLEAERKRQ---LEIIAES 2418
Cdd:COG3206 66 SDVLLSGLSSLSASDSPLETQIEILKSR-PVLERVVDKLNLDEDPLGEEASREAaiERLRKNLTVEPVKGsnvIEISYTS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2419 E-----KLKLQ------VSQLSEAQAKAQEEAKKF-KKQADSIASRLHETELAtqekmtvVEKLEVAR--LTSSKEADDL 2484
Cdd:COG3206 145 PdpelaAAVANalaeayLEQNLELRREEARKALEFlEEQLPELRKELEEAEAA-------LEEFRQKNglVDLSEEAKLL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2485 RKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEkemLLKKEKLIEEEKKRLESQFEEEVKKAK 2564
Cdd:COG3206 218 LQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ---LRAQLAELEAELAELSARYTPNHPDVI 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2565 ALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMK---------ELERKRLEQERILAEEN-QKLREKL 2634
Cdd:COG3206 295 ALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEarlaelpelEAELRRLEREVEVARELyESLLQRL 374
|
....*..
gi 1927222982 2635 QQLEEAQ 2641
Cdd:COG3206 375 EEARLAE 381
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2115-2447 |
2.59e-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: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2115 LKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEaefEAAKRAQAENAALK 2194
Cdd:pfam13868 1 LRENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEK---EEERKEERKRYRQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2195 QKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKL----KLDETDKQKSVLDEELQRLKDEVDDAV-KQRGQVEEELLKV 2269
Cdd:pfam13868 78 LEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEedqaEAEEKLEKQRQLREEIDEFNEEQAEWKeLEKEEEREEDERI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2270 KVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEdaarlsveaQEAARLRQIAEDdlnQQRALADKMLK 2349
Cdd:pfam13868 158 LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAE---------RDELRAKLYQEE---QERKERQKERE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2350 EKMQAIQEASRLRAE-AEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQL 2428
Cdd:pfam13868 226 EAEKKARQRQELQQArEEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQ 305
|
330
....*....|....*....
gi 1927222982 2429 SEAQAKAQEEAKKFKKQAD 2447
Cdd:pfam13868 306 RAAEREEELEEGERLREEE 324
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2765-2798 |
2.64e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.64e-05
10 20 30
....*....|....*....|....*....|....
gi 1927222982 2765 LLEAQAATGSILDPIKNQKLSVNEAVKEGVIGPE 2798
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4164-4192 |
2.72e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.72e-05
10 20
....*....|....*....|....*....
gi 1927222982 4164 VRKRRVVIVDPETGKEMTVYEAYRKGLID 4192
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
67-178 |
2.91e-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: 46.50 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 67 DRVQKKTFTKWVNKHLIKS--QRQVTDLYEDLRDGHNLISLLEVLSGETLpreRDVVRSvrlPREKGRMrfhkLQNVQIA 144
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKI---EDINGC---PKNRSQM----IENIDAC 77
|
90 100 110
....*....|....*....|....*....|....
gi 1927222982 145 LDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTI 178
Cdd:cd21285 78 LSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1583-1756 |
3.48e-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: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1583 LENL-KRQAEE--AERQVKQAEIEKERQIQVAhVAAQKSAAAELQSKhmsfvektskleeslkQEHGAVLQLQHEAAALK 1659
Cdd:COG2268 186 LDALgRRKIAEiiRDARIAEAEAERETEIAIA-QANREAEEAELEQE----------------REIETARIAEAEAELAK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1660 KQQEDAERARE---EAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAE 1736
Cdd:COG2268 249 KKAEERREAETaraEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAE 328
|
170 180
....*....|....*....|
gi 1927222982 1737 NELERQRKVAESTAQQKLTA 1756
Cdd:COG2268 329 AEAIRAKGLAEAEGKRALAE 348
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
70-190 |
3.52e-05 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 46.97 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 70 QKKTFTKWVNK---------HLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPrERDVVRSVRLPrekgrmrFHKLQN 140
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTID-ERAINKKKLTP-------FIIQEN 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1927222982 141 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQIN 190
Cdd:cd21325 97 LNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1862-2101 |
3.54e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1862 RQVAEEEAARQRAEAERILKEklaAISDATRLKTEAEIALKEkeaENERLRRQAEDEAYQRKA----LEDQANQHKQQIE 1937
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEE---AKKEAEAIKKEALLEAKE---EIHKLRNEFEKELRERRNelqkLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1938 EKIVLLKKSsEAEMERQRAIVDDTLKQRRVVEEEIRILKLNfekassgkldlelELNKLKNIA----EETQQSKL-RAEE 2012
Cdd:PRK12704 100 RKLELLEKR-EEELEKKEKELEQKQQELEKKEEELEELIEE-------------QLQELERISgltaEEAKEILLeKVEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2013 EAEKlrklaleeekrrreaeekvkkiaaaeeeaarqrqaaqdELDRLKKKAEEarKQKDDADKEAEKQILmaqQAAQKCS 2092
Cdd:PRK12704 166 EARH--------------------------------------EAAVLIKEIEE--EAKEEADKKAKEILA---QAIQRCA 202
|
250
....*....|..
gi 1927222982 2093 ---AAEQQVQSV 2101
Cdd:PRK12704 203 adhVAETTVSVV 214
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2480-2648 |
4.09e-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: 49.56 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2480 EADDLRKAIADLEKEKS--------RLKKEAEDLQNKSKEMADA---QQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEE 2548
Cdd:pfam15709 317 EEDPSKALLEKREQEKAsrdrlraeRAEMRRLEVERKRREQEEQrrlQQEQLERAEKMREELELEQQRRFEEIRLRKQRL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2549 KKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAalNKQKEAEKEMHNKQKEmKELERKRLEQERILAE--E 2626
Cdd:pfam15709 397 EEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRK--KQQEEAERAEAEKQRQ-KELEMQLAEEQKRLMEmaE 473
|
170 180
....*....|....*....|..
gi 1927222982 2627 NQKLREKLQQLEEAQKDQPDKE 2648
Cdd:pfam15709 474 EERLEYQRQKQEAEEKARLEAE 495
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2109-2371 |
5.07e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2109 TIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAAlLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQA 2188
Cdd:PRK05035 440 AIEQEKKKAEEAKARFEARQARLEREKAAREAR-HKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSA 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2189 ENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAV-----KQRGQVE 2263
Cdd:PRK05035 519 VIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIarakaKKAAQQA 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2264 EELLKVKVQMEELLKlKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARlsveAQEAARLRQIAEDDLNQQRAL 2343
Cdd:PRK05035 599 ASAEPEEQVAEVDPK-KAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAI----ARAKARKAAQQQANAEPEEAE 673
|
250 260
....*....|....*....|....*...
gi 1927222982 2344 ADKmlKEKMqaiqEASRLRAEAEMLQRQ 2371
Cdd:PRK05035 674 DPK--KAAV----AAAIARAKAKKAAQQ 695
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2354-2644 |
5.28e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.48 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2354 AIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLE----AERKRQLEIIAESEKLKLQVSQLS 2429
Cdd:pfam02029 15 AREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDrtakREERRQKRLQEALERQKEFDPTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2430 EA-------QAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEK----LEVARLTSSKEADDLRKAIADLEKEKSRL 2498
Cdd:pfam02029 95 DEkesvaerKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQenkwSTEVRQAEEEGEEEEDKSEEAEEVPTENF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2499 KKEAEDLQNKSKEMADA-------QQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQE 2571
Cdd:pfam02029 175 AKEEVKDEKIKKEKKVKyeskvflDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2572 RQKQQMEDEK-KKLQatmdaalNKQKEAEKEMHNKQKEMK---------ELERKRLEQERILAEENQKLREKLQ----QL 2637
Cdd:pfam02029 255 RRRQEKESEEfEKLR-------QKQQEAELELEELKKKREerrklleeeEQRRKQEEAERKLREEEEKRRMKEEierrRA 327
|
....*..
gi 1927222982 2638 EEAQKDQ 2644
Cdd:pfam02029 328 EAAEKRQ 334
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1195-1933 |
5.49e-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: 49.95 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1195 EAELKKATAVSDKMSRVHSERDAELDHYRQLLSSLQDRWKAVFSQIDLRQRELEQLGRQLGYYREsydwlirwindAKQR 1274
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQ-----------AVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1275 QEKIQAV------TITDSKTLKEQL-AQEKKLLEEVEGNKDKVDECQKyAKAYIDtiKDYELqlvaykaqVEPLASPLKK 1347
Cdd:COG3096 422 LEKARALcglpdlTPENAEDYLAAFrAKEQQATEEVLELEQKLSVADA-ARRQFE--KAYEL--------VCKIAGEVER 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1348 TKLDSASDNIIQEYVTLRTKYSELMTLTSQYikfiTDSQRRLEdEEKAAEKLKAEEQKKMAmmqAELDKQKQLAEVHAKA 1427
Cdd:COG3096 491 SQAWQTARELLRRYRSQQALAQRLQQLRAQL----AELEQRLR-QQQNAERLLEEFCQRIG---QQLDAAEELEELLAEL 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1428 IAKAE------KEAQELKLRMQ---EEVNRREDAVVDAEKQKHNIQLELHELKNLSEQQIMDkSKQVDDALQSRVKIE-- 1496
Cdd:COG3096 563 EAQLEeleeqaAEAVEQRSELRqqlEQLRARIKELAARAPAWLAAQDALERLREQSGEALAD-SQEVTAAMQQLLEREre 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1497 -----EEIRLIRLQLETTVKQKSTA----ESELKQLRDR-----------------AAEAEKLR------------KAAQ 1538
Cdd:COG3096 642 atverDELAARKQALESQIERLSQPggaeDPRLLALAERlggvllseiyddvtledAPYFSALYgparhaivvpdlSAVK 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1539 E---------------------------EAEKLRKQV---NEETQKK-----------RMAEEelKRkaeaekeaakqkq 1577
Cdd:COG3096 722 EqlagledcpedlyliegdpdsfddsvfDAEELEDAVvvkLSDRQWRysrfpevplfgRAARE--KR------------- 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1578 kaledLENLKRQAEEAERQVKQAEIEKERQIQVAH-----------VAAQKSAAAELQSKHmsfvEKTSKLEESLKQEHG 1646
Cdd:COG3096 787 -----LEELRAERDELAEQYAKASFDVQKLQRLHQafsqfvgghlaVAFAPDPEAELAALR----QRRSELERELAQHRA 857
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1647 AVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEA------HKKSLAQED-------AEKQKEE 1713
Cdd:COG3096 858 QEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAqafiqqHGKALAQLEplvavlqSDPEQFE 937
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1714 AEREAKKRAKAEDSALKQKEMAENELeRQRKV--AESTAQQKLTAEQELI-RLRADFDNAEQQRSLLEDelyrlknevvA 1790
Cdd:COG3096 938 QLQADYLQAKEQQRRLKQQIFALSEV-VQRRPhfSYEDAVGLLGENSDLNeKLRARLEQAEEARREARE----------Q 1006
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1791 AQQQRKQLEDELAkvrsemdVLIQLKSKAEketmsnserskqlleveaTKMRDLAEEASKLRAIAEEAKHQrqvAEEEAA 1870
Cdd:COG3096 1007 LRQAQAQYSQYNQ-------VLASLKSSRD------------------AKQQTLQELEQELEELGVQADAE---AEERAR 1058
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 1871 RQRAEaeriLKEKLAAiSDATRLKTEAEIALKEKEAEN--ERLRRQAEDEAYQRKaledQANQHK 1933
Cdd:COG3096 1059 IRRDE----LHEELSQ-NRSRRSQLEKQLTRCEAEMDSlqKRLRKAERDYKQERE----QVVQAK 1114
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1386-1542 |
5.83e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.10 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1386 QRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKA------IAKAEKEAQELKLRMQEEVNRREdAVVDAEkq 1459
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEReietarIAEAEAELAKKKAEERREAETAR-AEAEAA-- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1460 khniqlelhelknLSEQQImdkskqvddalQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDR--AAEAEKLRKAA 1537
Cdd:COG2268 268 -------------YEIAEA-----------NAEREVQRQLEIAEREREIELQEKEAEREEAELEADVrkPAEAEKQAAEA 323
|
....*
gi 1927222982 1538 QEEAE 1542
Cdd:COG2268 324 EAEAE 328
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1163-1337 |
6.17e-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: 47.44 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1163 VPNDVKEVETYRTKLKKMRAEAEGEQPVFDSLEAElkkatavSDKMSRVHSERDAELdhyRQLLSSLQDRWKAVFSQIDL 1242
Cdd:cd00176 28 YGDDLESVEALLKKHEALEAELAAHEERVEALNEL-------GEQLIEEGHPDAEEI---QERLEELNQRWEELRELAEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1243 RQRELEQLGRQLGYYRESYDwLIRWINDAKQRQEKIQavTITDSKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYID 1322
Cdd:cd00176 98 RRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLE 174
|
170
....*....|....*
gi 1927222982 1323 TIKDYELQLVAYKAQ 1337
Cdd:cd00176 175 EGHPDADEEIEEKLE 189
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2273-2464 |
6.35e-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: 47.61 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2273 MEELLKLKLRIEEENQRL--IKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKmLKE 2350
Cdd:COG1579 2 MPEDLRALLDLQELDSELdrLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2351 KMQAIQEASrlraEAEMLQRQKDlAQEQAQKLLEDKQLmqqRLDEETEEYQKSLEAERKRQLEIIAESEKLKlqvSQLSE 2430
Cdd:COG1579 81 QLGNVRNNK----EYEALQKEIE-SLKRRISDLEDEIL---ELMERIEELEEELAELEAELAELEAELEEKK---AELDE 149
|
170 180 190
....*....|....*....|....*....|....
gi 1927222982 2431 AQAKAQEEAKKFKKQADSIASRLHETELATQEKM 2464
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKIPPELLALYERI 183
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
64-179 |
6.62e-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: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 64 DERDRVQkktFTKWVNK---------HLIKSQRQVTDLYEDLRDGHNLISLLEvlsgETLPRERDVVRSVRLPRE-KGRM 133
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLIN----DSVPDTIDERVLNKPPRKnKPLN 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1927222982 134 RFHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 179
Cdd:cd21294 77 NFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1790-1963 |
6.63e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 49.25 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1790 AAQQQRKQLEDElAKVRSEmdvLIQLKSKAEKEtmsnsERSKQLLEVEAtkmRDLAEEAS-KLRAIAEeakhqrqvAEEE 1868
Cdd:PTZ00491 667 AARHQAELLEQE-ARGRLE---RQKMHDKAKAE-----EQRTKLLELQA---ESAAVESSgQSRAEAL--------AEAE 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1869 AARQRAEAErilkeklaaiSDATRLKTEAEIALKEKEAENERLRRQAEdeayqrkaledqANQHKQQIEEKIVLLKKSSE 1948
Cdd:PTZ00491 727 ARLIEAEAE----------VEQAELRAKALRIEAEAELEKLRKRQELE------------LEYEQAQNELEIAKAKELAD 784
|
170
....*....|....*....
gi 1927222982 1949 AEMERQRAIVD----DTLK 1963
Cdd:PTZ00491 785 IEATKFERIVEalgrETLI 803
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2112-2217 |
6.64e-05 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 45.93 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2112 QTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEE--AERQKAAAEQEAANQAKAQEDAERLRKEAEfeaAKRAQAE 2189
Cdd:COG0711 33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEiiAEARKEAEAIAEEAKAEAEAEAERIIAQAE---AEIEQER 109
|
90 100
....*....|....*....|....*...
gi 1927222982 2190 NAALKQKQQADAEMAkhKKLAEQTLKQK 2217
Cdd:COG0711 110 AKALAELRAEVADLA--VAIAEKILGKE 135
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
70-189 |
6.91e-05 |
|
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: 46.16 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 70 QKKTFTKWVNK---------HLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPrERDVVRSVRLPrekgrmrFHKLQN 140
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTID-ERTINKKKLTP-------FTIQEN 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1927222982 141 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQI 189
Cdd:cd21324 97 LNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1748-1900 |
7.85e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 49.25 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1748 STAQQKLTAEQELIRLradfdnaEQQ-RSLLEdeLYRLKNEVVAAQQQRK--QLEDELAKVRSemdvliQLKSKAEKETM 1824
Cdd:PTZ00491 660 TTKSQEAAARHQAELL-------EQEaRGRLE--RQKMHDKAKAEEQRTKllELQAESAAVES------SGQSRAEALAE 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1825 SNSERSKQLLEVEATKMRDLAE------EASKLRAIAE-EAKHQRQVAEEEAARQRAEAErILKEKLAAISDATRLKTEA 1897
Cdd:PTZ00491 725 AEARLIEAEAEVEQAELRAKALrieaeaELEKLRKRQElELEYEQAQNELEIAKAKELAD-IEATKFERIVEALGRETLI 803
|
...
gi 1927222982 1898 EIA 1900
Cdd:PTZ00491 804 AIA 806
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1701-1954 |
8.04e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.99 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1701 SLAQEDAEKQKEEAEREAKKRAKAEdsalKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADfdnAEQQRSLLEDE 1780
Cdd:pfam00038 22 FLEQQNKLLETKISELRQKKGAEPS----RLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLA---AEDFRQKYEDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1781 LyRLKNEVVAA-QQQRKQLEDE-LAKVRSEMDV------LIQLKSKAE---KETMSNSERSKQLLEVEATKMRDLAeeas 1849
Cdd:pfam00038 95 L-NLRTSAENDlVGLRKDLDEAtLARVDLEAKIeslkeeLAFLKKNHEeevRELQAQVSDTQVNVEMDAARKLDLT---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1850 klRAIAEeakhQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERL--RRQAEDEAY--QRKAL 1925
Cdd:pfam00038 170 --SALAE----IRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTiqSLEIELQSLkkQKASL 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1927222982 1926 EDQ--------ANQHKQ------QIEEKIVLLKksseAEMERQ 1954
Cdd:pfam00038 244 ERQlaeteeryELQLADyqelisELEAELQETR----QEMARQ 282
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2092-2238 |
8.10e-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: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2092 SAAEQQVQSvLAQQKEDTImqtklKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEaanqaKAQEDA 2171
Cdd:TIGR02794 46 GAVAQQANR-IQQQKKPAA-----KKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAE-----QAAKQA 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222982 2172 ERLRKEAEfEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVE--QELTKVKLKLDETDKQK 2238
Cdd:TIGR02794 115 EEKQKQAE-EAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEakKKAEEAKKKAEAEAKAK 182
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2054-2515 |
8.22e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.97 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2054 DELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAK 2133
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELEL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2134 EKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQE---DAERLRKEAEFEAAKRAQ--AENAALKQKQQADAEMAKHKK 2208
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSslaEAEQRIKELEFEIQSQEQdsEIVKNSKSELARIPELEKELE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2209 ------------------LAEQT--LKQKFQ-----------VEQELTKVKLKLDETDK--QKSVLD-----------EE 2244
Cdd:pfam05557 208 rlrehnkhlnenienkllLKEEVedLKRKLEreekyreeaatLELEKEKLEQELQSWVKlaQDTGLNlrspedlsrriEQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2245 LQR----LKDEVDDAV-------KQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKdkdntQKFLAKEADNMKKL- 2312
Cdd:pfam05557 288 LQQreivLKEENSSLTssarqleKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRR-----VLLLTKERDGYRAIl 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2313 ---------AEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQ------- 2376
Cdd:pfam05557 363 esydkeltmSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADpsyskee 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2377 -EQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHE 2455
Cdd:pfam05557 443 vDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKK 522
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2456 TELATQEKMTVVEKlevARLTSSKEADDLRKAIADLEKEKSRLKkeaEDLQNKSKEMADA 2515
Cdd:pfam05557 523 LEDDLEQVLRLPET---TSTMNFKEVLDLRKELESAELKNQRLK---EVFQAKIQEFRDV 576
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2060-2511 |
8.61e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.50 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2060 KKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAERE 2139
Cdd:COG3064 26 RAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2140 AALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQ 2219
Cdd:COG3064 106 AAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2220 VEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQ 2299
Cdd:COG3064 186 AAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2300 KFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADkmlkekmqAIQEASRLRAEAEMLQRQKDLAQEQA 2379
Cdd:COG3064 266 AAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAV--------AAEEAVLAAAAAAGALVVRGGGAASL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2380 QKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELA 2459
Cdd:COG3064 338 EAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASA 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1927222982 2460 TQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKE 2511
Cdd:COG3064 418 VELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAV 469
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2049-2188 |
8.76e-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: 48.46 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2049 RQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSvlAQQKEDTIMQTKLKEEYEKAKKLAKQ 2128
Cdd:pfam05262 215 AQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADT--SSPKEDKQVAENQKREIEKAQIEIKK 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222982 2129 AEAAKEKAEREAA--LLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQA 2188
Cdd:pfam05262 293 NDEEALKAKDHKAfdLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNED 354
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2061-2397 |
8.81e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 48.11 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2061 KKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREA 2140
Cdd:pfam15558 18 KEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2141 ALLRQQaeEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAEnaalkQKQQADAEMAKHKK-LAEQTLKQKFQ 2219
Cdd:pfam15558 98 EQAEDQ--ENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNS-----LQLQERLEEACHKRqLKEREEQKKVQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2220 VE--QELTKVKLKLDETDKQkSVLDEELQRLKDEVDDAVKQ---RGQVEEEL--LKVKVQMEE--LLKLKLRIEEENQRl 2290
Cdd:pfam15558 171 ENnlSELLNHQARKVLVDCQ-AKAEELLRRLSLEQSLQRSQenyEQLVEERHreLREKAQKEEeqFQRAKWRAEEKEEE- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2291 ikkdKDNTQKFLAKEADNMKKLAEDAARLSVEaQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQE----ASRLRAEAE 2366
Cdd:pfam15558 249 ----RQEHKEALAELADRKIQQARQVAHKTVQ-DKAQRARELNLEREKNHHILKLKVEKEEKCHREGikeaIKKKEQRSE 323
|
330 340 350
....*....|....*....|....*....|.
gi 1927222982 2367 MLQRQKDLAQEQAQKLLEDKQLMQQRLDEET 2397
Cdd:pfam15558 324 QISREKEATLEEARKTARASFHMREKVREET 354
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1786-1907 |
8.88e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.05 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1786 NEVVAA-QQQRKQLEDELAKVRSemdvliqLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQ--R 1862
Cdd:PRK00409 519 NELIASlEELERELEQKAEEAEA-------LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiiK 591
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1927222982 1863 QVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAE 1907
Cdd:PRK00409 592 ELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4031-4062 |
9.00e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 9.00e-05
10 20 30
....*....|....*....|....*....|..
gi 1927222982 4031 KLLSAERAVTGYRDPYSGKTISLFQAMKKGLI 4062
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1766-1918 |
9.11e-05 |
|
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: 48.77 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1766 DFDNAEQQRSLlEDELYRLKNEVVAAQQQ-----RKQLEDELAKVRSE-MDVLIqLKSKAEKEtmsnsERSKQLLEVEAt 1839
Cdd:pfam04147 120 DFDDDDDDDSE-EEEDGQLDLKRVRRAHFgggedDEEEEPERKKSKKEvMEEVI-AKSKLHKY-----ERQKAKEEDEE- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1840 kMR-----DLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAE--RILKE----KLAAISDatRLKTEAEIALKEKE--- 1905
Cdd:pfam04147 192 -LReeldkELKDLRSLLSGSKRPKPEQAKKPEEKPDRKKPDDDydKLVRElafdKRAKPSD--RTKTEEELAEEEKErle 268
|
170
....*....|....*
gi 1927222982 1906 -AENERLRR-QAEDE 1918
Cdd:pfam04147 269 kLEEERLRRmRGEED 283
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
69-182 |
9.20e-05 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 45.10 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 69 VQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPrerdvVRSVRLPREKGRmrfHKLQNVQIALDFL 148
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVP-----LHSFHLTPTSFE---QKVHNVQFAFELM 87
|
90 100 110
....*....|....*....|....*....|....
gi 1927222982 149 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 182
Cdd:cd21306 88 QDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1502-1850 |
9.51e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.75 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1502 IRLQLETTVKQKSTAESE--LKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKqkqka 1579
Cdd:PRK11281 41 VQAQLDALNKQKLLEAEDklVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETR----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1580 lEDLENLK-RQAEE--AERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLK--QEHGAVL----- 1649
Cdd:PRK11281 116 -ETLSTLSlRQLESrlAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKggKVGGKALrpsqr 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1650 -QLQHEAAALKKQ---QEDAERAREEAEKELEKWRQKANEALRlRLQAE-----EEAHKKSLAQedAEKQKEEAErEAKK 1720
Cdd:PRK11281 195 vLLQAEQALLNAQndlQRKSLEGNTQLQDLLQKQRDYLTARIQ-RLEHQlqllqEAINSKRLTL--SEKTVQEAQ-SQDE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1721 RAKAEDSALKQKEMAENELERQRKVAESTAQQKLTaeQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAA----QQQR- 1795
Cdd:PRK11281 271 AARIQANPLVAQELEINLQLSQRLLKATEKLNTLT--QQNLRVKNWLDRLTQSERNIKEQISVLKGSLLLSrilyQQQQa 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 1796 -------KQLEDELAKVRSEM-------DVLIQLKS------KAEKETMSNSERsKQLLEVEATKmRDLAEEASK 1850
Cdd:PRK11281 349 lpsadliEGLADRIADLRLEQfeinqqrDALFQPDAyidkleAGHKSEVTDEVR-DALLQLLDER-RELLDQLNK 421
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
71-148 |
9.83e-05 |
|
first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409070 Cd Length: 106 Bit Score: 44.57 E-value: 9.83e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 71 KKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRErDVVRSVRLPRekgrmrfHKLQNVQIALDFL 148
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVP-EVAQSEEGQK-------QKLAVVLACVNFL 72
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1611-1831 |
9.85e-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: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1611 AHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQK--ANEALR 1688
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1689 LRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMA---------ENELERQRKVAESTAQQKLTAEQE 1759
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaparREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222982 1760 LIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSK 1831
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1385-1563 |
1.00e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1385 SQRRLEDEEKAAEKLKAEEQKkmammqaELDKQKQLAEVHAKaiakaeKEAQELKLRMQEEVNRREDavvdaekqkhniq 1464
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKK-------EAEAIKKEALLEAK------EEIHKLRNEFEKELRERRN------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1465 lelhELKNLsEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRaaEAEKLRKAA---QEEA 1541
Cdd:PRK12704 83 ----ELQKL-EKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE--QLQELERISgltAEEA 155
|
170 180
....*....|....*....|....*...
gi 1927222982 1542 -EKLRKQVNEETQKKRMA-----EEELK 1563
Cdd:PRK12704 156 kEILLEKVEEEARHEAAVlikeiEEEAK 183
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2085-2211 |
1.05e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 48.86 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2085 QQAAQKCSAAEQQVQSVLAQQKedtiMQTKLKEEYEKAKKLAKQAEA----------AKEKAEREAALLRQQAE-EAERQ 2153
Cdd:PTZ00491 666 AAARHQAELLEQEARGRLERQK----MHDKAKAEEQRTKLLELQAESaavessgqsrAEALAEAEARLIEAEAEvEQAEL 741
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 2154 KAAaeqeaanqakaqedAERLRKEAEFEaAKRAQAENAALKQKQQADAEMAKHKKLAE 2211
Cdd:PTZ00491 742 RAK--------------ALRIEAEAELE-KLRKRQELELEYEQAQNELEIAKAKELAD 784
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1828-2066 |
1.05e-04 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 48.60 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1828 ERSKQLLEVEATKM----RDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDAtrlKTEAEIALKE 1903
Cdd:COG1193 503 ERARELLGEESIDVekliEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKA---REEAEEILRE 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1904 KEAENERLRRQAEdeayQRKALEDQANQHKQQIEEkivlLKKSSEAEMERQRAIVDDTLKQRRVVE-EEIRILKLNfeka 1982
Cdd:COG1193 580 ARKEAEELIRELR----EAQAEEEELKEARKKLEE----LKQELEEKLEKPKKKAKPAKPPEELKVgDRVRVLSLG---- 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1983 SSGKLdleLELNKLKNIaeETQQSKLRAEEEAEKLRKLAleeekrrREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKK 2062
Cdd:COG1193 648 QKGEV---LEIPKGGEA--EVQVGILKMTVKLSDLEKVE-------KKKPKKPKKRPAGVSVSVSKASTVSPELDLRGMR 715
|
....
gi 1927222982 2063 AEEA 2066
Cdd:COG1193 716 VEEA 719
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2060-2340 |
1.09e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.58 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2060 KKKAEEARKQKDDADKEAEKQILMAQQAA----QKCSAAEQQVQSVLAQQKE-----DTIMQTKLKEEYEKAKKLAKQAE 2130
Cdd:pfam17380 306 EEKAREVERRRKLEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEErkrelERIRQEEIAMEISRMRELERLQM 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2131 AAKEKAER-----EAALlRQQAEEAERQKAAAEQ-----------EAANqakaQEDAERLRKEAEFEAAKRAQAEnaaLK 2194
Cdd:pfam17380 386 ERQQKNERvrqelEAAR-KVKILEEERQRKIQQQkvemeqiraeqEEAR----QREVRRLEEERAREMERVRLEE---QE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2195 QKQQAdaemakhkklaeQTLKQKfqvEQELTKVKLKLDEtDKQKSVLDEELQRLKDEVDDAVKQRGQVEEElLKVKVQME 2274
Cdd:pfam17380 458 RQQQV------------ERLRQQ---EEERKRKKLELEK-EKRDRKRAEEQRRKILEKELEERKQAMIEEE-RKRKLLEK 520
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222982 2275 ELLKLKLRIEEENQRLIKKDKDNTQKFLAKE---ADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQ 2340
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERRKQQEMEERrriQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1511-1783 |
1.09e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.92 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1511 KQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVneetQKKRMAEEelkrkaeaekeaakqkqkaledlenlKRQA 1590
Cdd:TIGR02794 58 QKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELE----QRAAAEKA--------------------------AKQA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1591 EEAerqvKQAEIEKERQiqvAHVAAQKSAAaelqskhmsfvEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERARE 1670
Cdd:TIGR02794 108 EQA----AKQAEEKQKQ---AEEAKAKQAA-----------EAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1671 EAEKELEKWRQKANEALRlRLQAEEEAHKKSLAQEDAE---KQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAE 1747
Cdd:TIGR02794 170 EAKKKAEAEAKAKAEAEA-KAKAEEAKAKAEAAKAKAAaeaAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEK 248
|
250 260 270
....*....|....*....|....*....|....*.
gi 1927222982 1748 STAQQKLTAEQELIRLRADFDNAEQQRsLLEDELYR 1783
Cdd:TIGR02794 249 QGGARGAAAGSEVDKYAAIIQQAIQQN-LYDDPSFR 283
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2120-2217 |
1.10e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 45.54 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2120 EKAKKLAKQAEAAkEKAEREAALLRQQAEEAERQkaaaeqeaanqakAQEDAERLRKEAEFEAAK-----RAQAENAALK 2194
Cdd:PRK05759 35 ERQKKIADGLAAA-ERAKKELELAQAKYEAQLAE-------------ARAEAAEIIEQAKKRAAQiieeaKAEAEAEAAR 100
|
90 100
....*....|....*....|...
gi 1927222982 2195 QKQQADAEMAKHKKLAEQTLKQK 2217
Cdd:PRK05759 101 IKAQAQAEIEQERKRAREELRKQ 123
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2373-2601 |
1.11e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2373 DLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASr 2452
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2453 lhetelATQEKMTVVEKLEVarLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQnkskemadAQQKQIEHEKTVLQQtfl 2532
Cdd:COG3883 94 ------ALYRSGGSVSYLDV--LLGSESFSDFLDRLSALSKIADADADLLEELK--------ADKAELEAKKAELEA--- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222982 2533 sEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKE 2601
Cdd:COG3883 155 -KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1762-2015 |
1.21e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1762 RLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLedelakvrsemdvliqlksKAEKETMSNSERSKQLLEveatKM 1841
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEF-------------------RQKNGLVDLSEEAKLLLQ----QL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1842 RDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIAlkekeaeneRLRRQAEDEAYQ 1921
Cdd:COG3206 222 SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELA---------ELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1922 RKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTlkQRRVVEEEIRILKLNfekassgklDLELELNKLK---N 1998
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASL--QAQLAQLEARLAELP---------ELEAELRRLErevE 361
|
250
....*....|....*..
gi 1927222982 1999 IAEETQQSKLRAEEEAE 2015
Cdd:COG3206 362 VARELYESLLQRLEEAR 378
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2283-2481 |
1.24e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2283 IEEENQRLIKKDKdntqkflaKEADNMKKLAEdaarlsVEAQEAA-RLRQIAEDDLNQQRALADKMLKekmQAIQEASRL 2361
Cdd:PRK12704 36 AEEEAKRILEEAK--------KEAEAIKKEAL------LEAKEEIhKLRNEFEKELRERRNELQKLEK---RLLQKEENL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2362 RAEAEMLQRQKDLAQEQAQKLLEdkqlMQQRLDEETEEYQKsLEAERKRQLEIIaeseklklqvSQLSEAQAKAQ--EEA 2439
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQ----KQQELEKKEEELEE-LIEEQLQELERI----------SGLTAEEAKEIllEKV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1927222982 2440 KKfKKQADsIASRLHETElatqekmtvveklEVARLTSSKEA 2481
Cdd:PRK12704 164 EE-EARHE-AAVLIKEIE-------------EEAKEEADKKA 190
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2054-2275 |
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 1927222982 2054 DELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEdtiMQTKLKEEYEKAKKLAKQAEAAK 2133
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA---LEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2134 EKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAER-LRKEAEFEAAKRAQAEnaALKQKQQadaEMAKHKKLAEQ 2212
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRrLQYLKYLAPARREQAE--ELRADLA---ELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927222982 2213 TLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEE 2275
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1390-1625 |
1.26e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1390 EDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKaIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHE 1469
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1470 LKNLSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLEttvKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVN 1549
Cdd:COG3883 109 LGSESFSDFLDRLSALSKIADADADLLEELKADKAELE---AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222982 1550 EETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQS 1625
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGS 261
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2095-2293 |
1.37e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.28 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2095 EQQVQSVLAQQKEdtimqtkLKEEYEKAKKLAKQAEAAKEKAEREAALLrQQAEEAERQkaaaeqeaanqaKAQEDAERL 2174
Cdd:PRK00409 519 NELIASLEELERE-------LEQKAEEAEALLKEAEKLKEELEEKKEKL-QEEEDKLLE------------EAEKEAQQA 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2175 RKEAEFEAAK-------RAQAENAALKQKQQADA--EMAKHKKLAEQTLKQKFQVEQELT---KVKLKldeTDKQKSVLD 2242
Cdd:PRK00409 579 IKEAKKEADEiikelrqLQKGGYASVKAHELIEArkRLNKANEKKEKKKKKQKEKQEELKvgdEVKYL---SLGQKGEVL 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1927222982 2243 EELQrlKDEVddavkqrgQVEEELLKVKVQMEELLKLKLRIEEENQRLIKK 2293
Cdd:PRK00409 656 SIPD--DKEA--------IVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTV 696
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2182-2396 |
1.41e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2182 AAKRAQAENAA---LKQKQQADAEMAKhkklAEQTLkQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQ 2258
Cdd:COG3206 167 ELRREEARKALeflEEQLPELRKELEE----AEAAL-EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2259 RGQVEEELLKVKVQMEELL------KLKLRIEEENQRLIKKDKDNT------QKFLAKEADNMKKLAEDAARLSVEAQEA 2326
Cdd:COG3206 242 LAALRAQLGSGPDALPELLqspviqQLRAQLAELEAELAELSARYTpnhpdvIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2327 ARLRQIAEDDLNQQraladkmLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLedKQLMQQRLDEE 2396
Cdd:COG3206 322 LEALQAREASLQAQ-------LAQLEARLAELPELEAELRRLEREVEVARELYESLL--QRLEEARLAEA 382
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2055-2386 |
1.46e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2055 ELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKE 2134
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2135 KAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTL 2214
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2215 KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKD 2294
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2295 KDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDL 2374
Cdd:COG4372 279 EIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
330
....*....|..
gi 1927222982 2375 AQEQAQKLLEDK 2386
Cdd:COG4372 359 LSKGAEAGVADG 370
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1140-2020 |
1.84e-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: 48.12 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1140 IRNTQgAEGVLKQYEDCLREVHTVpnDVKEVETYRT--KLKKMRAEAEGEQPVFDSLEAELKKA-----TAVSDKMSRVH 1212
Cdd:TIGR01612 801 IDNIK-DEDAKQNYDKSKEYIKTI--SIKEDEIFKIinEMKFMKDDFLNKVDKFINFENNCKEKidsehEQFAELTNKIK 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1213 SE-RDAELDHYRQLLSSLQDRWKAVFSQIDLRQRELEQLGRQLGYYR------ESydwlirwINDAKQRQEKIQAVTITD 1285
Cdd:TIGR01612 878 AEiSDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKicentkES-------IEKFHNKQNILKEILNKN 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1286 SKTLKEQLAQEKKLLEEVEGN-KDKVDECQKYAKAYidTIKDYEL---QLVAYKAQV-EPLASPLKKT------KLDSAS 1354
Cdd:TIGR01612 951 IDTIKESNLIEKSYKDKFDNTlIDKINELDKAFKDA--SLNDYEAknnELIKYFNDLkANLGKNKENMlyhqfdEKEKAT 1028
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1355 DNIIQEYVTLRTKYSELMTLTSQYIKFITDsqrRLEDE-EKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHakaiaKAEK 1433
Cdd:TIGR01612 1029 NDIEQKIEDANKNIPNIEIAIHTSIYNIID---EIEKEiGKNIELLNKEILEEAEINITNFNEIKEKLKHY-----NFDD 1100
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1434 EAQELKLRMQEEVNRREDAVVDAEKQ-KHNIQlELHELKNLSEQQIMDKSKQVDD--ALQSRVKIEEEIRLIRLQLE--- 1507
Cdd:TIGR01612 1101 FGKEENIKYADEINKIKDDIKNLDQKiDHHIK-ALEEIKKKSENYIDEIKAQINDleDVADKAISNDDPEEIEKKIEniv 1179
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1508 TTVKQKSTAESELKQLRDRAAEAEKlRKAAQEEAEKLRKQVNEETQKkrMAEEELKRKAEAEKEAAKQKQKALEDLENLK 1587
Cdd:TIGR01612 1180 TKIDKKKNIYDEIKKLLNEIAEIEK-DKTSLEEVKGINLSYGKNLGK--LFLEKIDEEKKKSEHMIKAMEAYIEDLDEIK 1256
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1588 RQAEEAERQVkQAEIEKERQIQVAHVAAQKSAAAELQSKHMSfvEKTSKL-EESLKQEHGavLQLQHEAAALKKQQEDAE 1666
Cdd:TIGR01612 1257 EKSPEIENEM-GIEMDIKAEMETFNISHDDDKDHHIISKKHD--ENISDIrEKSLKIIED--FSEESDINDIKKELQKNL 1331
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1667 RAREEAEKELEKWRQK-ANEALRLRLQaeeeaHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAEN-ELERQRK 1744
Cdd:TIGR01612 1332 LDAQKHNSDINLYLNEiANIYNILKLN-----KIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDiNLEECKS 1406
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1745 VAESTAQ--------QKLTAEQELI-----RLRADFDNAEQQRsllEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDV 1811
Cdd:TIGR01612 1407 KIESTLDdkdideciKKIKELKNHIlseesNIDTYFKNADENN---ENVLLLFKNIEMADNKSQHILKIKKDNATNDHDF 1483
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1812 LI-QLKSKAEKETMSNSERSKQLLEVEATKM------RDLAEEASKLRAIAEEAKhqrqvaeeeAARQRAEAERILKEkl 1884
Cdd:TIGR01612 1484 NInELKEHIDKSKGCKDEADKNAKAIEKNKElfeqykKDVTELLNKYSALAIKNK---------FAKTKKDSEIIIKE-- 1552
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1885 aaISDA-TRLKTEAEIA-LKEKEAENERLRrqAEDEAyqrkALEDQANQHKQQIEEKIVLLkKSSEAEMERQRAIVDDTL 1962
Cdd:TIGR01612 1553 --IKDAhKKFILEAEKSeQKIKEIKKEKFR--IEDDA----AKNDKSNKAAIDIQLSLENF-ENKFLKISDIKKKINDCL 1623
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927222982 1963 KQRRVVEEEIRILKLN-----FEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKL 2020
Cdd:TIGR01612 1624 KETESIEKKISSFSIDsqdteLKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKI 1686
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2057-2205 |
1.91e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.56 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2057 DRLKKKAEEARKQkDDADKEAEKQILMAQQAAQKcsAAEQQVQSVLAQQkedtimQTKLKEEyEKAKKLAKQAEAAKEKA 2136
Cdd:COG2268 245 ELAKKKAEERREA-ETARAEAEAAYEIAEANAER--EVQRQLEIAERER------EIELQEK-EAEREEAELEADVRKPA 314
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222982 2137 EREAALLRQQAE-EAERQKAaaeqeaanqaKAQEDAERLRKEAE-FEAAKRAQAENAALKQKQQADAEMAK 2205
Cdd:COG2268 315 EAEKQAAEAEAEaEAEAIRA----------KGLAEAEGKRALAEaWNKLGDAAILLMLIEKLPEIAEAAAK 375
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2467-2634 |
1.93e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2467 VEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKskeMADAQQKQIEHEKTVLQQTFLSEKEMLLkkeklie 2546
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---IKKYEEQLGNVRNNKEYEALQKEIESLK------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2547 eekkRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAalnKQKEAEKEMHNKQKEMKELERKRLEQERILAEE 2626
Cdd:COG1579 103 ----RRISDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
....*...
gi 1927222982 2627 NQKLREKL 2634
Cdd:COG1579 176 LLALYERI 183
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1843-2079 |
1.94e-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: 47.07 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1843 DLAEEASKLRAIAEEAKHQRQvAEEEAARQRAEAERILKEKLAAISDATRL--KTEAEIALKEKEAE--NERLRRQAEDE 1918
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEK-ELAALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAelEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1919 AYQRKALEDQ--ANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRvveEEIRILKLNFEKASSGKLDLELELNKL 1996
Cdd:COG4942 100 EAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR---EQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1997 KNIAEETQQSKLRAEEEAEKLRKLAleeekrrREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKE 2076
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLL-------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 1927222982 2077 AEK 2079
Cdd:COG4942 250 ALK 252
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1846-2198 |
1.95e-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: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1846 EEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAL 1925
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1926 EDQANQHKQQI---EEKIVLLKKSS---EAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNI 1999
Cdd:pfam07888 121 LAQRAAHEARIrelEEDIKTLTQRVlerETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2000 AEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAqdelDRLKKKAEEARKQKDDADKEAEK 2079
Cdd:pfam07888 201 LAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV----EGLGEELSSMAAQRDRTQAELHQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2080 QILMAQQAAQKCSAAEQQVQSVLAQ-QKEDTIMQTKLKEEYEKAKKLAKQAEAAKEkaereaallRQQAEEAERQKAAAE 2158
Cdd:pfam07888 277 ARLQAAQLTLQLADASLALREGRARwAQERETLQQSAEADKDRIEKLSAELQRLEE---------RLQEERMEREKLEVE 347
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1927222982 2159 QEAANQAKAQEDAERLRKEAEFEAAKR-AQAENAALKQKQQ 2198
Cdd:pfam07888 348 LGREKDCNRVQLSESRRELQELKASLRvAQKEKEQLQAEKQ 388
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1384-1621 |
1.98e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1384 DSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELklrmQEEVNRREDAVVDAEKQ-KHN 1462
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREElGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1463 IQLELHELKNLSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAE 1542
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222982 1543 KLRKQVNEETQKKRMAEEELKRkaeaekeaakqkqkALEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAA 1621
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAA--------------AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2326-2521 |
2.00e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2326 AARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLE 2405
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2406 AERKRQ-----LEIIAESEKLK------LQVSQLSEAQAK-------AQEEAKKFKKQADSIASRLHETELATQEKmtvV 2467
Cdd:COG3883 94 ALYRSGgsvsyLDVLLGSESFSdfldrlSALSKIADADADlleelkaDKAELEAKKAELEAKLAELEALKAELEAA---K 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1927222982 2468 EKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIE 2521
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1757-1940 |
2.02e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1757 EQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKetmsnserskQLLEV 1836
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE----------QLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1837 EATKMrdlaeeaskLRAIAEEakhqrqvaEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAE 1916
Cdd:COG1579 86 RNNKE---------YEALQKE--------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|....
gi 1927222982 1917 DEAYQRKALEDQANQHKQQIEEKI 1940
Cdd:COG1579 149 EELAELEAELEELEAEREELAAKI 172
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2479-2639 |
2.02e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2479 KEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEmADAQQKQIEHEKTVLQQtflsekemllkkeklieeEKKRLESQFEE 2558
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELED-LEKEIKRLELEIEEVEA------------------RIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2559 eVKKAKALK------DEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLRE 2632
Cdd:COG1579 85 -VRNNKEYEalqkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*..
gi 1927222982 2633 KLQQLEE 2639
Cdd:COG1579 164 EREELAA 170
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1677-1890 |
2.08e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1677 EKWRQKANEALRLRLQAEEEAH--------KKSLAQEDAEKQKEEAEREAKKRAK-AEDSALKQKEMAENELERQRKVAE 1747
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQKQAAEqerlkqleKERLAAQEQKKQAEEAAKQAALKQKqAEEAAAKAAAAAKAKAEAEAKRAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1748 STAQQkltAEQElirlradfdnaeqqrslledelyrlKNEVVAAQQQRKQLEDELAKVRSEMdvliqlKSKAEKEtmsns 1827
Cdd:PRK09510 158 AAAKK---AAAE-------------------------AKKKAEAEAAKKAAAEAKKKAEAEA------AAKAAAE----- 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927222982 1828 erSKQLLEVEATKMrdlAEEASKLRAIAEEAKhqrqVAEEEAARQRAEAERILKEKLAAISDA 1890
Cdd:PRK09510 199 --AKKKAEAEAKKK---AAAEAKKKAAAEAKA----AAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2553-2648 |
2.20e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2553 ESQFEEEVKKAKALKDEQERQKQQMEDEKKkLQATmDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLRE 2632
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEAL-LEAK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEK 107
|
90
....*....|....*.
gi 1927222982 2633 KLQQLEEAQKDQPDKE 2648
Cdd:PRK12704 108 REEELEKKEKELEQKQ 123
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1210-2020 |
2.27e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1210 RVHSERdaELDHYRQLLSSLQDRWKAVFSQIDLRqRELEQLGRQLGY----YRESYDWLIRwINDAKQRQEKIQAVtITD 1285
Cdd:PRK04863 282 RVHLEE--ALELRRELYTSRRQLAAEQYRLVEMA-RELAELNEAESDleqdYQAASDHLNL-VQTALRQQEKIERY-QAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1286 SKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDyelQLVAYKaqveplasplkkTKLDSASDNIIQ--EYVT 1363
Cdd:PRK04863 357 LEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKS---QLADYQ------------QALDVQQTRAIQyqQAVQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1364 LRTKYSELMTLTSQYIKFITDSQRRLEDEEKAA-EKLKAEEQKkMAMMQAELDKQKQLAEVHAKAIA-----KAEKEAQE 1437
Cdd:PRK04863 422 ALERAKQLCGLPDLTADNAEDWLEEFQAKEQEAtEELLSLEQK-LSVAQAAHSQFEQAYQLVRKIAGevsrsEAWDVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1438 LKLRMQEEVNRREdavvdaekQKHNIQLELHELKNLSEQQ----------IMDKSKQVDDALQ-SRVKIEEEIRLIRL-- 1504
Cdd:PRK04863 501 LLRRLREQRHLAE--------QLQQLRMRLSELEQRLRQQqraerllaefCKRLGKNLDDEDElEQLQEELEARLESLse 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1505 QLETTVKQKSTAESELKQLRDRAAEAEKLR---KAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKqkalE 1581
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARIQRLAARApawLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVER----D 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1582 DLENLKRQAEEAERQVKQAE-IEKERQIQVA-----------------HVAAQKSAAAElQSKHMSFVEKTSKLEESLKQ 1643
Cdd:PRK04863 649 ELAARKQALDEEIERLSQPGgSEDPRLNALAerfggvllseiyddvslEDAPYFSALYG-PARHAIVVPDLSDAAEQLAG 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1644 EHGA---VLQLQHEAAALKkqqedaerAREEAEKELEK----------WR-----------QKANEALRLRLQAEEEAHK 1699
Cdd:PRK04863 728 LEDCpedLYLIEGDPDSFD--------DSVFSVEELEKavvvkiadrqWRysrfpevplfgRAAREKRIEQLRAEREELA 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1700 KSLAQEDAEKQKEEAEREAKKR--------AKAED--SALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDN 1769
Cdd:PRK04863 800 ERYATLSFDVQKLQRLHQAFSRfigshlavAFEADpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNR 879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1770 AEQQRSLLEDElyRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQlkskaeketmsnserskqlLEVEATKMRDLAEEAS 1849
Cdd:PRK04863 880 LLPRLNLLADE--TLADRVEEIREQLDEAEEAKRFVQQHGNALAQ-------------------LEPIVSVLQSDPEQFE 938
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1850 KLRAIAEEAKHQRQvaeeeAARQRAEAeriLKEklaAISDATRLKTEAEIALKEKEAE-NERLRRQAEDEAYQRKALEDQ 1928
Cdd:PRK04863 939 QLKQDYQQAQQTQR-----DAKQQAFA---LTE---VVQRRAHFSYEDAAEMLAKNSDlNEKLRQRLEQAEQERTRAREQ 1007
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1929 ANQHKQQIEEKI-VLLKKSSEAEMERQraivddtlkQRRVVEEEIRILKLNF-----EKASSGKLDLELEL--NKLKNIA 2000
Cdd:PRK04863 1008 LRQAQAQLAQYNqVLASLKSSYDAKRQ---------MLQELKQELQDLGVPAdsgaeERARARRDELHARLsaNRSRRNQ 1078
|
890 900
....*....|....*....|..
gi 1927222982 2001 EETQQSKLRAEEEA--EKLRKL 2020
Cdd:PRK04863 1079 LEKQLTFCEAEMDNltKKLRKL 1100
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2168-2646 |
2.45e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.51 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2168 QEDAERLRKEAEFEAakRAQAENAALKQKqqaDAEMAKHKklaeQTLKQKFQVEQELTKVKL---KLDETDKQKSVLDEE 2244
Cdd:pfam10174 178 EEDWERTRRIAEAEM--QLGHLEVLLDQK---EKENIHLR----EELHRRNQLQPDPAKTKAlqtVIEMKDTKISSLERN 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2245 LQRLKDEVD----DAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDntqkflakeadnMKKLaedaarls 2320
Cdd:pfam10174 249 IRDLEDEVQmlktNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESE------------LLAL-------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2321 veaqeaarlrQIAEDDLNQQRALADK---MLKEKMQAI-QEASRLRAEAEMLQrqkdLAQEQAQKLLEDKQLMQQRLDEE 2396
Cdd:pfam10174 309 ----------QTKLETLTNQNSDCKQhieVLKESLTAKeQRAAILQTEVDALR----LRLEEKESFLNKKTKQLQDLTEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2397 teeyqKSLEAERKRQLEIIAESEKLKLQVsqLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVArlT 2476
Cdd:pfam10174 375 -----KSTLAGEIRDLKDMLDVKERKINV--LQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEA--L 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2477 SSKEaddlrKAIADLEKEKSRLKKE-AEDLQNKSKEMADAQQK--QIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLE 2553
Cdd:pfam10174 446 SEKE-----RIIERLKEQREREDRErLEELESLKKENKDLKEKvsALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2554 S-QFEEEVKKAKALKDEQERQK-QQME------------------------DEKKKLQATMDAALNKQKEAEKEMHNKQK 2607
Cdd:pfam10174 521 SlEIAVEQKKEECSKLENQLKKaHNAEeavrtnpeindrirlleqevarykEESGKAQAEVERLLGILREVENEKNDKDK 600
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1927222982 2608 EMKELERKRLEQ--------ERILAEENQKLREKLQQLEEAQKDQPD 2646
Cdd:pfam10174 601 KIAELESLTLRQmkeqnkkvANIKHGQQEMKKKGAQLLEEARRREDN 647
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
2102-2410 |
2.48e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.45 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2102 LAQQKEDtiMQTKLKEEYEKakklaKQAEAAKEKA--EREAALLRQQAEEAERQKAAAEQEAAnqaKAQEDAERLRKEAE 2179
Cdd:pfam00038 23 LEQQNKL--LETKISELRQK-----KGAEPSRLYSlyEKEIEDLRRQLDTLTVERARLQLELD---NLRLAAEDFRQKYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2180 FEAAKRAQAENAALKQKQQADAEMAkhkklaeqtlkQKFQVEqelTKVKLKLDETDKQKSVLDEELQRLKD--------- 2250
Cdd:pfam00038 93 DELNLRTSAENDLVGLRKDLDEATL-----------ARVDLE---AKIESLKEELAFLKKNHEEEVRELQAqvsdtqvnv 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2251 EVDDAVKQ---------RGQVEEELLKVKVQMEELLKLKLrieEENQRLIKKDKDNTQKflAKEadNMKKLAEDAARLSV 2321
Cdd:pfam00038 159 EMDAARKLdltsalaeiRAQYEEIAAKNREEAEEWYQSKL---EELQQAAARNGDALRS--AKE--EITELRRTIQSLEI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2322 E-----AQEAARLRQIAEddLNQQRALADKMLKEKMQAIQEAsrlraeaemLQRQKdlaQEQAQKLLEDKQLM--QQRLD 2394
Cdd:pfam00038 232 ElqslkKQKASLERQLAE--TEERYELQLADYQELISELEAE---------LQETR---QEMARQLREYQELLnvKLALD 297
|
330
....*....|....*.
gi 1927222982 2395 EETEEYQKSLEAERKR 2410
Cdd:pfam00038 298 IEIATYRKLLEGEECR 313
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
186-299 |
2.51e-04 |
|
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: 43.64 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 186 DIQINGQSEDMTAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLV-DMGRVYRQTNLENLEQAFGVA 264
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQ---NKLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|....*
gi 1927222982 265 ERDLGVTRLLDPEDVDVPHPDEKSIITYVSSLYDA 299
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2277-2451 |
2.64e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2277 LKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQ 2356
Cdd:PRK00409 497 LGLPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2357 EA-SRLRAEAEMLQRQKDLAQEQAQKLLEDKQL--MQQRLDEETEEYQKSLEAERKRQ--------------------LE 2413
Cdd:PRK00409 577 QAiKEAKKEADEIIKELRQLQKGGYASVKAHELieARKRLNKANEKKEKKKKKQKEKQeelkvgdevkylslgqkgevLS 656
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1927222982 2414 IIAESE--------KLKLQVSQLSEAQAKAQEEAKKFKKQADSIAS 2451
Cdd:PRK00409 657 IPDDKEaivqagimKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRT 702
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2495-2642 |
2.70e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2495 KSRLKKEAEDLQNKSKEMADAQQKQIEHEKtvlQQTFLSEKEmllkkeklieeEKKRLESQFEEEVKKAKALKDEQERQK 2574
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIK---KEALLEAKE-----------EIHKLRNEFEKELRERRNELQKLEKRL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2575 QQMEDEKKKLQATMDaalNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLrEKLQQL--EEAQK 2642
Cdd:PRK12704 92 LQKEENLDRKLELLE---KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLtaEEAKE 157
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1683-2019 |
2.73e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 47.21 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1683 ANEALRLRLQAEEEAH-KKSLAQEDAEKQKEEAEREA----KKRAKAEDSALKQKEMAENELERQRkvaESTAQQKLTAE 1757
Cdd:pfam15964 333 AYEQVKQAVQMTEEANfEKTKALIQCEQLKSELERQKerleKELASQQEKRAQEKEALRKEMKKER---EELGATMLALS 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1758 QELIRLRADFDNAEQQRSlledelyRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQL----KSKAEKETMSNSERSKQL 1833
Cdd:pfam15964 410 QNVAQLEAQVEKVTREKN-------SLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQtkmkKDEAEKEHREYRTKTGRQ 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1834 LEVEatkmrdlAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERIlkeklaaisdaTRLKTEAEIALKEKEAENERLRR 1913
Cdd:pfam15964 483 LEIK-------DQEIEKLGLELSESKQRLEQAQQDAARAREECLKL-----------TELLGESEHQLHLTRLEKESIQQ 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1914 QAEDEAyqrKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASsgkldlelel 1993
Cdd:pfam15964 545 SFSNEA---KAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEIT---------- 611
|
330 340
....*....|....*....|....*.
gi 1927222982 1994 NKLKNIAEETQQSKLRAEEEAEKLRK 2019
Cdd:pfam15964 612 QKSRSEVEQLSQEKEYLQDRLEKLQK 637
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1387-1496 |
2.85e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1387 RRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHA-KAIAKAEKEAQELKLRMQEEvnRREDAVVDAEKQKHNIQL 1465
Cdd:PRK00409 537 EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAqQAIKEAKKEADEIIKELRQL--QKGGYASVKAHELIEARK 614
|
90 100 110
....*....|....*....|....*....|...
gi 1927222982 1466 ELHElKNLSEQQIMDKSKQVDDALQS--RVKIE 1496
Cdd:PRK00409 615 RLNK-ANEKKEKKKKKQKEKQEELKVgdEVKYL 646
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3423-3456 |
3.07e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.07e-04
10 20 30
....*....|....*....|....*....|....
gi 1927222982 3423 LLEAQAATGFMVDPVKKQCLSVDEAVKSGLVGPE 3456
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2334-2642 |
3.13e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2334 EDDLNQQRALADKMLKEKMQAIQEasrLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSleaeRKRQLE 2413
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDE---LNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL----KEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2414 IIAESEKLKLQVSQLSEAQAKAQ---EEAKKFKKQADSIASRLHETELATQEKMTVVEKLEV--ARLTSSKEADDLRKAI 2488
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNkagGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKEleKELEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2489 ADLEKEKSRLKKEAEDLQNKSKEMADAQQKqiehektvlqqtflsekemllkkeklieeekkrLESQFEEEVKKAKALKD 2568
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQE---------------------------------LHEEMIELYKEADELRK 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1927222982 2569 EQERQKQQMEDEKKKLqatmDAALNKQKEAEKEMHNKQKEMKELERKRLEQERilAEENQKLREKLQQLEEAQK 2642
Cdd:COG1340 210 EADELHKEIVEAQEKA----DELHEEIIELQKELRELRKELKKLRKKQRALKR--EKEKEELEEKAEEIFEKLK 277
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3129-3165 |
3.23e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.23e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1927222982 3129 KLLSAERAVTGYKDPYTGKTVSLFQAMKKDLIPKEQG 3165
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1210-1625 |
3.24e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.25 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1210 RVHSERDAELDhyRQLLSSLQDRWKAVFSQIDLRqRELEQLGRQLGY----YRESYDWLIRWINdAKQRQEKIQAVTiTD 1285
Cdd:COG3096 281 RELSERALELR--RELFGARRQLAEEQYRLVEMA-RELEELSARESDleqdYQAASDHLNLVQT-ALRQQEKIERYQ-ED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1286 SKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDyelQLVAYKaqveplasplkkTKLDSASDNIIQEYVTLR 1365
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKS---QLADYQ------------QALDVQQTRAIQYQQAVQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1366 T--KYSELMTLTSQYIKFITDSQRRLEDEEKAA-EKLKAEEQKkMAMMQA---ELDKQKQLAEVHAKAIAKAE--KEAQE 1437
Cdd:COG3096 421 AleKARALCGLPDLTPENAEDYLAAFRAKEQQAtEEVLELEQK-LSVADAarrQFEKAYELVCKIAGEVERSQawQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1438 LKLRMQEEVNRREdavvdaekQKHNIQLELHELKNLSEQQ------IMDKSKQVDDALQSRVKIEE-----EIRLIRL-- 1504
Cdd:COG3096 500 LLRRYRSQQALAQ--------RLQQLRAQLAELEQRLRQQqnaerlLEEFCQRIGQQLDAAEELEEllaelEAQLEELee 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1505 QLETTVKQKSTAESELKQLRDRAAEAEKLRKA---AQEEAEKLRKQVNEETQKKRMAEEELKRKaeaekeaakqkqkale 1581
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKELAARAPAwlaAQDALERLREQSGEALADSQEVTAAMQQL---------------- 635
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1927222982 1582 dLENLkRQAEEAERQVKQAEIEKERQIQVAHvAAQKSAAAELQS 1625
Cdd:COG3096 636 -LERE-REATVERDELAARKQALESQIERLS-QPGGAEDPRLLA 676
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1417-1608 |
3.37e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1417 QKQLAEVHAKaIAKAEKEAQELKLR-----MQEEVNRREDAVVDAEKQKHNIQLELHELKNLSEQ---QIMDKSKQVDDA 1488
Cdd:COG3206 181 EEQLPELRKE-LEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAlraQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1489 LQSRVKIEEEIRLIRLQLE-TTVKQKSTAES-ELKQLRdraAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKA 1566
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAElAELSARYTPNHpDVIALR---AQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQL 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1927222982 1567 EAEKEAAKQKQKALEDLENLKRQAEEAER-------QVKQAEIEKERQI 1608
Cdd:COG3206 337 AQLEARLAELPELEAELRRLEREVEVARElyesllqRLEEARLAEALTV 385
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
70-189 |
3.39e-04 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 43.81 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 70 QKKTFTKWVN---------KHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPrERDVVRsvrlpreKGRMRFHKLQN 140
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTID-ERAINK-------KKLTVFTIHEN 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1927222982 141 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQI 189
Cdd:cd21292 97 LTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1514-1756 |
3.53e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 46.51 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1514 STAESELKQLRDRAAEAEKLRkAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEaekeaakqkqkalEDLENLKRQAEEA 1593
Cdd:PRK07735 1 MDPEKDLEDLKKEAARRAKEE-ARKRLVAKHGAEISKLEEENREKEKALPKNDD-------------MTIEEAKRRAAAA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1594 ERqVKQAEIEKERQIQVAHV------AAQKSAAAELQSKHMSFVEKT------SKLEESLKQEHGAVLQLQHEAAALKKQ 1661
Cdd:PRK07735 67 AK-AKAAALAKQKREGTEEVteeekaKAKAKAAAAAKAKAAALAKQKregteeVTEEEKAAAKAKAAAAAKAKAAALAKQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1662 QEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSL-AQEDAEKQKEEAEREAKKR----AKAEDSAL-KQKEM- 1734
Cdd:PRK07735 146 KREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAeAGEGTEEVTEEEKAKAKAKaaaaAKAKAAALaKQKASq 225
|
250 260
....*....|....*....|....*.
gi 1927222982 1735 ----AENELERQRKVAESTAQQKLTA 1756
Cdd:PRK07735 226 gngdSGDEDAKAKAIAAAKAKAAAAA 251
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2303-2521 |
3.57e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2303 AKEADNMKKLAEDAArlsvEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKL 2382
Cdd:TIGR02794 64 KKEQERQKKLEQQAE----EAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2383 LEDKQLmqqrldeetEEYQKSLEAERKRQLEiiAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQE 2462
Cdd:TIGR02794 140 AERKAK---------EEAAKQAEEEAKAKAA--AEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAE 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222982 2463 kmtvveklevarltSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIE 2521
Cdd:TIGR02794 209 --------------AAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGAR 253
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2082-2525 |
3.61e-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: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2082 LMAQQAAQKCSAAEQQVQSvlaqqKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKaeREAALLRQQAEE-AERQKAAAEQE 2160
Cdd:pfam05667 208 LLERNAAELAAAQEWEEEW-----NSQGLASRLTPEEYRKRKRTKLLKRIAEQL--RSAALAGTEATSgASRSAQDLAEL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2161 AANQAKAQEDAERLRKEAEFEAAKRAQAENAAlkqkqQADAEMAKHKKLAEQTLKQkfQVEQELtkvklkldetdkqksv 2240
Cdd:pfam05667 281 LSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEA-----PAATSSPPTKVETEEELQQ--QREEEL---------------- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2241 ldEELQRLKDEVDDAVKqrgQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKF-LAKEAD-NMKKLAEDaar 2318
Cdd:pfam05667 338 --EELQEQLEDLESSIQ---ELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLdLLPDAEeNIAKLQAL--- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2319 lsVEAQeAARLRQIAED-------DLNQQRALADKMLKEKMqaiqEASRLRAEAEMLQRQ-KDLAQEQAQKLLEDKQLMQ 2390
Cdd:pfam05667 410 --VDAS-AQRLVELAGQwekhrvpLIEEYRALKEAKSNKED----ESQRKLEEIKELREKiKEVAEEAKQKEELYKQLVA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2391 Q--RLDEETeeyqkSLEAERKRQLEIIAESEKLKlqvsqlsEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMtvve 2468
Cdd:pfam05667 483 EyeRLPKDV-----SRSAYTRRILEIVKNIKKQK-------EEITKILSDTKSLQKEINSLTGKLDRTFTVTDELV---- 546
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2469 klevarLTSSKEADDLRKA---IADLEKEKSRLKKEAEDLQNKSKEMADAQQkQIEHEKT 2525
Cdd:pfam05667 547 ------FKDAKKDESVRKAykyLAALHENCEQLIQTVEETGTIMREIRDLEE-QIETESG 599
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2112-2216 |
3.63e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 43.58 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2112 QTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEaerqkaaaeqeaaNQAKAQEDAERLRKEAefeaakRAQAENA 2191
Cdd:cd06503 32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQE-------------IIEEARKEAEKIKEEI------LAEAKEE 92
|
90 100
....*....|....*....|....*
gi 1927222982 2192 ALKQKQQADAEMAKHKKLAEQTLKQ 2216
Cdd:cd06503 93 AERILEQAKAEIEQEKEKALAELRK 117
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2356-2615 |
3.75e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.86 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2356 QEASRLRAeaemlQRQKDLAQEQAQKLLEDKQlmqQRLDEEteeyqkslEAERKRQLEIIAESEKLKLQvsqlsEAQAKA 2435
Cdd:PRK05035 433 QAKAEIRA-----IEQEKKKAEEAKARFEARQ---ARLERE--------KAAREARHKKAAEARAAKDK-----DAVAAA 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2436 QEEAKKFKKQADSIASRLHE-----TELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSK 2510
Cdd:PRK05035 492 LARVKAKKAAATQPIVIKAGarpdnSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEA 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2511 EMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDE---KKKLQAT 2587
Cdd:PRK05035 572 EEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVdprKAAVAAA 651
|
250 260
....*....|....*....|....*...
gi 1927222982 2588 MDAAlnKQKEAEKEMHNKQKEMKELERK 2615
Cdd:PRK05035 652 IARA--KARKAAQQQANAEPEEAEDPKK 677
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2114-2268 |
3.89e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2114 KLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAeRQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAAL 2193
Cdd:COG1579 35 ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-EARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 2194 KQKQQADAEMAKHKKLAEqtlkqkfQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKqrgQVEEELLK 2268
Cdd:COG1579 114 ELMERIEELEEELAELEA-------ELAELEAELEEKKAELDEELAELEAELEELEAEREELAA---KIPPELLA 178
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1441-1626 |
3.99e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1441 RMQEEVNRREDAVVDAEKQKHNIQLELHELKNLSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQlettvkQKSTAESEL 1520
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALK------QKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1521 KQLRDRAAEAEKLRKAAQEEAeklrKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQA 1600
Cdd:PRK09510 140 KAAAAAKAKAEAEAKRAAAAA----KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEA 215
|
170 180
....*....|....*....|....*...
gi 1927222982 1601 E--IEKERQIQVAHVAAQKSAAAELQSK 1626
Cdd:PRK09510 216 KkkAAAEAKAAAAKAAAEAKAAAEKAAA 243
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
2324-2534 |
4.42e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2324 QEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEY-QK 2402
Cdd:pfam17045 56 KEIGLLRQQLEELEKGKQELVAKYEQQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFrQK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2403 SLEAERKRQLeiiaesekLKLQVSQLsEAQAKAQEEakkfkkQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEA- 2481
Cdd:pfam17045 136 SLEWEQQRLQ--------YQQQVASL-EAQRKALAE------QSSLIQSAAYQVQLEGRKQCLEASQSEIQRLRSKLERa 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1927222982 2482 -----------DDLRKAIADLEKEKSRLKKEAEDLQNKSKeMADAQQKQIEHEKTVLQQTFLSE 2534
Cdd:pfam17045 201 qdslcaqelelERLRMRVSELGDSNRKLLEEQQRLLEELR-MSQRQLQVLQNELMELKATLQSQ 263
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2062-2293 |
4.80e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.68 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2062 KAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQsvlAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAA 2141
Cdd:pfam13868 111 QEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE---EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2142 LLRQQAEEAERQKAAAEQEAANqaKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKqkfqvE 2221
Cdd:pfam13868 188 RLRAQQEKAQDEKAERDELRAK--LYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAERE-----E 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2222 QELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQ---------RGQVEEELLKVKVQMEELLKLKLRIEEENQRLIK 2292
Cdd:pfam13868 261 EEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKqieereeqrAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
.
gi 1927222982 2293 K 2293
Cdd:pfam13868 341 E 341
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3994-4028 |
5.07e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.07e-04
10 20 30
....*....|....*....|....*....|....*
gi 1927222982 3994 LLEAQAATGYVIDPIKNLKLTVSEAVRMGIVGPEF 4028
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2804-2834 |
5.22e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.22e-04
10 20 30
....*....|....*....|....*....|.
gi 1927222982 2804 LSAERAVVGYKDPYTGGKISVFEAMKKGLIE 2834
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2181-2326 |
5.95e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 45.76 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2181 EAAKRAQAENAALKQKQQADAEMAKHKKLAEQTL-KQKFQVEQELTKVKLKLDETDKQKSVLDEELQR-LKDEVDDAVKQ 2258
Cdd:pfam05262 210 EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNAdKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAEnQKREIEKAQIE 289
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 2259 RGQVEEELLKVKVQMEELLKLKLRieEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEA 2326
Cdd:pfam05262 290 IKKNDEEALKAKDHKAFDLKQESK--ASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2524-2638 |
5.95e-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: 45.36 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2524 KTVLQQtFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQE------RQKQQMEDEKKKLQATMDAALNKQKE 2597
Cdd:pfam02841 175 EEVLQE-FLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQEllrekqKEEEQMMEAQERSYQEHVKQLIEKME 253
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1927222982 2598 AEKEMHNKQKEMKeLERKRLEQERILAE----ENQKLREKLQQLE 2638
Cdd:pfam02841 254 AEREQLLAEQERM-LEHKLQEQEELLKEgfktEAESLQKEIQDLK 297
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2110-2328 |
6.18e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2110 IMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALlrqqaeeaerqkaaaeqeaanqaKAQEDAERLRKEAEFEAAKRaqae 2189
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALL-----------------------EAKEEIHKLRNEFEKELRER---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2190 NAALKQKqqadaemakhkklaEQTLKQKfqvEQELTKvklKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEellKV 2269
Cdd:PRK12704 81 RNELQKL--------------EKRLLQK---EENLDR---KLELLEKREEELEKKEKELEQKQQELEKKEEELEE---LI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2270 KVQMEELLKL-KLRIEEENQRLIKKDKDNTQkflaKEADNMKKLAEDAARLsvEAQEAAR 2328
Cdd:PRK12704 138 EEQLQELERIsGLTAEEAKEILLEKVEEEAR----HEAAVLIKEIEEEAKE--EADKKAK 191
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2317-2644 |
6.57e-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: 45.66 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2317 ARLSVEAQEAARLRQIAE--DDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQR-L 2393
Cdd:pfam07888 67 DREQWERQRRELESRVAElkEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRvL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2394 DEETE-----EYQKSLEAERKRQlEIIAESEKLKLQVSQL-SEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVV 2467
Cdd:pfam07888 147 ERETElermkERAKKAGAQRKEE-EAERKQLQAKLQQTEEeLRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2468 EKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDL-QNKSKEMADAQQKQIEHEKTVLQqtfLSEKEMLLKkeklie 2546
Cdd:pfam07888 226 HRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMaAQRDRTQAELHQARLQAAQLTLQ---LADASLALR------ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2547 eekkrlesqfEEEVKKAKalkdEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEE 2626
Cdd:pfam07888 297 ----------EGRARWAQ----ERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSES 362
|
330
....*....|....*...
gi 1927222982 2627 NQKLREKLQQLEEAQKDQ 2644
Cdd:pfam07888 363 RRELQELKASLRVAQKEK 380
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2339-2648 |
6.59e-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: 46.16 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2339 QQRALADKMLKEKMQAIQEASRL--RAEAEMLQRQK---DLAQEQAQK---LLEDKQLMQQRLDEETEEYQKSLEAERKR 2410
Cdd:NF033838 85 QNVALNKKLSDIKTEYLYELNVLkeKSEAELTSKTKkelDAAFEQFKKdtlEPGKKVAEATKKVEEAEKKAKDQKEEDRR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2411 Q--------LEI-IAESEkLKLQVSQLSEAQAKAQE----------EAKKFKKQADsiASRLHETElatQEKMTVVEKLE 2471
Cdd:NF033838 165 NyptntyktLELeIAESD-VEVKKAELELVKEEAKEprdeekikqaKAKVESKKAE--ATRLEKIK---TDREKAEEEAK 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2472 VARLTSSKEADDLRKAIADLEKEKSRLKKEA---EDLQNKSKEMADAQQKQIeHEKTVLQQTFLSEKEMLLKkeklieee 2548
Cdd:NF033838 239 RRADAKLKEAVEKNVATSEQDKPKRRAKRGVlgePATPDKKENDAKSSDSSV-GEETLPSPSLKPEKKVAEA-------- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2549 kkrlESQFEEEVKKAKALKDEQER-------------------QKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEM 2609
Cdd:NF033838 310 ----EKKVEEAKKKAKDQKEEDRRnyptntyktleleiaesdvKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEA 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1927222982 2610 KELE-----RKRLEQE--RILAEENQKLREKLQQLEEAQKDQPDKE 2648
Cdd:NF033838 386 TRLEkiktdRKKAEEEakRKAAEEDKVKEKPAEQPQPAPAPQPEKP 431
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1415-1635 |
6.71e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1415 DKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELknlsEQQIMDKSKQVDDAlqsRVK 1494
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEER---REE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1495 IEEEIRLIRLQ------LETTVKQKSTAE-----SELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELK 1563
Cdd:COG3883 88 LGERARALYRSggsvsyLDVLLGSESFSDfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222982 1564 RKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTS 1635
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1647-1878 |
7.16e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1647 AVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAED 1726
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1727 SALKQKEMAENELERQRKVAESTAQQK-----------LTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQR 1795
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1796 KQLEDELAKVRSEMDVLIQLKSKAEKEtmsnSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAE 1875
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKL----LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 1927222982 1876 AER 1878
Cdd:COG4942 250 ALK 252
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1681-1973 |
7.23e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.22 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1681 QKANEALRLRLQAEEEAHKkslaQEDAEKQKEEAEREAKKRAKAEDSALKQKEmaenelerQRKVAESTAQQkltaeqel 1760
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKK----EQERQKKLEQQAEEAEKQRAAEQARQKELE--------QRAAAEKAAKQ-------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1761 irlradfdnAEQQRSlledelyrlknevvAAQQQRKQLEDELAKVRSEmdvliqLKSKAEKEtmsnseRSKQLLEVEATK 1840
Cdd:TIGR02794 107 ---------AEQAAK--------------QAEEKQKQAEEAKAKQAAE------AKAKAEAE------AERKAKEEAAKQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1841 mrdlAEEASKLRAIAE---EAKHQRQVAEEEaARQRAEAERILK-EKLAAISDATRLKTEAEIALKEKEAENERLRRQAE 1916
Cdd:TIGR02794 152 ----AEEEAKAKAAAEakkKAEEAKKKAEAE-AKAKAEAEAKAKaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAE 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222982 1917 DEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIR 1973
Cdd:TIGR02794 227 RKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQNLYDDPSFR 283
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1524-1752 |
7.35e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.63 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1524 RDRAAEAEKLRKAAQEEAEKLrKQVNEETQKKRMAEEELKRKAEAEKEAAKQkqkalEDLENLKRQAEEaERQVKQAEIE 1603
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERE-TEIAIAQANREAEEAELEQEREIETARIAE-----AEAELAKKKAEE-RREAETARAE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1604 KERQIQVAHVAAQKSAAAELqskhmsfvektskleESLKQEHGAVLQlqhEAAALKKQQEdaerareeaekeLEKWRQKA 1683
Cdd:COG2268 264 AEAAYEIAEANAEREVQRQL---------------EIAEREREIELQ---EKEAEREEAE------------LEADVRKP 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1684 NEALRLRLQAEEEAHKkslaqeDAEKQKEEAEREAkKRAKAE-DSALKQKEMAENELERQRKVAESTAQQ 1752
Cdd:COG2268 314 AEAEKQAAEAEAEAEA------EAIRAKGLAEAEG-KRALAEaWNKLGDAAILLMLIEKLPEIAEAAAKP 376
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1695-2151 |
7.59e-04 |
|
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: 45.89 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1695 EEAHKKSLAQED----AEKQKEEAE----------REAKKRAKAEDSALKQKEMAE--------------NELERQRKVA 1746
Cdd:pfam05557 44 DRESDRNQELQKrirlLEKREAEAEealreqaelnRLKKKYLEALNKKLNEKESQLadarevisclknelSELRRQIQRA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1747 ESTAQQKLTAEQELIR----LRADFDNAEQQRSLLEDELYRLKnevvAAQQQRKQLEDELAKvrSEMDVLIQLKSKAEKE 1822
Cdd:pfam05557 124 ELELQSTNSELEELQErldlLKAKASEAEQLRQNLEKQQSSLA----EAEQRIKELEFEIQS--QEQDSEIVKNSKSELA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1823 TMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAK---HQRQVAEEEAARQRAEAERILKE-----KLAAISDATRLK 1894
Cdd:pfam05557 198 RIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKrklEREEKYREEAATLELEKEKLEQElqswvKLAQDTGLNLRS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1895 TEA-----------EIALKEkeaENERLRRQAEDEAYQRKALEDQANQHKQQIEEkivlLKKsseaEMERQRAIVDDTLK 1963
Cdd:pfam05557 278 PEDlsrrieqlqqrEIVLKE---ENSSLTSSARQLEKARRELEQELAQYLKKIED----LNK----KLKRHKALVRRLQR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1964 QRRVVEEEIRILK---------LNFEKASSGKLDLELELNKL------KNIAEETQQSKLRAEEEAEKLRKLALEEEKRR 2028
Cdd:pfam05557 347 RVLLLTKERDGYRailesydkeLTMSNYSPQLLERIEEAEDMtqkmqaHNEEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2029 REAEEKVKKIAAAEEEAARQRQaaqdELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKED 2108
Cdd:pfam05557 427 LRQQESLADPSYSKEEVDSLRR----KLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQR 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1927222982 2109 TIMQTKLKEEYEKAKKLAKQAEAAKEK-----------AEREAALLRQQAEEAE 2151
Cdd:pfam05557 503 KNQLEKLQAEIERLKRLLKKLEDDLEQvlrlpettstmNFKEVLDLRKELESAE 556
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1903-2214 |
8.01e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1903 EKEAENERLRRQAEDEAYQRKALE------DQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLK-----QRRVVEEE 1971
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEpsgqvtESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKreerrQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1972 IRiLKLNFEKASSGKLDLELELNKL-----KNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAA 2046
Cdd:pfam02029 84 ER-QKEFDPTIADEKESVAERKENNeeeenSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2047 RQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQ--AAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKA-- 2122
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRghPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAev 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2123 -----KKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQK- 2196
Cdd:pfam02029 243 fleaeQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEi 322
|
330
....*....|....*....
gi 1927222982 2197 QQADAEMA-KHKKLAEQTL 2214
Cdd:pfam02029 323 ERRRAEAAeKRQKLPEDSS 341
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1680-1981 |
8.21e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1680 RQKANEAlRLRLQAEEEAHKKSLAQEDAEKQKEEAER----EAKKRAKAEDSALKQkEMAENELERQRKVAESTAQQK-- 1753
Cdd:pfam02029 12 RRRAREE-RRRQKEEEEPSGQVTESVEPNEHNSYEEDselkPSGQGGLDEEEAFLD-RTAKREERRQKRLQEALERQKef 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1754 ---LTAEQELIRLRADfDNAEQQRSLLEDELYRlknevvaaqQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERS 1830
Cdd:pfam02029 90 dptIADEKESVAERKE-NNEEEENSSWEKEEKR---------DSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1831 KQL-LEVEATKMRDLAEEASKLRAIAEEAK---------HQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEI- 1899
Cdd:pfam02029 160 EDKsEEAEEVPTENFAKEEVKDEKIKKEKKvkyeskvflDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEe 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1900 --ALKEKEAENERLRRQ---AEDEAYQRKaledqaNQHKQQIEEKIVLLKKSSEaemERQRAIVDDtlKQRRVVEEEIRI 1974
Cdd:pfam02029 240 aeVFLEAEQKLEELRRRrqeKESEEFEKL------RQKQQEAELELEELKKKRE---ERRKLLEEE--EQRRKQEEAERK 308
|
....*..
gi 1927222982 1975 LKLNFEK 1981
Cdd:pfam02029 309 LREEEEK 315
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2210-2427 |
8.69e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.21 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2210 AEQTLKQKFQVEQELTKVKLKLDETDKQKsvldEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKL---KLRIEEE 2286
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDASK----QRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEilaSLSLEEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2287 NQRLIKKDKD--NTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQ-EASRLRA 2363
Cdd:pfam12795 84 EQRLLQTSAQlqELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaELAALKA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 2364 EAEMLQRQ---KDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLE-IIAESEKLKLQVSQ 2427
Cdd:pfam12795 164 QIDMLEQEllsNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQEAEqAVAQTEQLAEEAAG 231
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2424-2614 |
8.83e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2424 QVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKE-KSRLKKEA 2502
Cdd:PRK09510 63 QYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQaEEAAAKAA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2503 EDLQNKSKE---MADAQQKQIEHEKTVlqqtflseKEMLLKKEKLIEEEKKRLEsqfEEEVKKAKAL---KDEQERQKQQ 2576
Cdd:PRK09510 143 AAAKAKAEAeakRAAAAAKKAAAEAKK--------KAEAEAAKKAAAEAKKKAE---AEAAAKAAAEakkKAEAEAKKKA 211
|
170 180 190
....*....|....*....|....*....|....*...
gi 1927222982 2577 MEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELER 2614
Cdd:PRK09510 212 AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEK 249
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2221-2629 |
8.94e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2221 EQELTKVKLKLDETDKQKSVLDEELQRLKDEVDdaVKQRgqvEEELLKVKVQ-MEELLKLKLRIEEENQRLIK---KDKD 2296
Cdd:pfam10174 358 ESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLD--VKER---KINVLQKKIEnLQEQLRDKDKQLAGLKERVKslqTDSS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2297 NTQKFLA--KEADNMKKLAEDAARLSVEAQEAARLRQIaeDDLNQQralaDKMLKEKMQAIQE--ASRLRAEAEMLQRQK 2372
Cdd:pfam10174 433 NTDTALTtlEEALSEKERIIERLKEQREREDRERLEEL--ESLKKE----NKDLKEKVSALQPelTEKESSLIDLKEHAS 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2373 DLAQEQAQKLLEDKQL---MQQRLDEETE---EYQKSLEAERKRQLeiiaeSEKLKLQVSQLSEAQAKAQEEAKKFKKQA 2446
Cdd:pfam10174 507 SLASSGLKKDSKLKSLeiaVEQKKEECSKlenQLKKAHNAEEAVRT-----NPEINDRIRLLEQEVARYKEESGKAQAEV 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2447 DSIASRLHETElatqekmtvveklevarltssKEADDLRKAIADLEKEKSRLKKEaedlqnKSKEMADAQQKQIEHEKTV 2526
Cdd:pfam10174 582 ERLLGILREVE---------------------NEKNDKDKKIAELESLTLRQMKE------QNKKVANIKHGQQEMKKKG 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2527 LQqtflsekEMLLKKEKLIEEEKKRLESQFEEevkkakaLKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQ 2606
Cdd:pfam10174 635 AQ-------LLEEARRREDNLADNSQQLQLEE-------LMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERR 700
|
410 420
....*....|....*....|....
gi 1927222982 2607 KEMKE-LERKrleQERILAEENQK 2629
Cdd:pfam10174 701 KQLEEiLEMK---QEALLAAISEK 721
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1690-1880 |
8.99e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1690 RLQAEEEAHKKSL-AQEDAEKQKEEAEREAKKRakaedsalkqkemaENELERQrkvaESTAQQKltaEQELirlradfd 1768
Cdd:PRK12704 48 KKEAEAIKKEALLeAKEEIHKLRNEFEKELRER--------------RNELQKL----EKRLLQK---EENL-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1769 naEQQRSLLEDElyrlKNEVVAAQQQRKQLEDELAKVRSEMDVLIQlKSKAEKETMSN--SERSKQLL--EVEAtKMRdl 1844
Cdd:PRK12704 99 --DRKLELLEKR----EEELEKKEKELEQKQQELEKKEEELEELIE-EQLQELERISGltAEEAKEILleKVEE-EAR-- 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 1927222982 1845 AEEASKLRAIAEEAKhqrqvaeEEAARqraEAERIL 1880
Cdd:PRK12704 169 HEAAVLIKEIEEEAK-------EEADK---KAKEIL 194
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1465-1823 |
9.10e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.33 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1465 LELHELKNLSEQQIMDKSKQVDdalqSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAE------------- 1531
Cdd:COG5185 184 LTLGLLKGISELKKAEPSGTVN----SIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEdlaqtsdkleklv 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1532 ----KLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQ 1607
Cdd:COG5185 260 eqntDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQ 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1608 IQVAHVAAQKSAAAELQSKHMSFVEKTSKLEEslkqehgaVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEAL 1687
Cdd:COG5185 340 NLTAEIEQGQESLTENLEAIKEEIENIVGEVE--------LSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1688 rlrlqaeeEAHKKSlaqedAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELI--RLRA 1765
Cdd:COG5185 412 --------EDTLKA-----ADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEInrSVRS 478
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 1766 DFDNAEQQRSLLEDELYRLKNEVvaaQQQRKQLEDELAKVRSEMDVLIQLKSKAEKET 1823
Cdd:COG5185 479 KKEDLNEELTQIESRVSTLKATL---EKLRAKLERQLEGVRSKLDQVAESLKDFMRAR 533
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2124-2337 |
9.30e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2124 KLAKQAEAAKEKAEREAALLRQQAEEAERQKAaaeqeaanqaKAQEDAERLRKEAEFEAAKRAQAENAA-LKQKQQADAE 2202
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQA----------AEQERLKQLEKERLAAQEQKKQAEEAAkQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2203 MAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQksvlDEELQRLKDEVDDAVKQrgqveEELLKVKVQMEELLKLKLR 2282
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKK----AEAEAAKKAAAEAKKKA-----EAEAAAKAAAEAKKKAEAE 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222982 2283 IEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAE-DDL 2337
Cdd:PRK09510 207 AKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEvDDL 262
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
50-176 |
9.73e-04 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 45.32 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 50 EVLDPAERAVIRIADERDRVQKKTFTKWVNKHLIKSQrqVTDLYEDLRDGhnlISLLEVLSGETLPRERDVVRSVRLPRE 129
Cdd:COG5069 360 EPLEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSPE--ITNLFGDLRDQ---LILLQALSKKLMPMTVTHKLVKKQPAS 434
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1927222982 130 KGRM-RFHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNpKLTLGLIW 176
Cdd:COG5069 435 GIEEnRFKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVW 481
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2008-2413 |
9.96e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2008 LRAEEEAEKLRKLALEEEKRRREAEEKVKKiaaaeeeaarqrqaaqdELDRLKKKAEEArkqkdDADKEAEKQILMAQQA 2087
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTSRRQLAA-----------------EQYRLVEMAREL-----AELNEAESDLEQDYQA 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2088 AqkcSAAEQQVQSVLAQQKEDTIMQTKLKeeyEKAKKLAKQAEAAKEKAEreaallrqQAEEAERQKAAaeqeaanqakA 2167
Cdd:PRK04863 333 A---SDHLNLVQTALRQQEKIERYQADLE---ELEERLEEQNEVVEEADE--------QQEENEARAEA----------A 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2168 QEDAERLRKE-AEFEAA-----KRA----QAENAALKQKQQ---ADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDET 2234
Cdd:PRK04863 389 EEEVDELKSQlADYQQAldvqqTRAiqyqQAVQALERAKQLcglPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVA 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2235 DKQKSVLDEELQ---RLKDEVD--DAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKkdKDNTQKFLAKEADNM 2309
Cdd:PRK04863 469 QAAHSQFEQAYQlvrKIAGEVSrsEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQ--QQRAERLLAEFCKRL 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2310 KKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEA-EMLQRQKDLAQ--EQAQKLLEDK 2386
Cdd:PRK04863 547 GKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARApAWLAAQDALARlrEQSGEEFEDS 626
|
410 420 430
....*....|....*....|....*....|..
gi 1927222982 2387 Q----LMQQRLDEETE-EYQKSLEAERKRQLE 2413
Cdd:PRK04863 627 QdvteYMQQLLERERElTVERDELAARKQALD 658
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
2195-2628 |
1.09e-03 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 45.24 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2195 QKQQADAEMAKHKKLAEQTLKQKF------QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLK 2268
Cdd:pfam09730 8 KKVAADGESREESLLQESASKEAYyaqrilELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRDEIKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2269 VKVQMEELLKLKLRIEEENQRLIKKD---KDNTQKFLAKEADnMKKLAEDAARLSVEAQEAARLRQIAEddlnqqralad 2345
Cdd:pfam09730 88 YKVREARLLQDYSELEEENISLQKQVsvlKQNQVEFEGLKHE-ITRKEEETELLNSQLEEAIRLREIAE----------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2346 KMLKEKMQAIQEASRLRAEAemlqrQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESE----KL 2421
Cdd:pfam09730 156 RQLDEALETLKTEREQKNSL-----RKELSHYMTLNDFDYVSHLSISLDGLKFSEDEGAGTEPNNDGEAMDGGEngggGL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2422 KLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETEL---------ATQEKMTVVEKLEvarlTSSKEADDLRKAIADLE 2492
Cdd:pfam09730 231 KNSGLDNRTSTPRKSEVFPPAPSLVSDLLSELNISEIqklkqqliqVEREKVSLLSTLQ----ESQKQLEQAKGALSEQQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2493 KEKSRLKKEAEDLQN----KSKEMADAQQKQ-IEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFeeevkkaKALK 2567
Cdd:pfam09730 307 EKVNRLTENLEAMRGlqasKERQDALDSEKDrDSHEDGDYYEVDINGPEILECKYRVAVEEAGELREEL-------KALK 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222982 2568 DEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELErKRLEQERILAEENQ 2628
Cdd:pfam09730 380 ARYNTLEERYKEEKTRWEAEAQDLAEKIRQLEKASHQDQERIAHLE-KELGKTRKVAGESE 439
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2235-2451 |
1.10e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2235 DKQKSVLDEELQRLKDEvddavkqRGQVEEELLKVKVQMEELLKLklrieeENQRLIKKDKDNTQKFLAKEADNMKKLAE 2314
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKE-------QQQAEELQQKQAAEQERLKQL------EKERLAAQEQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2315 DAARlsvEAQEAARLRqiAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMlqrQKDLAQEQAQKLledkqlmqqrld 2394
Cdd:PRK09510 136 EAAA---KAAAAAKAK--AEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEA---KKKAEAEAAAKA------------ 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222982 2395 eeTEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIAS 2451
Cdd:PRK09510 196 --AAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKA 250
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1636-1923 |
1.10e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 44.64 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1636 KLEESLKQEHGAVLQLQHEAAALKKQQEDaerareeaekeLEKWRQKANEALRLRLQAEEEAHKKSLAQEdaekQKEEAE 1715
Cdd:pfam15558 19 EEQRMRELQQQAALAWEELRRRDQKRQET-----------LERERRLLLQQSQEQWQAEKEQRKARLGRE----ERRRAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1716 REAKKRAKAEDSALKQKEMAEN----ELERQRKVAESTAQ---QKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEV 1788
Cdd:pfam15558 84 RREKQVIEKESRWREQAEDQENqrqeKLERARQEAEQRKQcqeQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKER 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1789 vaAQQQRKQLEDELAKVRSE-MDVLIQLKSKAEKETMSNS---------ERSKQLLEVEATKMRDLA--EEASKLRA--I 1854
Cdd:pfam15558 164 --EEQKKVQENNLSELLNHQaRKVLVDCQAKAEELLRRLSleqslqrsqENYEQLVEERHRELREKAqkEEEQFQRAkwR 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222982 1855 AEEAKHQRQ------VAEEEAARQRAE--AERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRK 1923
Cdd:pfam15558 242 AEEKEEERQehkealAELADRKIQQARqvAHKTVQDKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKK 318
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2130-2573 |
1.10e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 45.28 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2130 EAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAER---LRKEAEFEAAKRAQAENAALKQKQQADAEMAKH 2206
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQviaLRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2207 KKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEE 2286
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2287 NQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAE 2366
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2367 MLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQA 2446
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2447 DSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTV 2526
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1927222982 2527 LQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQ 2573
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASA 528
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2275-2439 |
1.12e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.99 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2275 ELLKLKLRIEEENQRLIKKDKDNTQKfLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQA 2354
Cdd:pfam05262 199 DMTDLKERESQEDAKRAQQLKEELDK-KQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2355 IQeasrlRAEAEMLQRQKDLAQEQAQKLLEDK--QLMQQRLDEETEEYQKSLEAERKRqLEIIAESEKLKLQVsqlsEAQ 2432
Cdd:pfam05262 278 NQ-----KREIEKAQIEIKKNDEEALKAKDHKafDLKQESKASEKEAEDKELEAQKKR-EPVAEDLQKTKPQV----EAQ 347
|
....*..
gi 1927222982 2433 AKAQEEA 2439
Cdd:pfam05262 348 PTSLNED 354
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1703-1887 |
1.12e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 44.20 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1703 AQEDAEKQKEEAEREAKKRAKAEDS-ALKQKEMAENELERQR---------KVAESTAQQKLTAEQELIRLRADFDNAEQ 1772
Cdd:pfam12037 1 GGPGSDKDPKKSNDKPRTAYSGFDPeALERAAKAARELESSPhakkalelmKKQEQTRQAELQAKIKEYEAAQEQLKIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1773 QRsLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAE-----------KETMSNSERSKQLLEVEA--- 1838
Cdd:pfam12037 81 QR-VEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEEllrkqeesvakQEAMRIQAQRRQTEEHEAelr 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1927222982 1839 --TKMRDLAEEAsklRAIAEEAKHQRQVAEEEaARQRAEAERilKEKLAAI 1887
Cdd:pfam12037 160 reTERAKAEAEA---EARAKEERENEDLNLEQ-LREKANEER--ETVLESI 204
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2349-2601 |
1.14e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.32 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2349 KEKMQAiqEASRLRAEAemlqRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEaeRKRQLEIIAESEKLKLQVSQL 2428
Cdd:PRK05035 443 QEKKKA--EEAKARFEA----RQARLEREKAAREARHKKAAEARAAKDKDAVAAALA--RVKAKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2429 SEAQAKAQEEAKKFKKQADsiASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNK 2508
Cdd:PRK05035 515 DNSAVIAAREARKAQARAR--QAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAK 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2509 SKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEE--------EVKKAKALKDEQER---QKQQM 2577
Cdd:PRK05035 593 KAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDprkaavaaAIARAKARKAAQQQanaEPEEA 672
|
250 260
....*....|....*....|....*.
gi 1927222982 2578 EDEKKklqATMDAALN--KQKEAEKE 2601
Cdd:PRK05035 673 EDPKK---AAVAAAIAraKAKKAAQQ 695
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2326-2644 |
1.16e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2326 AARLRQIAEDDLNQQRALADK--MLKEKMQAIQEASRL---RAEAEMLQ-RQKDLAQEQaQKLLEDKQLMQQ--RLDEET 2397
Cdd:COG3096 271 ADYMRHANERRELSERALELRreLFGARRQLAEEQYRLvemARELEELSaRESDLEQDY-QAASDHLNLVQTalRQQEKI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2398 EEYQKSLEAERKRqLEIIAEseklklQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTvveklevarlts 2477
Cdd:COG3096 350 ERYQEDLEELTER-LEEQEE------VVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQT------------ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2478 skEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMA--DAQQKQIEHEKTVLQQTfLSEKEMLLkkeklieeekkrleSQ 2555
Cdd:COG3096 411 --RAIQYQQAVQALEKARALCGLPDLTPENAEDYLAafRAKEQQATEEVLELEQK-LSVADAAR--------------RQ 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2556 FEEEVKKAKALKDEQERQ------KQQMED--EKKKLQATMDAALNKQKEAEKEMHNKQKEMKELER--KRLEQ------ 2619
Cdd:COG3096 474 FEKAYELVCKIAGEVERSqawqtaRELLRRyrSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEfcQRIGQqldaae 553
|
330 340
....*....|....*....|....*..
gi 1927222982 2620 --ERILAEENQKLREKLQQLEEAQKDQ 2644
Cdd:COG3096 554 elEELLAELEAQLEELEEQAAEAVEQR 580
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1866-1965 |
1.20e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 41.91 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1866 EEEAARQRAEAERILKEKLAAISdatrlktEAEIALKEKEAENERLRRQAEDEAYQ-RKALEDQANQHKQQIEEkivllk 1944
Cdd:pfam00430 32 RELIADEIAEAEERRKDAAAALA-------EAEQQLKEARAEAQEIIENAKKRAEKlKEEIVAAAEAEAERIIE------ 98
|
90 100
....*....|....*....|.
gi 1927222982 1945 kSSEAEMERQRAIVDDTLKQR 1965
Cdd:pfam00430 99 -QAAAEIEQEKDRALAELRQQ 118
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2401-2521 |
1.20e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2401 QKSLEAERKRQlEIIAESEKLKLQVSQlsEAQAKAQEEAKKFKKQADSiASRLHETELATQEKmtvveKLEVARLTSSKE 2480
Cdd:PRK12704 31 AKIKEAEEEAK-RILEEAKKEAEAIKK--EALLEAKEEIHKLRNEFEK-ELRERRNELQKLEK-----RLLQKEENLDRK 101
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1927222982 2481 ADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIE 2521
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1073-1724 |
1.23e-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: 45.17 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1073 KVQVELEGLKKDLNKVSAK----TKEVLASPQQTASAPVLRSELdlTVEKMDHTHMLSSVYLEKLKTVEMVIRNTQGAEG 1148
Cdd:pfam01576 437 KLQSELESVSSLLNEAEGKniklSKDVSSLESQLQDTQELLQEE--TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRN 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1149 VLKQYEDCLREVHTVPNDVKE----VETYRTKLKKMRAEAEGEQPVFDSLEAELKKATAVSDKMSRVHSERDAELDHYRQ 1224
Cdd:pfam01576 515 VERQLSTLQAQLSDMKKKLEEdagtLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQ 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1225 LLSSLQDRWKAvFSQIDLRQRELEqlgrqlGYYRESYDWLirwinDAKQRQEKIQAVTITdsktlkeqlaqekKLLEEVE 1304
Cdd:pfam01576 595 LVSNLEKKQKK-FDQMLAEEKAIS------ARYAEERDRA-----EAEAREKETRALSLA-------------RALEEAL 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1305 GNKDKVDECQKYAKAYIDtikdyelQLVAYKAQVEPLASPLKKTKldSASDNIIQEyvtLRTKYSElmtltsqyikfitd 1384
Cdd:pfam01576 650 EAKEELERTNKQLRAEME-------DLVSSKDDVGKNVHELERSK--RALEQQVEE---MKTQLEE-------------- 703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1385 sqrrLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKA-EKEAQELKLRMQEEVNRREDAVvdAEKQKhnI 1463
Cdd:pfam01576 704 ----LEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQlVKQVRELEAELEDERKQRAQAV--AAKKK--L 775
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1464 QLELHELknlsEQQIMDKSKQVDDALQSRVKIE----------EEIRLIRLQLETTVKQKS----TAESELKQLRDRAAE 1529
Cdd:pfam01576 776 ELDLKEL----EAQIDAANKGREEAVKQLKKLQaqmkdlqrelEEARASRDEILAQSKESEkklkNLEAELLQLQEDLAA 851
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1530 AEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQ--AEIEKERq 1607
Cdd:pfam01576 852 SERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQltTELAAER- 930
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1608 iqvAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEH-GAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEA 1686
Cdd:pfam01576 931 ---STSQKSESARQQLERQNKELKAKLQEMEGTVKSKFkSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEV 1007
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1927222982 1687 LrlrLQAEEEAHKKSLAQEDAEK----------QKEEAEREAkKRAKA 1724
Cdd:pfam01576 1008 L---LQVEDERRHADQYKDQAEKgnsrmkqlkrQLEEAEEEA-SRANA 1051
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1474-1999 |
1.29e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1474 SEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLrKQVNEETQ 1553
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDL-SMELEKNN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1554 KKRMAEEELKRkaeAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAeiekERQIQVAHVAAQKsaAAELQSKHMSFVEK 1633
Cdd:PRK01156 274 YYKELEERHMK---IINDPVYKNRNYINDYFKYKNDIENKKQILSNI----DAEINKYHAIIKK--LSVLQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1634 TSKLEEslkqehgavlqLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEE 1713
Cdd:PRK01156 345 KSRYDD-----------LNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1714 AEREAKK-RAKAEDSALKQKEMAENELERQRKVAESTAQQKLT------AEQELIRLRADFDNaeqQRSLLEDELYRLKN 1786
Cdd:PRK01156 414 INVKLQDiSSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPvcgttlGEEKSNHIINHYNE---KKSRLEEKIREIEI 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1787 EVVAAQQQRKQLE--------DELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEE- 1857
Cdd:PRK01156 491 EVKDIDEKIVDLKkrkeylesEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSw 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1858 --AKHQRQVAEEEAARQRAEaerilkEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEA--YQRKALEDQANQ-H 1932
Cdd:PRK01156 571 lnALAVISLIDIETNRSRSN------EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEAnnLNNKYNEIQENKiL 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1933 KQQIEEKIVLLKKSSEAEMERQ--------------------RAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELE 1992
Cdd:PRK01156 645 IEKLRGKIDNYKKQIAEIDSIIpdlkeitsrindiednlkksRKALDDAKANRARLESTIEILRTRINELSDRINDINET 724
|
....*..
gi 1927222982 1993 LNKLKNI 1999
Cdd:PRK01156 725 LESMKKI 731
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2459-2643 |
1.32e-03 |
|
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: 44.90 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2459 ATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEml 2538
Cdd:pfam15964 333 AYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQ-- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2539 lkkeklieeEKKRLESQFEEEVKKAKALKDEQERQKQQM---EDEKKKLQATMDAALNKQK----EAEKEMHN-KQKEMK 2610
Cdd:pfam15964 411 ---------NVAQLEAQVEKVTREKNSLVSQLEEAQKQLasqEMDVTKVCGEMRYQLNQTKmkkdEAEKEHREyRTKTGR 481
|
170 180 190
....*....|....*....|....*....|...
gi 1927222982 2611 ELERKRLEQERILAEenqkLREKLQQLEEAQKD 2643
Cdd:pfam15964 482 QLEIKDQEIEKLGLE----LSESKQRLEQAQQD 510
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1492-1955 |
1.32e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.68 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1492 RVKIEE-EIRLIRLQLETTVKQKSTAESelKQLRDraaEAEKLRKAAqEEAEKLRKQVneETQKKRmaeeelkrkaeaek 1570
Cdd:pfam05622 86 RIKCEElEKEVLELQHRNEELTSLAEEA--QALKD---EMDILRESS-DKVKKLEATV--ETYKKK-------------- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1571 eaakqkqkaLEDLENLKRQ--------AEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLK 1642
Cdd:pfam05622 144 ---------LEDLGDLRRQvklleernAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1643 QEHGAVLQLQHEAAALKKQQEDAerareeaekelekwrQKANEALRLrlqAEEEAHKKSLAQEDAEKQKEEAEREAKKRA 1722
Cdd:pfam05622 215 KLEEKLEALQKEKERLIIERDTL---------------RETNEELRC---AQLQQAELSQADALLSPSSDPGDNLAAEIM 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1723 KAEdsaLKQK-EMAENELERQRKVAESTAQQKLTAEQELIrlradfDNAEQQRSLLEDELyRLKNE-VVAAQQQRKQLED 1800
Cdd:pfam05622 277 PAE---IREKlIRLQHENKMLRLGQEGSYRERLTELQQLL------EDANRRKNELETQN-RLANQrILELQQQVEELQK 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1801 ELAKVRSEMDVLIQLKSKAE----KETMSNSERSK---QLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQR 1873
Cdd:pfam05622 347 ALQEQGSKAEDSSLLKQKLEehleKLHEAQSELQKkkeQIEELEPKQDSNLAQKIDELQEALRKKDEDMKAMEERYKKYV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1874 AEAERILK-----EKLAAISDATRLKT-----EAEIALKEKEAENERLRRQAEDE----AYQRKALedqaNQHKQQIEEK 1939
Cdd:pfam05622 427 EKAKSVIKtldpkQNPASPPEIQALKNqllekDKKIEHLERDFEKSKLQREQEEKlivtAWYNMGM----ALHRKAIEER 502
|
490
....*....|....*.
gi 1927222982 1940 IVLLKKSSEAEMERQR 1955
Cdd:pfam05622 503 LAGLSSPGQSFLARQR 518
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1709-1939 |
1.35e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.21 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1709 KQKEEAEREAKKRAKAEDSALKQKEMAEN-----ELERQRKVAE-STAQQKLTAEQELirlrADFDNAEQQRSLLEDELY 1782
Cdd:NF012221 1541 SQQADAVSKHAKQDDAAQNALADKERAEAdrqrlEQEKQQQLAAiSGSQSQLESTDQN----ALETNGQAQRDAILEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1783 RLKNEVVAAQQQRKQLEDE-------------------LAKVRSEMDvliQLKSKAEKETmsnsERSKQLLEVEATKMRD 1843
Cdd:NF012221 1617 AVTKELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLD---DAKKISGKQL----ADAKQRHVDNQQKVKD 1689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1844 laeEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRK 1923
Cdd:NF012221 1690 ---AVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ 1766
|
250
....*....|....*.
gi 1927222982 1924 AledQANQHKQQIEEK 1939
Cdd:NF012221 1767 A---DAKGAKQDESDK 1779
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1268-1460 |
1.39e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1268 INDAKQRQEKIQAVTITDSKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLASPLKK 1347
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1348 TK---------LDSASdniIQEYVTLRTKYSELMTLTSQYIKFITDSQRRLEDEEKAAEKLKAE---EQKKMAMMQAELD 1415
Cdd:COG3883 98 SGgsvsyldvlLGSES---FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEleaLKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1927222982 1416 KQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQK 1460
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
219-296 |
1.41e-03 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 40.75 E-value: 1.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 219 DNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERdLGVTRLLDPEDVDVPHPDEKSIITYVSSL 296
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1856-2315 |
1.42e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.75 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1856 EEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERlrrQAEDEAYQRKALEDQAnqhKQQ 1935
Cdd:pfam09731 52 GEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEEK---EATKDAAEAKAQLPKS---EQE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1936 IEEKIVLLKKSSEAEMER-QRAIVDDTLKQRRVVEEEIRILKLNFEKAssgkldlelelnkLKNIAEETQQSKLRAEEEA 2014
Cdd:pfam09731 126 KEKALEEVLKEAISKAESaTAVAKEAKDDAIQAVKAHTDSLKEASDTA-------------EISREKATDSALQKAEALA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2015 EKLRKLAleeekrRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAA 2094
Cdd:pfam09731 193 EKLKEVI------NLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2095 EQQVQSVLaqqKEDTIMQT--------KLKEEYEKA-KKLAKQ--------AEAAKEKAEREAALLRQQAEEAERQKaaa 2157
Cdd:pfam09731 267 FPDIIPVL---KEDNLLSNddlnsliaHAHREIDQLsKKLAELkkreekhiERALEKQKEELDKLAEELSARLEEVR--- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2158 eqeaaNQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQElTKVklkLDETDKQ 2237
Cdd:pfam09731 341 -----AADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIK-EKV---EEERAGR 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 2238 KSVLDEELQRLKdEVDDAVKQRGQVEEELLKVKvqmeellKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAED 2315
Cdd:pfam09731 412 LLKLNELLANLK-GLEKATSSHSEVEDENRKAQ-------QLWLAVEALRSTLEDGSADSRPRPLVRELKALKELASD 481
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4308-4341 |
1.45e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.45e-03
10 20 30
....*....|....*....|....*....|....
gi 1927222982 4308 EETGPIAGILDIDTLEKVSITEAIHRNLVDNISG 4341
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2111-2456 |
1.46e-03 |
|
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: 44.90 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2111 MQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKaaaeqeaanqakaqedaERLRKEAEFEAAKRAQAEN 2190
Cdd:pfam15964 326 AQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQK-----------------ERLEKELASQQEKRAQEKE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2191 AALKqkqqadaEMAKHKKLAEQTLkqkFQVEQELTKVKLKLDETDKQKSVLDEELQrlkdevdDAVKQRGQVEEELLKVK 2270
Cdd:pfam15964 389 ALRK-------EMKKEREELGATM---LALSQNVAQLEAQVEKVTREKNSLVSQLE-------EAQKQLASQEMDVTKVC 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2271 VQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKK----LAEDAARLSVEAQEAARLRQ----IAEDDLNQQRA 2342
Cdd:pfam15964 452 GEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKlgleLSESKQRLEQAQQDAARAREeclkLTELLGESEHQ 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2343 LadKMLKEKMQAIQEASRLRAEAEMLQrqkdlAQEQAQKLLEDKQLMQQRLDE-ETEEY-----QKSLEAERKRQLEIIA 2416
Cdd:pfam15964 532 L--HLTRLEKESIQQSFSNEAKAQALQ-----AQQREQELTQKMQQMEAQHDKtVNEQYslltsQNTFIAKLKEECCTLA 604
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1927222982 2417 E-----SEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIAS------RLHET 2456
Cdd:pfam15964 605 KkleeiTQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEEqcvqhgRMHER 655
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1520-1656 |
1.52e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1520 LKQLRDRAAEAEKLRKAAQEEAEKLRKQV------------NEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLK 1587
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAAlleakelllrerNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1588 RQAEEAERQVKQAEIE-KERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAA 1656
Cdd:PRK12705 105 NQLEEREKALSARELElEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEA 174
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2055-2516 |
1.62e-03 |
|
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: 44.63 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2055 ELDRLKKKAEEARKQKDDADKEAEKQIL----MAQQAAQKCS-AAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKK----L 2125
Cdd:pfam05701 78 LIEELKLNLERAQTEEAQAKQDSELAKLrveeMEQGIADEASvAAKAQLEVAKARHAAAVAELKSVKEELESLRKeyasL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2126 AKQAEAAKEKAErEAALLRQQAEeaerqkaaaeqeaanqaKAQED--AERLRKEAEFEAAKRAQAEnaalKQKQQADAEM 2203
Cdd:pfam05701 158 VSERDIAIKRAE-EAVSASKEIE-----------------KTVEEltIELIATKESLESAHAAHLE----AEEHRIGAAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2204 AK-HKKLA-EQTLKQkfqVEQELTKVKLKLDETDKQKSVLD---EELQRLKDEVDDAVKqrGQVEEELLKVKVqmeellk 2278
Cdd:pfam05701 216 AReQDKLNwEKELKQ---AEEELQRLNQQLLSAKDLKSKLEtasALLLDLKAELAAYME--SKLKEEADGEGN------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2279 lklriEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAqeaARLRqiaeDDLNQQRA-LADKMLKEKMQAIQE 2357
Cdd:pfam05701 284 -----EKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAA---ASLR----SELEKEKAeLASLRQREGMASIAV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2358 ASrLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEyqksleaerkrqleiiAESEKLKLQVSQlsEAQAKAQE 2437
Cdd:pfam05701 352 SS-LEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQE----------------AEEAKSLAQAAR--EELRKAKE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2438 EAKKFKKQADSIASRLH----ETELA-TQEKMTVV-----EKLEVARLTSSKEaDDLRKAIADLEK--EKSRLKKEAEDL 2505
Cdd:pfam05701 413 EAEQAKAAASTVESRLEavlkEIEAAkASEKLALAaikalQESESSAESTNQE-DSPRGVTLSLEEyyELSKRAHEAEEL 491
|
490
....*....|.
gi 1927222982 2506 QNKSKEMADAQ 2516
Cdd:pfam05701 492 ANKRVAEAVSQ 502
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1369-1561 |
1.92e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.83 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1369 SELMTLTSQYIKFITDS---QRRLEDEEKAAE---KLKAEEQKKMAMM---QAELDKQKQLA-----EVHAKAIaKAEKE 1434
Cdd:NF012221 1538 SESSQQADAVSKHAKQDdaaQNALADKERAEAdrqRLEQEKQQQLAAIsgsQSQLESTDQNAletngQAQRDAI-LEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1435 A--QELKLRMQEEVNRREDAVVDAEKQKH-----------NIQLELHELKNLSEQQIMDKSKQVDDALQsrvKIEEEIRl 1501
Cdd:NF012221 1617 AvtKELTTLAQGLDALDSQATYAGESGDQwrnpfagglldRVQEQLDDAKKISGKQLADAKQRHVDNQQ---KVKDAVA- 1692
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1927222982 1502 irlQLETTVKQKSTAESELKQ-LRDRAAEAEKLRKAA---QEEAEKLRKQVNEETQKKRMAEEE 1561
Cdd:NF012221 1693 ---KSEAGVAQGEQNQANAEQdIDDAKADAEKRKDDAlakQNEAQQAESDANAAANDAQSRGEQ 1753
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
2121-2314 |
1.94e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 44.47 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2121 KAKKLAKQAEAAKEKAEREAALLRQQAE-EAERQKAAaeqeaanqakAQEDAERLRKEAEFEAAKRAQaenaalKQKQQA 2199
Cdd:PRK00106 25 KMKSAKEAAELTLLNAEQEAVNLRGKAErDAEHIKKT----------AKRESKALKKELLLEAKEEAR------KYREEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2200 DAEMakhkKLAEQTLKQkfqVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQ-MEELLK 2278
Cdd:PRK00106 89 EQEF----KSERQELKQ---IESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQVEKLEEQkKAELER 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1927222982 2279 LKLRIEEENQRLIKKDkdnTQKFLAKEADNMKKLAE 2314
Cdd:PRK00106 162 VAALSQAEAREIILAE---TENKLTHEIATRIREAE 194
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1834-2485 |
1.94e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1834 LEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEE-EAARQRAEAERILKEKLAAISDATRLKTeAEIALKEKEAENERLR 1912
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIELLEPiRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1913 RQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSS-------EAEMERQRAIVDDTLKQRRVVEEEIRILKLnfekassg 1985
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgdrleqlEREIERLERELEERERRRARLEALLAALGL-------- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1986 klDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAaaeeeaarqrqaaqDELDRLKK---- 2061
Cdd:COG4913 374 --PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE--------------AEIASLERrksn 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2062 ---KAEEARKQKDDADKEAEKQI-----LMaqQAAQKCSAAEQQVQSVLAQQKEDTIM-------------QTKLKEE-- 2118
Cdd:COG4913 438 ipaRLLALRDALAEALGLDEAELpfvgeLI--EVRPEEERWRGAIERVLGGFALTLLVppehyaaalrwvnRLHLRGRlv 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2119 YEKAKKLAKQAEAAKEKAEREA---------------ALLRQQ--------AEEAER------------QKAAAEQEAAN 2163
Cdd:COG4913 516 YERVRTGLPDPERPRLDPDSLAgkldfkphpfrawleAELGRRfdyvcvdsPEELRRhpraitragqvkGNGTRHEKDDR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2164 QAKAQE-----DAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAE--QTLKQKFQVEQELTKVKLKLDETDK 2236
Cdd:COG4913 596 RRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2237 QKSVLDE---ELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNmkkLA 2313
Cdd:COG4913 676 ELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LE 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2314 EDAARLSVEAQEAARLRQIAE--DDLNQQRALADKMLKEKMQAIQ-----EASRLRAEAE-------MLQRQK--DLAqE 2377
Cdd:COG4913 753 ERFAAALGDAVERELRENLEEriDALRARLNRAEEELERAMRAFNrewpaETADLDADLEslpeylaLLDRLEedGLP-E 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2378 QAQKLledKQLMQQRLDEETEEYQKSLEAER---KRQLEIIAES---------EKLKLqvsqlsEAQAKAQEEAKKFKKQ 2445
Cdd:COG4913 832 YEERF---KELLNENSIEFVADLLSKLRRAIreiKERIDPLNDSlkripfgpgRYLRL------EARPRPDPEVREFRQE 902
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1927222982 2446 A-DSIASRLHETELATQEKMTVVEKLeVARLTSSKEADDLR 2485
Cdd:COG4913 903 LrAVTSGASLFDEELSEARFAALKRL-IERLRSEEEESDRR 942
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1772-2185 |
1.99e-03 |
|
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: 44.25 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1772 QQRSLLEDELYRLKNEV-------VAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSkQLLEVEATKM-RD 1843
Cdd:pfam05701 35 ERRKLVELELEKVQEEIpeykkqsEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDS-ELAKLRVEEMeQG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1844 LAEEAS-KLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKE-KEAEnerlrRQAEDEAYQ 1921
Cdd:pfam05701 114 IADEASvAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSAsKEIE-----KTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1922 ----RKALEDQANQHKQQIEEKIvllkkssEAEMERQRaivdDTLKQRR---VVEEEIRilKLNFEKASSGKLDLELELN 1994
Cdd:pfam05701 189 liatKESLESAHAAHLEAEEHRI-------GAALAREQ----DKLNWEKelkQAEEELQ--RLNQQLLSAKDLKSKLETA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1995 KLKniaeetqQSKLRAEEEAEKLRKLaleeekrrreaeekvKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDAD 2074
Cdd:pfam05701 256 SAL-------LLDLKAELAAYMESKL---------------KEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2075 KEAEkqiLMAQQAAQKCSAAEQQvQSVLA--QQKED--TIMQTKLKEEYEKAKK----LAKQAEAAKEKAEREAALLRQQ 2146
Cdd:pfam05701 314 DEVN---CLRVAAASLRSELEKE-KAELAslRQREGmaSIAVSSLEAELNRTKSeialVQAKEKEAREKMVELPKQLQQA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1927222982 2147 AEEAERQKAAAEQEAANQAKAQEDAERLRK-----EAEFEAAKR 2185
Cdd:pfam05701 390 AQEAEEAKSLAQAAREELRKAKEEAEQAKAaastvESRLEAVLK 433
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2310-2609 |
2.08e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2310 KKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLM 2389
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2390 QQRLD---EETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETE-----LATQ 2461
Cdd:COG4372 100 QEELEslqEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEqelqaLSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2462 EKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKK 2541
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 2542 EKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEM 2609
Cdd:COG4372 260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2368-2644 |
2.12e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.29 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2368 LQRQKDLAQEQAQKLLEDKQLMQQRLDEeTEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQAD 2447
Cdd:pfam05622 19 LDQQVSLLQEEKNSLQQENKKLQERLDQ-LESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2448 SIASRLHETELATQEKMTVVEKLEVARLTSSKeaddlrkaIADLEKEKSRLKKEAEDLQNKSKEMadaqqKQIEHEKTV- 2526
Cdd:pfam05622 98 ELQHRNEELTSLAEEAQALKDEMDILRESSDK--------VKKLEATVETYKKKLEDLGDLRRQV-----KLLEERNAEy 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2527 LQQTFlsekemllkkeklieeekkrlesQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMdaalNKQKEAEKEMHNKQ 2606
Cdd:pfam05622 165 MQRTL-----------------------QLEEELKKANALRGQLETYKRQVQELHGKLSEES----KKADKLEFEYKKLE 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 1927222982 2607 KEMKELERkrlEQERILAEENQkLREKLQQLEEAQKDQ 2644
Cdd:pfam05622 218 EKLEALQK---EKERLIIERDT-LRETNEELRCAQLQQ 251
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2317-2507 |
2.13e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2317 ARLSVEAQE-AARLRQIAED-DLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDL-AQEQAQKLLEDKQLMQQRL 2393
Cdd:PRK05035 460 ARLEREKAArEARHKKAAEArAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAViAAREARKAQARARQAEKQA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2394 DEETEEYQKSLEAERKR--------QLEIIAESEKLKLQVSQLSEAQAKAQeeAKKFKKQADSIASRlhETELATQEKMT 2465
Cdd:PRK05035 540 AAAADPKKAAVAAAIARakakkaaqQAANAEAEEEVDPKKAAVAAAIARAK--AKKAAQQAASAEPE--EQVAEVDPKKA 615
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1927222982 2466 VVE---------KLEVARLTSSKEADDLRKAI--ADLEKEKSRLKKEAEDLQN 2507
Cdd:PRK05035 616 AVAaaiarakakKAEQQANAEPEEPVDPRKAAvaAAIARAKARKAAQQQANAE 668
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1194-1380 |
2.17e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1194 LEAELKKATAVSDKMSRVHSERDAELDHYRQLLSSLQDRWKAVFSQIDLR--QRELEQLGRQLGYYRESYDWLIRwindA 1271
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAsaEREIAELEAELERLDASSDDLAA----L 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1272 KQRQEKIQAVTITDSKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDYELQLVAykaqvEPLASPLKKTKLD 1351
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE-----ERFAAALGDAVER 765
|
170 180 190
....*....|....*....|....*....|...
gi 1927222982 1352 SASDNIIQEYVTLRTK----YSELMTLTSQYIK 1380
Cdd:COG4913 766 ELRENLEERIDALRARlnraEEELERAMRAFNR 798
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2308-2518 |
2.35e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.82 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2308 NMKKLAEDAARlsvEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQE-----------ASRLRAEAEMLQRQKDLAQ 2376
Cdd:PRK07735 6 DLEDLKKEAAR---RAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDdmtieeakrraAAAAKAKAAALAKQKREGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2377 EQAQKllEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHET 2456
Cdd:PRK07735 83 EEVTE--EEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEET 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222982 2457 ELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQK 2518
Cdd:PRK07735 161 DKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQK 222
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2322-2504 |
2.37e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.84 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2322 EAQEAARLRQIAEDDLNQQRALADKmlkekmqAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQ 2401
Cdd:pfam05262 207 ESQEDAKRAQQLKEELDKKQIDADK-------AQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2402 KSlEAERKRQleiiaeseklklqvsqlsEAQaKAQEEAKKFKKQADSIASRlhetELATQEKMTVVEKLEvARLTSSKEA 2481
Cdd:pfam05262 280 KR-EIEKAQI------------------EIK-KNDEEALKAKDHKAFDLKQ----ESKASEKEAEDKELE-AQKKREPVA 334
|
170 180
....*....|....*....|...
gi 1927222982 2482 DDLRKAIADLEKEKSRLKKEAED 2504
Cdd:pfam05262 335 EDLQKTKPQVEAQPTSLNEDAID 357
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1386-1604 |
2.38e-03 |
|
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: 43.68 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1386 QRRLEDEEKAAEKLKAEEQKKMAMMQ-AELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVvdAEKQKhniq 1464
Cdd:TIGR02794 71 KKLEQQAEEAEKQRAAEQARQKELEQrAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAE--AERKA---- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1465 lelhelknlseqqimdkskqvddALQSRVKIEEEirliRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEE---- 1540
Cdd:TIGR02794 145 -----------------------KEEAAKQAEEE----AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakak 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222982 1541 AEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDL--ENLKRQAEEAERQVKQAEIEK 1604
Cdd:TIGR02794 198 AEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLasGSNAEKQGGARGAAAGSEVDK 263
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2248-2647 |
2.45e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2248 LKDEVDDAVKQRGQVEEELLKVKVQMEELLK---LKLRIEEENQRLIKKDKD-NTQKFLAKEADNMKKLAEDAARLSVEA 2323
Cdd:pfam12128 198 VKSMIVAILEDDGVVPPKSRLNRQQVEHWIRdiqAIAGIMKIRPEFTKLQQEfNTLESAELRLSHLHFGYKSDETLIASR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2324 QEAarlRQIAEDDLNQQRALADKMLKEKMQAI-QEASRLRAEAEMLQRQKDLAQEQAQklledkqlmqQRLDEETEEYQK 2402
Cdd:pfam12128 278 QEE---RQETSAELNQLLRTLDDQWKEKRDELnGELSAADAAVAKDRSELEALEDQHG----------AFLDADIETAAA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2403 SLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHEtelatqekmtvveklevaRLTSSKEAD 2482
Cdd:pfam12128 345 DQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKD------------------KLAKIREAR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2483 DLRKAIA--DLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKR--LESQFEE 2558
Cdd:pfam12128 407 DRQLAVAedDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAReeQEAANAE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2559 ------EVKKAKALKDEQER---------QKQQMEDEKKKLQ-----ATMDAALNKQKEAEKEMHNKQKEMKELERK--- 2615
Cdd:pfam12128 487 verlqsELRQARKRRDQASEalrqasrrlEERQSALDELELQlfpqaGTLLHFLRKEAPDWEQSIGKVISPELLHRTdld 566
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1927222982 2616 -----------------RLEQERILAEE----NQKLREKLQQLEEAQKDQPDK 2647
Cdd:pfam12128 567 pevwdgsvggelnlygvKLDLKRIDVPEwaasEEELRERLDKAEEALQSAREK 619
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2383-2622 |
2.50e-03 |
|
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: 43.86 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2383 LEDKQLMQQRLD---EETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELA 2459
Cdd:pfam05701 34 VERRKLVELELEkvqEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMEQG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2460 TQEKMTVVEK--LEVAR---------LTSSK-EADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMadaqQKQIEH---EK 2524
Cdd:pfam05701 114 IADEASVAAKaqLEVAKarhaaavaeLKSVKeELESLRKEYASLVSERDIAIKRAEEAVSASKEI----EKTVEEltiEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2525 TVLQQTFLS---------EKEMLLKKEKLIEEEKKRLE-SQFEEEVKK-------AKALKDEQERQKQQMEDEKKKLQAT 2587
Cdd:pfam05701 190 IATKESLESahaahleaeEHRIGAALAREQDKLNWEKElKQAEEELQRlnqqllsAKDLKSKLETASALLLDLKAELAAY 269
|
250 260 270
....*....|....*....|....*....|....*...
gi 1927222982 2588 MDAALNK---QKEAEKEMHNKQKEMKELERKRLEQERI 2622
Cdd:pfam05701 270 MESKLKEeadGEGNEKKTSTSIQAALASAKKELEEVKA 307
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
986-1559 |
2.52e-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: 44.27 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 986 DDRMQIEEDYTKSTQHFDSLIRSMEKglmvVRHKGQqdetlckNYLSEIKdlrLRIEDCEAGTVARIRRPVEKEPLKECV 1065
Cdd:TIGR01612 1111 DEINKIKDDIKNLDQKIDHHIKALEE----IKKKSE-------NYIDEIK---AQINDLEDVADKAISNDDPEEIEKKIE 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1066 QKTTEQKKVQVELEGLKKDLNKVSAKTKEvlaspqQTASAPVLRSeldltveKMDHTHMLSSVYLEKLKtvemviRNTQG 1145
Cdd:TIGR01612 1177 NIVTKIDKKKNIYDEIKKLLNEIAEIEKD------KTSLEEVKGI-------NLSYGKNLGKLFLEKID------EEKKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1146 AEGVLKQYEDCLREVHTVPNDVKEVETYRTKLKKMRAEAEgeqpVFDSLEAELKKATAVSDKMSRVHSE-RDAEL----D 1220
Cdd:TIGR01612 1238 SEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEME----TFNISHDDDKDHHIISKKHDENISDiREKSLkiieD 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1221 HYRQllSSLQDRWKAVFSQIDLRQRELEQLGRQLGYYRESYDWLI-----RWINDAKQRQEKIQavtiTDSKTLKEQLAQ 1295
Cdd:TIGR01612 1314 FSEE--SDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKlnkikKIIDEVKEYTKEIE----ENNKNIKDELDK 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1296 EKKLLEEVEGNKDkVDECQKYAKAYIDTiKDYELQLVAYKAQVEPLASplKKTKLDSASDNIIQ--EYVTLRTKYSELMT 1373
Cdd:TIGR01612 1388 SEKLIKKIKDDIN-LEECKSKIESTLDD-KDIDECIKKIKELKNHILS--EESNIDTYFKNADEnnENVLLLFKNIEMAD 1463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1374 LTSQYI-------------------KFITDSQRRLEDE----EKAAEKLKA--EEQKKMAM----------MQAELDKQK 1418
Cdd:TIGR01612 1464 NKSQHIlkikkdnatndhdfninelKEHIDKSKGCKDEadknAKAIEKNKElfEQYKKDVTellnkysalaIKNKFAKTK 1543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1419 --------QLAEVHAKAIAKAEKEAQELKlRMQEEVNRREDAVVDAEKQKH---NIQLELHELKNlSEQQIMDKSKQVDD 1487
Cdd:TIGR01612 1544 kdseiiikEIKDAHKKFILEAEKSEQKIK-EIKKEKFRIEDDAAKNDKSNKaaiDIQLSLENFEN-KFLKISDIKKKIND 1621
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222982 1488 ALQSRVKIEEEIRLIRL-----QLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAE 1559
Cdd:TIGR01612 1622 CLKETESIEKKISSFSIdsqdtELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYE 1698
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1587-1882 |
2.58e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.37 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1587 KRQAEEAERQVKQAeIEKERQIQVAHVAAQKSAAAELQsKHMSFVEKTSKLEESLKQEHGavLQLQHEAAALKKQQEDAE 1666
Cdd:pfam13868 43 RRLDEMMEEERERA-LEEEEEKEEERKEERKRYRQELE-EQIEEREQKRQEEYEEKLQER--EQMDEIVERIQEEDQAEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1667 RAREEAEKELEKWRQKANEALRLRLQAEEEAHKK---SLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQR 1743
Cdd:pfam13868 119 EEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREedeRILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1744 KVAESTAQ-QKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMdvLIQLKSKAEKE 1822
Cdd:pfam13868 199 EKAERDELrAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFER--MLRKQAEDEEI 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 1823 TMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQR-----AEAERILKE 1882
Cdd:pfam13868 277 EQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERrerieEERQKKLKE 341
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2111-2384 |
2.61e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.82 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2111 MQTKLKEEYEKAKKLAKQAEAAKEKAEReaALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAEN 2190
Cdd:PRK07735 7 LEDLKKEAARRAKEEARKRLVAKHGAEI--SKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2191 A-----ALKQKQQADAEMAKHKKLAEQTLKQKFQV-EQELTKVKLKLDETDKQKSvldEELQRLKDEVDDAVKQRGQVEE 2264
Cdd:PRK07735 85 VteeekAKAKAKAAAAAKAKAAALAKQKREGTEEVtEEEKAAAKAKAAAAAKAKA---AALAKQKREGTEEVTEEEEETD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2265 ELL-------KVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKflAKEADNMKKLAEDAARlsveaQEAARLRQIAEDDL 2337
Cdd:PRK07735 162 KEKakakaaaAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAK--AKAAAAAKAKAAALAK-----QKASQGNGDSGDED 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1927222982 2338 NQQRALAdkMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLE 2384
Cdd:PRK07735 235 AKAKAIA--AAKAKAAAAARAKTKGAEGKKEEEPKQEEPSVNQPYLN 279
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2323-2648 |
2.71e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2323 AQEAARLRQIAEDDLNQQRALADKmlKEKMQAIQEA-SRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQ--RLDEETEE 2399
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTS--RRQLAAEQYRlVEMARELAELNEAESDLEQDYQAASDHLNLVQTalRQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2400 YQKSLEaERKRQLEiiAESEKLKLQVSQLSEAQAK---AQEEAKKFKKQ-ADsiasrlhetelatqekmtVVEKLEVARl 2475
Cdd:PRK04863 353 YQADLE-ELEERLE--EQNEVVEEADEQQEENEARaeaAEEEVDELKSQlAD------------------YQQALDVQQ- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2476 tssKEADDLRKAIADLEKEKSRLKKEAEDLQNKSK--EMADAQQKQIEHEKTVLQQTfLSEKEMLLkkeklieeekkrle 2553
Cdd:PRK04863 411 ---TRAIQYQQAVQALERAKQLCGLPDLTADNAEDwlEEFQAKEQEATEELLSLEQK-LSVAQAAH-------------- 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2554 SQFEEEVKKAKALKDEQERqkqqmEDEKKKLQATMDAALNKQKEAEKE--MHNKQKEMKELERKRLEQERILAEENQKLR 2631
Cdd:PRK04863 473 SQFEQAYQLVRKIAGEVSR-----SEAWDVARELLRRLREQRHLAEQLqqLRMRLSELEQRLRQQQRAERLLAEFCKRLG 547
|
330
....*....|....*..
gi 1927222982 2632 EKLQQLEEAQKDQPDKE 2648
Cdd:PRK04863 548 KNLDDEDELEQLQEELE 564
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2345-2665 |
2.75e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.98 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2345 DKMLKEKMQAIQEASRLRAEAE-----MLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESE 2419
Cdd:pfam09731 84 EEKKQVKIPRQSGVSSEVAEEEkeatkDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2420 KLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSrlk 2499
Cdd:pfam09731 164 DSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQS--- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2500 kEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEE------------EKKRLESQFEEEVKKAKALK 2567
Cdd:pfam09731 241 -LAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSliahahreidqlSKKLAELKKREEKHIERALE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2568 DEQERQKQQMEDEKKKLQATMDAALNK-QKEAEKEMHNKQKEMKELERKRLEQERILAEEnqKLREKLQQLEEAQKDQPD 2646
Cdd:pfam09731 320 KQKEELDKLAEELSARLEEVRAADEAQlRLEFEREREEIRESYEEKLRTELERQAEAHEE--HLKDVLVEQEIELQREFL 397
|
330
....*....|....*....
gi 1927222982 2647 KEVIhvTMVETTKNVYNGQ 2665
Cdd:pfam09731 398 QDIK--EKVEEERAGRLLK 414
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
63-183 |
2.79e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 40.75 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 63 ADERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPrerdvVRSVRLPREKGRmrfHKLQNVQ 142
Cdd:cd21337 14 APDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVP-----LHSFFLTPDSFE---QKVLNVS 85
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1927222982 143 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 183
Cdd:cd21337 86 FAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1999-2345 |
2.86e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1999 IAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAE 2078
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2079 KQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAE 2158
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2159 QEAANQAKAQEDAERLRKEAEFEAAKRAQAENAalKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQK 2238
Cdd:COG4372 164 EELAALEQELQALSEAEAEQALDELLKEANRNA--EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2239 SVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAAR 2318
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
330 340
....*....|....*....|....*..
gi 1927222982 2319 LSVEAQEAARLRQIAEDDLNQQRALAD 2345
Cdd:COG4372 322 LELAKKLELALAILLAELADLLQLLLV 348
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2111-2459 |
2.89e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2111 MQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAEN 2190
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2191 AALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVK 2270
Cdd:COG4372 98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2271 VQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQ--IAEDDLNQQRALADKML 2348
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALldALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2349 KEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQL 2428
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
|
330 340 350
....*....|....*....|....*....|.
gi 1927222982 2429 SEAQAKAQEEAKKFKKQADSIASRLHETELA 2459
Cdd:COG4372 338 ELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2370-2697 |
2.91e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2370 RQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSI 2449
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2450 ASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQ-QKQIEHEKTVLQ 2528
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALDELLKEAN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2529 QTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKE 2608
Cdd:COG4372 194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2609 MKELERKRLEQERILAEENQKLREKLQQLEEAQKDQPDKEVIHVTMVETTKNVYNGQNVGDVVDSAEKKPDPLAFNGIRE 2688
Cdd:COG4372 274 EEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDN 353
|
....*....
gi 1927222982 2689 KVPASRLHD 2697
Cdd:COG4372 354 DVLELLSKG 362
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1830-2016 |
2.92e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1830 SKQLLEVEATKMRDLAEEASKLRAIAEEAKHQrqvAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENE 1909
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLE---AKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1910 RLRRQAEDEAYQRKALEDQANQHKQQIEEKIvllkKSSEAEMERQRAIVDDTLKQR--RVVEEEIRIlklnfEKASsgkl 1987
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELI----EEQLQELERISGLTAEEAKEIllEKVEEEARH-----EAAV---- 173
|
170 180
....*....|....*....|....*....
gi 1927222982 1988 dlelelnKLKNIAEEtqqsklrAEEEAEK 2016
Cdd:PRK12704 174 -------LIKEIEEE-------AKEEADK 188
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1386-1607 |
2.94e-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: 43.37 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1386 QRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEV---NRREDAVVDAEKQKHN 1462
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKlqeREQMDEIVERIQEEDQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1463 IQLELHELKNLSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAA-EAEKLRKAAQEEA 1541
Cdd:pfam13868 116 AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEkEREIARLRAQQEK 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222982 1542 EKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQ 1607
Cdd:pfam13868 196 AQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEE 261
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2553-2647 |
2.97e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2553 ESQFEEEVKKAKAL---KDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQK 2629
Cdd:PRK12704 46 EAKKEAEAIKKEALleaKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQE 125
|
90
....*....|....*...
gi 1927222982 2630 LREKLQQLEEAQKDQPDK 2647
Cdd:PRK12704 126 LEKKEEELEELIEEQLQE 143
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1949-2508 |
3.04e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1949 AEMERQRAIVDDTLKQRRVVEEeIRILKLNFEKASSGKLDLELELNKLKniAEETQQSKLRAEEEAEKLRKlaleeekrr 2028
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRA--------- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2029 reaeekvkKIAAAEEEAArqrqAAQDELDRLKKKAEEARKQKDDAD----KEAEKQILMAQQAAQKCSAAEQQVQSVLAQ 2104
Cdd:COG4913 303 --------ELARLEAELE----RLEARLDALREELDELEAQIRGNGgdrlEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2105 QKEdtimqtKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKaaaeqeaanqAKAQEDAERLRKE------- 2177
Cdd:COG4913 371 LGL------PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL----------RDLRRELRELEAEiaslerr 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2178 -----AEFEAAKRAQAENAALKQKQ-------------QADAEMA----------------KHKKLA----EQT-LKQKF 2218
Cdd:COG4913 435 ksnipARLLALRDALAEALGLDEAElpfvgelievrpeEERWRGAiervlggfaltllvppEHYAAAlrwvNRLhLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2219 QVEQELTKVKLKLDETDKQKSVLDE---ELQRLKDEVDDAVKQRGQV-----EEELLKVK--VQMEELLKLKLRIEEEN- 2287
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDSLAGKldfKPHPFRAWLEAELGRRFDYvcvdsPEELRRHPraITRAGQVKGNGTRHEKDd 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2288 QRLIKKD----KDNTQKFLAKEADnmkkLAEDAARLSVEAQEAARLRQIAEDDLNQQRALadkmlkekmQAIQEASRLRA 2363
Cdd:COG4913 595 RRRIRSRyvlgFDNRAKLAALEAE----LAELEEELAEAEERLEALEAELDALQERREAL---------QRLAEYSWDEI 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2364 EAEMLQRQKDLAQEQAQKLLEDKQLMQQrLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAkkfk 2443
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAA-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---- 736
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 2444 KQADSIASRLHETELATQEKMTVVEKLEvarltsSKEADDLRKAIADLEKEKSRLKKEAEDLQNK 2508
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVE------RELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2406-2636 |
3.15e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2406 AERKRQLEI----IAESEK-LKLQVSQLSE--AQAKAQEeakkfkkQADSIASR-LHETelatQEKMTVVEKlEVARLTS 2477
Cdd:PRK11637 43 SDNRDQLKSiqqdIAAKEKsVRQQQQQRASllAQLKKQE-------EAISQASRkLRET----QNTLNQLNK-QIDELNA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2478 SkeaddlrkaIADLEKEKSRLKK----------------------EAEDLQNKSKEMA------DAQQKQIEHektvLQQ 2529
Cdd:PRK11637 111 S---------IAKLEQQQAAQERllaaqldaafrqgehtglqlilSGEESQRGERILAyfgylnQARQETIAE----LKQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2530 TflsEKEMLLKkeklieeekkrlESQFEEEVKKAKALKDEQERQKQQME---DEKKKLQATMDAALNKQKEAEKEMHNKQ 2606
Cdd:PRK11637 178 T---REELAAQ------------KAELEEKQSQQKTLLYEQQAQQQKLEqarNERKKTLTGLESSLQKDQQQLSELRANE 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 1927222982 2607 KEMK------ELERK-RLEQErilAEENQKLREKLQQ 2636
Cdd:PRK11637 243 SRLRdsiaraEREAKaRAERE---AREAARVRDKQKQ 276
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
846-890 |
3.21e-03 |
|
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: 38.41 E-value: 3.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1927222982 846 IQAVCDFK---QQEITVHKGDECALLNNSQPFKWKVLNRSGHEAVVPS 890
Cdd:cd11768 2 VVALYDFQpiePGDLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPS 49
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1008-1547 |
3.30e-03 |
|
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: 43.95 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1008 SMEKGLMVVRHKGQQDETLCKNYLSEIKDL--RLRIEDCEAgtvARIRRPVEKEPLKECVQKTTEQKKVQVELEGLKKDL 1085
Cdd:pfam15921 296 SIQSQLEIIQEQARNQNSMYMRQLSDLESTvsQLRSELREA---KRMYEDKIEELEKQLVLANSELTEARTERDQFSQES 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1086 NKVSAKTKEVLASpqqtasapVLRSELDLTVEKMDHTHML-----SSVYLEKLKTvEMVIRN--TQGAEGVLKQYE-DCL 1157
Cdd:pfam15921 373 GNLDDQLQKLLAD--------LHKREKELSLEKEQNKRLWdrdtgNSITIDHLRR-ELDDRNmeVQRLEALLKAMKsECQ 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1158 REVHTVPNDVKEVETYRTKLKKMRAEAEGEQPVFDSLEAELKKATAVSDKMSRVHSERDAELDHYRQLLSSLQDRWKAVF 1237
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLR 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1238 SQIDLRQRELEQLgrqlgyyresydwlirwindaKQRQEKIQAVTiTDSKTLKEQLAQEKKLLE----------EVEGNK 1307
Cdd:pfam15921 524 SRVDLKLQELQHL---------------------KNEGDHLRNVQ-TECEALKLQMAEKDKVIEilrqqienmtQLVGQH 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1308 DKVDECQKYAKAYIDT-IKDYELQLVAYK-------AQVEPLAS-----PLKKTKLDSASD-------NIIQEYVTL--- 1364
Cdd:pfam15921 582 GRTAGAMQVEKAQLEKeINDRRLELQEFKilkdkkdAKIRELEArvsdlELEKVKLVNAGSerlravkDIKQERDQLlne 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1365 -RTKYSELMTLTSQYIKFITDSQRRLEDEEKAAEKLKAEeqkkMAMMQAELDKQKQLaevhAKAIAKAEKEAQELKLRMQ 1443
Cdd:pfam15921 662 vKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ----LKSAQSELEQTRNT----LKSMEGSDGHAMKVAMGMQ 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1444 EEVNRR--------------EDAVVDAEKQKHNIQLELHELknlseqqimdkSKQVDDALQSRVKIEEEIRLIRLQlETT 1509
Cdd:pfam15921 734 KQITAKrgqidalqskiqflEEAMTNANKEKHFLKEEKNKL-----------SQELSTVATEKNKMAGELEVLRSQ-ERR 801
|
570 580 590
....*....|....*....|....*....|....*....
gi 1927222982 1510 VKQK-STAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQ 1547
Cdd:pfam15921 802 LKEKvANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2062-2214 |
3.54e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.97 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2062 KAEEARKQKDDADKEAEKQIlmaqqaaqkcSAAEQQVQSVLAQQKEdtiMQTKLKEEYEKAKKLAKQAEAAKEKAEREAA 2141
Cdd:pfam04012 19 KAEDPEKMLEQAIRDMQSEL----------VKARQALAQTIARQKQ---LERRLEQQTEQAKKLEEKAQAALTKGNEELA 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927222982 2142 llRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAEnaALKQKQQADAEMAKHKKLAEQTL 2214
Cdd:pfam04012 86 --REALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLK--AKKNLLKARLKAAKAQEAVQTSL 154
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2275-2440 |
3.60e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.47 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2275 ELLKLKLRIEEENQRlikkdkdntQKFLAKEADNMKKLAEDAARlsVEAQEAARLRQIaeddlnqqraladkmlkeKMQA 2354
Cdd:PTZ00491 684 ERQKMHDKAKAEEQR---------TKLLELQAESAAVESSGQSR--AEALAEAEARLI------------------EAEA 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2355 IQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQlmQQRLDEeteeyqksLEAERKRQLEIIaESEKLKLQVSQLS----E 2430
Cdd:PTZ00491 735 EVEQAELRAKALRIEAEAELEKLRKRQELELEY--EQAQNE--------LEIAKAKELADI-EATKFERIVEALGretlI 803
|
170
....*....|
gi 1927222982 2431 AQAKAQEEAK 2440
Cdd:PTZ00491 804 AIARAGPELQ 813
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3093-3125 |
3.81e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.81e-03
10 20 30
....*....|....*....|....*....|...
gi 1927222982 3093 LEAQAGTGYVVDPVDNKKYTVDEAVKAGVVGPE 3125
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1535-2254 |
3.81e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1535 KAAQEEAEKLRKQV------NEETQKKRMAEEELKRKAEAEKEAAK-QKQKALEDLENlkrQAEEAERQVKQAEIEKERq 1607
Cdd:COG4913 238 ERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRLwFAQRRLELLEA---ELEELRAELARLEAELER- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1608 iqvaHVAAQKSAAAELQSkhmsfvektskLEESLKQEHGAVLQlqheaaALKKQqedaerareeaekeLEKWRQKANEAL 1687
Cdd:COG4913 314 ----LEARLDALREELDE-----------LEAQIRGNGGDRLE------QLERE--------------IERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1688 RLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKvaestaqqklTAEQELIRLRADF 1767
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR----------DLRRELRELEAEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1768 DNAEQQRSLLEDELyrlknevvaaQQQRKQLEDELAKVRSEMDV---LIQLKSKAEKETMS--------------NSERS 1830
Cdd:COG4913 429 ASLERRKSNIPARL----------LALRDALAEALGLDEAELPFvgeLIEVRPEEERWRGAiervlggfaltllvPPEHY 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1831 KQLLE-VEATKMRdlaeeaskLRAIAEEAKHQRQVAEEEAARQRAEAERI----------LKEKLAAISDATRLKTEAEI 1899
Cdd:COG4913 499 AAALRwVNRLHLR--------GRLVYERVRTGLPDPERPRLDPDSLAGKLdfkphpfrawLEAELGRRFDYVCVDSPEEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1900 A-----------LKEKEAENERLRRQAEDEAY--------QRKALEDQAnqhkQQIEEKIVLLkkssEAEMERQRAIVDD 1960
Cdd:COG4913 571 RrhpraitragqVKGNGTRHEKDDRRRIRSRYvlgfdnraKLAALEAEL----AELEEELAEA----EERLEALEAELDA 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1961 TLKQRRVVEeeiRILKLNFEKASSGKLDLELElnklkniaeetqqsklRAEEEAEKLRKlaleeekrrreaeekvkkiaa 2040
Cdd:COG4913 643 LQERREALQ---RLAEYSWDEIDVASAEREIA----------------ELEAELERLDA--------------------- 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2041 aeeeaarqrqaAQDELDRLKKKAEEARKQKDDADKEAEkqilmaqQAAQKCSAAEQQVQSVLAQQKEdtimqtkLKEEYE 2120
Cdd:COG4913 683 -----------SSDDLAALEEQLEELEAELEELEEELD-------ELKGEIGRLEKELEQAEEELDE-------LQDRLE 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2121 KAKKLAKQAEAAkekaerEAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAE--FEAAKRAQAENAALKQKQQ 2198
Cdd:COG4913 738 AAEDLARLELRA------LLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELEraMRAFNREWPAETADLDADL 811
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2199 ADAE--MAKHKKLAEQTLKQKfqvEQELTKVKLKLDETDKQ--KSVLDEELQRLKDEVDD 2254
Cdd:COG4913 812 ESLPeyLALLDRLEEDGLPEY---EERFKELLNENSIEFVAdlLSKLRRAIREIKERIDP 868
|
|
| SH3_Eps8 |
cd11764 |
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ... |
855-890 |
3.83e-03 |
|
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar proteins; This group is composed of Eps8 and Eps8-like proteins including Eps8-like 1-3, among others. These proteins contain N-terminal Phosphotyrosine-binding (PTB), central SH3, and C-terminal effector domains. Eps8 binds either Abi1 (also called E3b1) or Rab5 GTPase activating protein RN-tre through its SH3 domain. With Abi1 and Sos1, it becomes part of a trimeric complex that is required to activate Rac. Together with RN-tre, it inhibits the internalization of EGFR. The SH3 domains of Eps8 and similar proteins recognize peptides containing a PxxDY motif, instead of the classical PxxP motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212698 [Multi-domain] Cd Length: 54 Bit Score: 38.40 E-value: 3.83e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1927222982 855 QEITVHKGDECALLNNSQPFkWKVLNRSGHEAVVPS 890
Cdd:cd11764 14 KELSVLKGEYLEVLDDSRQW-WKVRNSRGQVGYVPH 48
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1445-1785 |
3.88e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1445 EVNRREDAVVDAEKQKHNIQLELHELKNLSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLR 1524
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1525 DRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRkaeaekeaakqkqkaLEDLENL----KRQAEEAERQVKQA 1600
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEER---------------EEDERILeylkEKAEREEEREAERE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1601 EIEKERQIQVAHVAAQKSAAAELQSkhmsfvektskleeslkqehgavlqlQHEAAALKKQQEDAERAREEAEKELEKWR 1680
Cdd:pfam13868 177 EIEEEKEREIARLRAQQEKAQDEKA--------------------------ERDELRAKLYQEEQERKERQKEREEAEKK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1681 QKANEALRLRLQAEEEAHKKSLAqedAEKQKEEAEREAKKRAKAEDsalKQKEMAENELERQRKVAESTAQQKLTAEQEL 1760
Cdd:pfam13868 231 ARQRQELQQAREEQIELKERRLA---EEAEREEEEFERMLRKQAED---EEIEQEEAEKRRMKRLEHRRELEKQIEEREE 304
|
330 340
....*....|....*....|....*
gi 1927222982 1761 IRLRADFDNAEQQRSLLEDELYRLK 1785
Cdd:pfam13868 305 QRAAEREEELEEGERLREEEAERRE 329
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2214-2660 |
3.90e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2214 LKQKFQVEQ-ELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIK 2292
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2293 KDKDNTQkflakeadnMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLK----------EKMQAIQEASRLR 2362
Cdd:PRK01156 268 ELEKNNY---------YKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSnidaeinkyhAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2363 AEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLdEETEEYQKSLEAERKRQLEIIAE-SEKLKLQ-------VSQLSEAQAK 2434
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMDYNSYL-KSIESLKKKIEEYSKNIERMSAFiSEILKIQeidpdaiKKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2435 AQEEAKKFKKQADSIASrLHETELATQEKMTVVEKLEVARLTSSKEADD-LRKAIADLEKEKSRLKKEAEDLQNKSKEMA 2513
Cdd:PRK01156 418 LQDISSKVSSLNQRIRA-LRENLDELSRNMEMLNGQSVCPVCGTTLGEEkSNHIINHYNEKKSRLEEKIREIEIEVKDID 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2514 DAQQKQI---------EHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKL 2584
Cdd:PRK01156 497 EKIVDLKkrkeyleseEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAV 576
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 2585 QATMDAALNKQK--EAEKEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQPDKEVIHVTMVETTKN 2660
Cdd:PRK01156 577 ISLIDIETNRSRsnEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDN 654
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4418-4455 |
3.92e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.92e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1927222982 4418 QRFLEIQYLTGGLIEPDVEGRVSLDESIRKGTIDARTA 4455
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2565-2644 |
4.03e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2565 ALKDEQERQKQQMEDEKKKLQatmdaaLNKQKEAEKEMHNKQKEMKELER-KRLEQERILAEENQKLREKLQQLEEAQKD 2643
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRAEE------QRKKKEQQQAEELQQKQAAEQERlKQLEKERLAAQEQKKQAEEAAKQAALKQK 132
|
.
gi 1927222982 2644 Q 2644
Cdd:PRK09510 133 Q 133
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1633-1766 |
4.07e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.07 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1633 KTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEaekeLEKWRQKANEALRLRLQAEEEAHKKSlAQED---AEK 1709
Cdd:pfam05262 204 KERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDN----ADKQRDEVRQKQQEAKNLPKPADTSS-PKEDkqvAEN 278
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 1710 QKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQK-LTAEQELIRLRAD 1766
Cdd:pfam05262 279 QKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKeLEAQKKREPVAED 336
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2476-2598 |
4.22e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2476 TSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEmllkKEKLIEEEKKRLESQ 2555
Cdd:COG0542 408 SKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKE----LIEEIQELKEELEQR 483
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 2556 FEEEVKKAKALKDEQERQKQQ----------------------------MEDEKKKLQaTMDAALNK----QKEA 2598
Cdd:COG0542 484 YGKIPELEKELAELEEELAELapllreevteediaevvsrwtgipvgklLEGEREKLL-NLEEELHErvigQDEA 557
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1784-2125 |
4.26e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1784 LKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETmsnsERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQ 1863
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1864 VAEEEAARQRAEAERILKEKLAAISDATRLK---TEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKI 1940
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEaqiAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1941 VLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKL 2020
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2021 ALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQS 2100
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQ 344
|
330 340
....*....|....*....|....*
gi 1927222982 2101 VLAQQKEDTIMQTKLKEEYEKAKKL 2125
Cdd:COG4372 345 LLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1842-1965 |
4.57e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1842 RDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERIlkEKLAAisdatrlktEAEIALKEKEAENERLRRQAEDEAYQ 1921
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVAL--EGLAA---------ELEEKQQELEAQLEQLQEKAAETSQE 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1927222982 1922 RKAledQANQHKQQIEEKIVLlkksSEAEmerQRAIVDDTLKQR 1965
Cdd:PRK11448 214 RKQ---KRKEITDQAAKRLEL----SEEE---TRILIDQQLRKA 247
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1178-1605 |
4.66e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1178 KKMRAEAEGEQPVFDSLEAELKKAtavsdkmsrvhSERDAELDHYRQLLSSLQDRWKAVFSQIDLRQRELEQLGRQLGYY 1257
Cdd:pfam05557 69 EALREQAELNRLKKKYLEALNKKL-----------NEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1258 RESYDWLIRWINDAKQRQEKIQAvtitDSKTLKEQLAQEKKLLEEVEGNKDKVDECqKYAKAYIDTIKDYELQLVAYKAQ 1337
Cdd:pfam05557 138 QERLDLLKAKASEAEQLRQNLEK----QQSSLAEAEQRIKELEFEIQSQEQDSEIV-KNSKSELARIPELEKELERLREH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1338 VEPLASpLKKTKLdsasdnIIQEYVTlrtkyselmtltsqyikfitDSQRRLEDEEKAAEKLKAEEQKKmAMMQAELDKQ 1417
Cdd:pfam05557 213 NKHLNE-NIENKL------LLKEEVE--------------------DLKRKLEREEKYREEAATLELEK-EKLEQELQSW 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1418 KQLAEVHAKAIAKAEKEAQELKLRMQEEVNRRED--AVVDAEKQKHNIQLELHE-----LKNLSEQQIMDKS-KQVDDAL 1489
Cdd:pfam05557 265 VKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEEnsSLTSSARQLEKARRELEQelaqyLKKIEDLNKKLKRhKALVRRL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1490 QSRVKI-EEEIRLIRLQLETTVKQKSTAESELKQLRdRAAEAEKLRKAAQEEAEKLRKQ--VNEET---QKKRMAEEELK 1563
Cdd:pfam05557 345 QRRVLLlTKERDGYRAILESYDKELTMSNYSPQLLE-RIEEAEDMTQKMQAHNEEMEAQlsVAEEElggYKQQAQTLERE 423
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1927222982 1564 RKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKE 1605
Cdd:pfam05557 424 LQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKN 465
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1681-1850 |
4.69e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1681 QKANEAlrlRLQAEEEAHKKSLAQEDAEKQKEEAEREAK---KRAKAEDSALKQKEMAE---------NELERQRKVAES 1748
Cdd:COG2268 221 REAEEA---ELEQEREIETARIAEAEAELAKKKAEERREaetARAEAEAAYEIAEANAErevqrqleiAEREREIELQEK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1749 TAQQKLTAEQELIRLRADfdnAEQQRslledelyrlkneVVAAQQQRKQLEDELAKVRSEMdvlIQLKSKAEKEtMSNSE 1828
Cdd:COG2268 298 EAEREEAELEADVRKPAE---AEKQA-------------AEAEAEAEAEAIRAKGLAEAEG---KRALAEAWNK-LGDAA 357
|
170 180
....*....|....*....|..
gi 1927222982 1829 RSKQLLEveatKMRDLAEEASK 1850
Cdd:COG2268 358 ILLMLIE----KLPEIAEAAAK 375
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1693-1940 |
4.72e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1693 AEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELirlrADFDNAEQ 1772
Cdd:PRK07735 18 AKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEV----TEEEKAKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1773 QRSLLEDELYR---LKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEAS 1849
Cdd:PRK07735 94 KAKAAAAAKAKaaaLAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1850 KLRAIA---EEAKHQRQ----VAEEEAARQRAEAERILKEKLAAI-----------SDATRLKTEAEIALKEKEAENERL 1911
Cdd:PRK07735 174 KAKAAAlakQKAAEAGEgteeVTEEEKAKAKAKAAAAAKAKAAALakqkasqgngdSGDEDAKAKAIAAAKAKAAAAARA 253
|
250 260 270
....*....|....*....|....*....|....*.
gi 1927222982 1912 RRQA-----EDEAYQRKALEDQA--NQHKQQIEEKI 1940
Cdd:PRK07735 254 KTKGaegkkEEEPKQEEPSVNQPylNKYVEVIKEKL 289
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2060-2216 |
4.72e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2060 KKKAEEARKQKDDADKEAEKQILMAqqAAQKCSAAEQQVQSVLAQQKEDTIMQTKlKEEYEKAKKLAKQAEAAKEKAERE 2139
Cdd:PRK07735 68 KAKAAALAKQKREGTEEVTEEEKAK--AKAKAAAAAKAKAAALAKQKREGTEEVT-EEEKAAAKAKAAAAAKAKAAALAK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2140 -----AALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEmAKHKKLAEQTL 2214
Cdd:PRK07735 145 qkregTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAK-AKAAALAKQKA 223
|
..
gi 1927222982 2215 KQ 2216
Cdd:PRK07735 224 SQ 225
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1032-1594 |
4.76e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1032 SEIKDLRLRIEDCEAgtvariRRPVEKEPLKECVQKTTEQKKVQVELEGLKKDLNKVSAkTKEVLASPQQTASAPVlrSE 1111
Cdd:PRK02224 213 SELAELDEEIERYEE------QREQARETRDEADEVLEEHEERREELETLEAEIEDLRE-TIAETEREREELAEEV--RD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1112 LDLTVEKM--DHTHMLSSVYLEKL--KTVEMVIRNTQGAEgvlKQYEDCLREVHTVPNDV-KEVETYRTKLKKMRAEAEG 1186
Cdd:PRK02224 284 LRERLEELeeERDDLLAEAGLDDAdaEAVEARREELEDRD---EELRDRLEECRVAAQAHnEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1187 EQPVFDSLEAELKKA-TAVSDKMSRVhserdAELDhyrqllsslqdrwkavfSQIDLRQRELEQLGRQLGYYRESYDWLI 1265
Cdd:PRK02224 361 LREEAAELESELEEArEAVEDRREEI-----EELE-----------------EEIEELRERFGDAPVDLGNAEDFLEELR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1266 RWINDAKQRQEKIQAvtitDSKTLKEQLAQEKKLLEEvegnkDKVDECQKYAK--AYIDTIKDYELQLVAYKAQVEPLAS 1343
Cdd:PRK02224 419 EERDELREREAELEA----TLRTARERVEEAEALLEA-----GKCPECGQPVEgsPHVETIEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1344 PLKK--TKLDSASDNIIQE--YVTLRTKYSELMTLTSQYIKFITDSQRRLEDEEKAAEKLKAEEQKKmammQAELDKQKQ 1419
Cdd:PRK02224 490 EVEEveERLERAEDLVEAEdrIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK----REAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1420 LAEVHAKAIAKAEKEAQELKLRMqEEVNRREDAVVDAEKQKHNIQLELHELKNLSEQQimDKSKQVDDALQSRVKieeei 1499
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAELN--DERRERLAEKRERKR----- 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1500 rlirlQLETTVKqkstaESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRkAEAEKEAAKQKQKA 1579
Cdd:PRK02224 638 -----ELEAEFD-----EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE-LEELRERREALENR 706
|
570
....*....|....*
gi 1927222982 1580 LEDLENLKRQAEEAE 1594
Cdd:PRK02224 707 VEALEALYDEAEELE 721
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2336-2508 |
4.82e-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: 41.83 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2336 DLNQQRALAD--KMLKEKMQAIQEASRLRAEAEMLQRQKDLAQ---EQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKR 2410
Cdd:COG1579 2 MPEDLRALLDlqELDSELDRLEHRLKELPAELAELEDELAALEarlEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2411 QLEIIA--ESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETElatqekmtvvEKLEVARLTSSKEADDLRKAI 2488
Cdd:COG1579 82 LGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE----------AELAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|
gi 1927222982 2489 ADLEKEKSRLKKEAEDLQNK 2508
Cdd:COG1579 152 AELEAELEELEAEREELAAK 171
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1648-1874 |
5.11e-03 |
|
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: 42.53 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1648 VLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKAnEALRLRLQAEEEAHKKSLAQEDAEKQKEEAE--REAKKRAKAE 1725
Cdd:TIGR02794 42 LVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQA-EEAEKQRAAEQARQKELEQRAAAEKAAKQAEqaAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1726 DSALKQKEMAEN----ELERQRKVAESTAQQkltAEQElirlrADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDE 1801
Cdd:TIGR02794 121 AEEAKAKQAAEAkakaEAEAERKAKEEAAKQ---AEEE-----AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927222982 1802 LAKVRSEmdvliQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRA 1874
Cdd:TIGR02794 193 EAKAKAE-----AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1714-2022 |
5.34e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1714 AEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQ 1793
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1794 QRKQLEDELAKVRSEMDVLIQLKSKAEKEtmsnSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQR 1873
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEE----AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1874 AEAERILKE-KLAAISDATRLKTEAEIALKEKEAE-NERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEM 1951
Cdd:COG4372 157 EQLESLQEElAALEQELQALSEAEAEQALDELLKEaNRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222982 1952 ERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLAL 2022
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2561-2636 |
5.41e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.25 E-value: 5.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222982 2561 KKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMhnkQKEMKELERKRLEQERILAEENQKLREKLQQ 2636
Cdd:pfam03938 26 KKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQEL---QKKEQELQQLQQKAQQELQKKQQELLQPIQD 98
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2345-2632 |
5.66e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2345 DKMLKEKMQAIQEaSRLRAEAEMLQRQKDLAQEQAqkllEDKQLMQQRLDEETEEYQKSLEAERKRQLEI----IAESEK 2420
Cdd:pfam02029 61 EEAFLDRTAKREE-RRQKRLQEALERQKEFDPTIA----DEKESVAERKENNEEEENSSWEKEEKRDSRLgrykEEETEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2421 LKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVE-KLEVARLTSSKEADDLRKAIADLEKEKSRLK 2499
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKiKKEKKVKYESKVFLDQKRGHPEVKSQNGEEE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2500 KEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRL-ESQFEEEVKKAKALKDEQERQKQQME 2578
Cdd:pfam02029 216 VTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLrQKQQEAELELEELKKKREERRKLLEE 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1927222982 2579 DEKKKLQATMDaalnkQKEAEKEMHNKQKEmkELERKRLEQerilAEENQKLRE 2632
Cdd:pfam02029 296 EEQRRKQEEAE-----RKLREEEEKRRMKE--EIERRRAEA----AEKRQKLPE 338
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
408-582 |
6.15e-03 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 42.67 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 408 GRLHVAILERERLLRIEFERLERLQRIvSKVQMESGLCDEQLSHLETLLQMD-------IRLLSAGKPAQHTAEVERELD 480
Cdd:COG3914 92 GRYEEALALYRRALALNPDNAEALFNL-GNLLLALGRLEEALAALRRALALNpdfaeayLNLGEALRRLGRLEEAIAALR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 481 KAV----NMIRLLFNDVQVLKD-GRHPQAEQMYRRVYRLDERLVNLRSDY-NLRLKSAVTTVKVPMQQTTQQTMKVRPEL 554
Cdd:COG3914 171 RALeldpDNAEALNNLGNALQDlGRLEEAIAAYRRALELDPDNADAHSNLlFALRQACDWEVYDRFEELLAALARGPSEL 250
|
170 180
....*....|....*....|....*...
gi 1927222982 555 DDVTLRYIQDLLAWVEENQHRideaQWG 582
Cdd:COG3914 251 SPFALLYLPDDDPAELLALAR----AWA 274
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2329-2521 |
6.17e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2329 LRQIAE--DDLNQQRALADKmlkEKMQAIQEASRLRAEAEmlqrqkdLAQEQAQKLLEDKQLmQQRLDEETEEYQksLEA 2406
Cdd:COG2268 191 RRKIAEiiRDARIAEAEAER---ETEIAIAQANREAEEAE-------LEQEREIETARIAEA-EAELAKKKAEER--REA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2407 ERKRqleIIAEseklklqvsqlsEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLevarltsskEADDLRK 2486
Cdd:COG2268 258 ETAR---AEAE------------AAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAEL---------EADVRKP 313
|
170 180 190
....*....|....*....|....*....|....*
gi 1927222982 2487 AIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIE 2521
Cdd:COG2268 314 AEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAE 348
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3833-3866 |
6.23e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.08 E-value: 6.23e-03
10 20 30
....*....|....*....|....*....|....
gi 1927222982 3833 LEAQTATGGIIDPEFQFHLPADVAMQRGYINKET 3866
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1364-1554 |
6.31e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1364 LRTKYSELMTLTSQyIKFITDSQRRLEDEEKAAEKLKAeEQKKMAMMQAE-------------LDKQKQLA------EVH 1424
Cdd:PRK11637 91 LRETQNTLNQLNKQ-IDELNASIAKLEQQQAAQERLLA-AQLDAAFRQGEhtglqlilsgeesQRGERILAyfgylnQAR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1425 AKAIAKAEKEAQELKLRMQEEVnrredavvdaekQKHNIQLELhelknLSEQQimDKSKQVDDALQSRVKIEEEirlirl 1504
Cdd:PRK11637 169 QETIAELKQTREELAAQKAELE------------EKQSQQKTL-----LYEQQ--AQQQKLEQARNERKKTLTG------ 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222982 1505 qLETTVKQKSTAESELKQ----LRDRAAEAEKLRKAAQE----EAEKLRKQVNEETQK 1554
Cdd:PRK11637 224 -LESSLQKDQQQLSELRAnesrLRDSIARAEREAKARAErearEAARVRDKQKQAKRK 280
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1390-1791 |
6.48e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.82 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1390 EDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKlRMQEEVNRREDAVVDAEKQ-----KHNIQ 1464
Cdd:pfam09731 100 EVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAK-EAKDDAIQAVKAHTDSLKEasdtaEISRE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1465 LELHELKNLSEQQIMDKSKQVDDALQSrvkieeeirlirlQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEA--- 1541
Cdd:pfam09731 179 KATDSALQKAEALAEKLKEVINLAKQS-------------EEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAklv 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1542 EKLRKQVNEETQKKRMaeeELKRKAEAEKEAAKQKQKALEDleNLKRQAEEAERQVKQAEiekeRQIQVAHVAAQKSAAA 1621
Cdd:pfam09731 246 DQYKELVASERIVFQQ---ELVSIFPDIIPVLKEDNLLSND--DLNSLIAHAHREIDQLS----KKLAELKKREEKHIER 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1622 ELQSKHMSFvektSKLEESLKQEhgavlqLQHEAAALKKQqedaerAREEAEKELEKWRQKANEALRLRLQAEEEAHKKS 1701
Cdd:pfam09731 317 ALEKQKEEL----DKLAEELSAR------LEEVRAADEAQ------LRLEFEREREEIRESYEEKLRTELERQAEAHEEH 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1702 LAQEDAEkQKEEAEREAKKRAK---AEDSALKQKEMAE-----NELERQ---RKVAESTAQ--QKLTAEQELIRLRADFD 1768
Cdd:pfam09731 381 LKDVLVE-QEIELQREFLQDIKekvEEERAGRLLKLNEllanlKGLEKAtssHSEVEDENRkaQQLWLAVEALRSTLEDG 459
|
410 420
....*....|....*....|....*...
gi 1927222982 1769 NAEQQRSLLEDELYRLK-----NEVVAA 1791
Cdd:pfam09731 460 SADSRPRPLVRELKALKelasdDEVVKA 487
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
2114-2204 |
6.50e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 42.55 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2114 KLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAaaeqeaanqakaQEDAERLRKEAEFEAAKRAQAENAAL 2193
Cdd:PRK12472 194 TLAREAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKA------------RADAELKRADKALAAAKTDEAKARAE 261
|
90
....*....|.
gi 1927222982 2194 KQKQQADAEMA 2204
Cdd:PRK12472 262 ERQQKAAQQAA 272
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2230-2521 |
6.50e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2230 KLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKdkdntqkflakeadnM 2309
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREK---------------R 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2310 KKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQaIQEASRLRAEAEMLQRQKDLAQEqaqkllEDKQLM 2389
Cdd:COG1340 67 DELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGS-IDKLRKEIERLEWRQQTEVLSPE------EEKELV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2390 QQ--RLDEETEEYQKSLEAERKRQlEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHET-ELATQEKMTV 2466
Cdd:COG1340 140 EKikELEKELEKAKKALEKNEKLK-ELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELrKEADELHKEI 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222982 2467 VEKLEVARLTsSKEADDLRKAIADLEKEKSRLKKEAEDLQ-NKSKEMADAQQKQIE 2521
Cdd:COG1340 219 VEAQEKADEL-HEEIIELQKELRELRKELKKLRKKQRALKrEKEKEELEEKAEEIF 273
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2366-2524 |
6.67e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2366 EMLQRQKDLAQEQ-AQKLLEdkqlmQQRLDEETEEyqkslEAERKRQLEIIAESEKLklQVSQLSEAQAKAQEEAKKFKK 2444
Cdd:PTZ00491 665 EAAARHQAELLEQeARGRLE-----RQKMHDKAKA-----EEQRTKLLELQAESAAV--ESSGQSRAEALAEAEARLIEA 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2445 QADsiasrlhetelatqekmtvvekLEVARLTSskEADDLRKAiADLEKEKSRLKKEAEDLQ-------NKSKEMADaqq 2517
Cdd:PTZ00491 733 EAE----------------------VEQAELRA--KALRIEAE-AELEKLRKRQELELEYEQaqneleiAKAKELAD--- 784
|
....*..
gi 1927222982 2518 kqIEHEK 2524
Cdd:PTZ00491 785 --IEATK 789
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2320-2502 |
6.72e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.63 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2320 SVEAQEAARLRQIAEDDLNQQRALADKMLKEKMqaiqEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEE 2399
Cdd:pfam15709 316 SEEDPSKALLEKREQEKASRDRLRAERAEMRRL----EVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2400 YQKSLEAERKRQ--------LEIIAESEKLKLQVSQ----LSEAQAKAQEEAKKfKKQADSIASRLHETELATQEK---- 2463
Cdd:pfam15709 392 RKQRLEEERQRQeeeerkqrLQLQAAQERARQQQEEfrrkLQELQRKKQQEEAE-RAEAEKQRQKELEMQLAEEQKrlme 470
|
170 180 190
....*....|....*....|....*....|....*....
gi 1927222982 2464 MTVVEKLEVARLTSSKEADdlrkaiADLEKEKSRLKKEA 2502
Cdd:pfam15709 471 MAEEERLEYQRQKQEAEEK------ARLEAEERRQKEEE 503
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1386-1662 |
6.78e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1386 QRRLEDEEKAAEKLkaEEQkkmAMMQAELDKQKQLAEVHAKAiakAEKEAQELK-----------------LRMQEEVNR 1448
Cdd:COG3096 350 ERYQEDLEELTERL--EEQ---EEVVEEAAEQLAEAEARLEA---AEEEVDSLKsqladyqqaldvqqtraIQYQQAVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1449 REDA---VVDAEKQKHNIQLELHELKN---------LSEQQIMDKSK----QVDDALQSRVKIEEEI------RLIRLQL 1506
Cdd:COG3096 422 LEKAralCGLPDLTPENAEDYLAAFRAkeqqateevLELEQKLSVADaarrQFEKAYELVCKIAGEVersqawQTARELL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1507 ETTVKQKSTAEsELKQLRDRAAEAEKlRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKAL----ED 1582
Cdd:COG3096 502 RRYRSQQALAQ-RLQQLRAQLAELEQ-RLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAaeavEQ 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1583 LENLKRQAEEAERQVKQ----AEIEKERQIQVAHVAAQKSAAAElqskhmSFVEKTSKLEESLKQEHGAVLQLQHEAAal 1658
Cdd:COG3096 580 RSELRQQLEQLRARIKElaarAPAWLAAQDALERLREQSGEALA------DSQEVTAAMQQLLEREREATVERDELAA-- 651
|
....
gi 1927222982 1659 KKQQ 1662
Cdd:COG3096 652 RKQA 655
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2054-2153 |
6.83e-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: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2054 DELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAK 2133
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQALREELNELKAEIAELKAEA 80
|
90 100
....*....|....*....|
gi 1927222982 2134 EKAEREAALLRQQAEEAERQ 2153
Cdd:pfam07926 81 ESAKAELEESEESWEEQKKE 100
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2372-2644 |
6.83e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.71 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2372 KDLAQEQAQKLLEDKQLMQQRLDEEteEYQKsleaeRKRQleiiaesEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIAS 2451
Cdd:pfam05667 214 AELAAAQEWEEEWNSQGLASRLTPE--EYRK-----RKRT-------KLLKRIAEQLRSAALAGTEATSGASRSAQDLAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2452 RLHE--------TELATQEKMTVVEKLEVAR---------LTSSKEADDLRKAiadLEKEKSRLKKEAEDLQNKSKEMad 2514
Cdd:pfam05667 280 LLSSfsgssttdTGLTKGSRFTHTEKLQFTNeapaatsspPTKVETEEELQQQ---REEELEELQEQLEDLESSIQEL-- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2515 aqQKQIEHEKTVLQQTFLSEKEMllkkekliEEEKKRLESQFEEEVKKAKALKDEQErqkqQMEDEKKKLQATMDAALNK 2594
Cdd:pfam05667 355 --EKEIKKLESSIKQVEEELEEL--------KEQNEELEKQYKVKKKTLDLLPDAEE----NIAKLQALVDASAQRLVEL 420
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1927222982 2595 QKEAEK---EMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEE--AQKDQ 2644
Cdd:pfam05667 421 AGQWEKhrvPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEeaKQKEE 475
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2210-2441 |
6.87e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2210 AEQTLKQKFQVEQELTKVKLKLDETDKQKSV----------LDEELQRLKDEVDDAVKQRGQVEEEL-LKVKVQMEELLK 2278
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLSETDARIKLaaqekihveiLEEQLEKLRNELLIRGATEGLCVHSLsKELDVLKEENML 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2279 LKLRIEEENQRLIK-KDKDNTQKFLAKEADNMK-KLAEDAARLSVEAQEAARLRQIaeddlnQQRALADKMlkEKMQAIQ 2356
Cdd:PLN02939 238 LKDDIQFLKAELIEvAETEERVFKLEKERSLLDaSLRELESKFIVAQEDVSKLSPL------QYDCWWEKV--ENLQDLL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2357 EASRLRAE--AEMLQRQKDLaQEQAQKL-------------LEDKQLMQQRLDEETEEYQKSlEAERKRQLEIIAESekl 2421
Cdd:PLN02939 310 DRATNQVEkaALVLDQNQDL-RDKVDKLeaslkeanvskfsSYKVELLQQKLKLLEERLQAS-DHEIHSYIQLYQES--- 384
|
250 260
....*....|....*....|
gi 1927222982 2422 klqVSQLSEAQAKAQEEAKK 2441
Cdd:PLN02939 385 ---IKEFQDTLSKLKEESKK 401
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2344-2455 |
6.93e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.79 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2344 ADKMLKEKMQAIQEAsrlRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEiiaesEKLKL 2423
Cdd:cd16269 189 ADQALTEKEKEIEAE---RAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLK-----EQERA 260
|
90 100 110
....*....|....*....|....*....|..
gi 1927222982 2424 QVSQLSEAQAKAQEEakkFKKQADSIASRLHE 2455
Cdd:cd16269 261 LESKLKEQEALLEEG---FKEQAELLQEEIRS 289
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2437-2650 |
7.09e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2437 EEAKKFKKQADSIASRLHETELATQEKMTVVEKLevarltsSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQ 2516
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEI-------SSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2517 Q-KQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQfEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQ 2595
Cdd:PRK03918 252 GsKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK-AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2596 KEAEK---EMHNKQKEMKELERK--RLEQERILAEENQKLREKLQQLEEAQKDQPDKEVI 2650
Cdd:PRK03918 331 KELEEkeeRLEELKKKLKELEKRleELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2258-2601 |
7.30e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2258 QRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSveaQEAARLRQIAEDDL 2337
Cdd:COG5185 204 VNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLR---LEKLGENAESSKRL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2338 NQQRALADKMLKEKMQAIQEasrlRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQksLEAERKRQLEIIAE 2417
Cdd:COG5185 281 NENANNLIKQFENTKEKIAE----YTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQN--LTAEIEQGQESLTE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2418 S-EKLKLQVSQL--SEAQAKAQEEAKKFKKQADSIASRLHE--TELATQEKMtVVEKLEVARLTSSKEADDLRKAIADLE 2492
Cdd:COG5185 355 NlEAIKEEIENIvgEVELSKSSEELDSFKDTIESTKESLDEipQNQRGYAQE-ILATLEDTLKAADRQIEELQRQIEQAT 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2493 ---KEKSRLKKEA-EDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEmllkkekLIEEEKKRLESQFEEEVKKAKALKD 2568
Cdd:COG5185 434 ssnEEVSKLLNELiSELNKVMREADEESQSRLEEAYDEINRSVRSKKE-------DLNEELTQIESRVSTLKATLEKLRA 506
|
330 340 350
....*....|....*....|....*....|...
gi 1927222982 2569 EQERQKQQMEDEKKKLQATMDAALNKQKEAEKE 2601
Cdd:COG5185 507 KLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1631-1840 |
7.64e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1631 VEKTSKLEESLKQeHGAVLQLQHEAAALKKQqedaerareeaekelekwrqkanealRLRLQAEEEAHKKSLAQEDAEKQ 1710
Cdd:PTZ00491 657 IEITTKSQEAAAR-HQAELLEQEARGRLERQ--------------------------KMHDKAKAEEQRTKLLELQAESA 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1711 KEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAEstaqqKLTAEQELirlradfdnaeqqrslledelyrlknevvA 1790
Cdd:PTZ00491 710 AVESSGQSRAEALAEAEARLIEAEAEVEQAELRAKAL-----RIEAEAEL-----------------------------E 755
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1791 AQQQRKQLEDELAKVRSEMDVliqlkskaeketmsnsERSKQLLEVEATK 1840
Cdd:PTZ00491 756 KLRKRQELELEYEQAQNELEI----------------AKAKELADIEATK 789
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1524-1717 |
8.10e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1524 RDRAAEAEKLRKaaqeEAEKLRKqvnEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLEnLKRQAEEAERQvKQAEIE 1603
Cdd:pfam15709 337 RLRAERAEMRRL----EVERKRR---EQEEQRRLQQEQLERAEKMREELELEQQRRFEEIR-LRKQRLEEERQ-RQEEEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1604 KERQIQVAhvAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEaAALKKQQEDAERAREEAEKELEKWRQKA 1683
Cdd:pfam15709 408 RKQRLQLQ--AAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKE-LEMQLAEEQKRLMEMAEEERLEYQRQKQ 484
|
170 180 190
....*....|....*....|....*....|....*...
gi 1927222982 1684 NEALRLRLQAEEEAHKKS----LAQEDAEKQKEEAERE 1717
Cdd:pfam15709 485 EAEEKARLEAEERRQKEEeaarLALEEAMKQAQEQARQ 522
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1680-1906 |
8.12e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.24 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1680 RQKANEAlRLRLQA------EEEAHKKSLAQEDAEKQKEEAER---EAKKRAKAEDSALKQKEMAENELERQRKVAESTA 1750
Cdd:PRK05035 445 KKKAEEA-KARFEArqarleREKAAREARHKKAAEARAAKDKDavaAALARVKAKKAAATQPIVIKAGARPDNSAVIAAR 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1751 QQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEvVAAQQQ-----RKQLEDELAKVRSEMdvliqLKSKAEKETMS 1825
Cdd:PRK05035 524 EARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAK-KAAQQAanaeaEEEVDPKKAAVAAAI-----ARAKAKKAAQQ 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1826 NSERSKQLLEVEATKMRDLAEEASKlRAIAEEAKHQR--QVAEEEAARQRAEAERI--LKEKLAAISDATRLKTEAEIAL 1901
Cdd:PRK05035 598 AASAEPEEQVAEVDPKKAAVAAAIA-RAKAKKAEQQAnaEPEEPVDPRKAAVAAAIarAKARKAAQQQANAEPEEAEDPK 676
|
....*
gi 1927222982 1902 KEKEA 1906
Cdd:PRK05035 677 KAAVA 681
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
2087-2360 |
8.13e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 42.36 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2087 AAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAK 2166
Cdd:pfam04747 56 ASLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEARRAEAEAKKRAAQEEEHKQWKAEQERIQKEQEK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2167 AQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKqksvldEELQ 2246
Cdd:pfam04747 136 KEADLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTPTNTPAEPA------EQVQ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2247 RLKDEVDDAVKQRGQVEEELLKVKVQmEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEA 2326
Cdd:pfam04747 210 EITGKKNKKNKKKSESEATAAPASVE-QVVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASETPVEPVVETTPP 288
|
250 260 270
....*....|....*....|....*....|....
gi 1927222982 2327 ARLRQiAEDDLNQQRALADKMLKEKMQAIQEASR 2360
Cdd:pfam04747 289 ASENQ-KKNKKDKKKSESEKVVEEPVQAEAPKSK 321
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2348-2518 |
8.19e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2348 LKEKMQAIQEASRLRAEAEM-LQRQKDLAQEQAQKLLEDKQLMQ-QRLDEETEEYQKSLE--AERKRQLEiiAESEKLKL 2423
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKeAEEKLEAALLEAKELLLRERNQQrQEARREREELQREEErlVQKEEQLD--ARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2424 QVSQLSEAQakaqeeaKKFKKQADSIASRLHETELatqekmtvvEKLEVARLTSSKEADDLrkaIADLEKEksrLKKEAE 2503
Cdd:PRK12705 103 LENQLEERE-------KALSARELELEELEKQLDN---------ELYRVAGLTPEQARKLL---LKLLDAE---LEEEKA 160
|
170
....*....|....*
gi 1927222982 2504 DLQNKSKEMADAQQK 2518
Cdd:PRK12705 161 QRVKKIEEEADLEAE 175
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2190-2327 |
8.27e-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: 41.06 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2190 NAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDE-TDKQKSVLDE-ELQRLKDEVDDAVKQRGQVEEELL 2267
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyEEQLGNVRNNkEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2268 KVkvqMEELLKLKLRIEEENQRLIKKDKDNTQKfLAKEADNMKKLAEDAARLSVEAQEAA 2327
Cdd:COG1579 114 EL---MERIEELEEELAELEAELAELEAELEEK-KAELDEELAELEAELEELEAEREELA 169
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2194-2380 |
8.61e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2194 KQKQQADAEMAKHKKLAEQT--LKQKFQVEQELTKV--KLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKV 2269
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAeeLQQKQAAEQERLKQleKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2270 KVQMEELLKLKLRIEEENQrliKKDKDNTQKFLAKEAdnmKKLAEDAARLSVEAQEAARLRQIAE---DDLNQQRALADK 2346
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAK---KKAEAEAAKKAAAEA---KKKAEAEAAAKAAAEAKKKAEAEAKkkaAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....
gi 1927222982 2347 mlKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQ 2380
Cdd:PRK09510 224 --KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1741-1931 |
8.75e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.16 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1741 RQRKVAESTAQQKLTAEQELIRLRADFD-NAEQQRSLLEDELYRLKNEVV--AAQQQRKQLEDELAKVRSEMDVLIQLKS 1817
Cdd:PRK00106 25 KMKSAKEAAELTLLNAEQEAVNLRGKAErDAEHIKKTAKRESKALKKELLleAKEEARKYREEIEQEFKSERQELKQIES 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1818 KAEKETMSNSERSKQLLEVEatKMRDlaeeaSKLRAIAEEAKH----QRQVAEEEAaRQRAEAERI----LKEKLAAISD 1889
Cdd:PRK00106 105 RLTERATSLDRKDENLSSKE--KTLE-----SKEQSLTDKSKHiderEEQVEKLEE-QKKAELERVaalsQAEAREIILA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1927222982 1890 ATRLKTEAEIALKEKEAENE---RLRRQAED---EAYQRKALEDQANQ 1931
Cdd:PRK00106 177 ETENKLTHEIATRIREAEREvkdRSDKMAKDllaQAMQRLAGEYVTEQ 224
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
2128-2222 |
8.82e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 39.60 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2128 QAEAAK--EKAEREAALLRQQAEEAERQkaaaeqEAANQAKAQEDAERLRKEAEFEAAKRAQAenaalkQKQQADAEMAK 2205
Cdd:PRK07353 45 RAEAKErlAEAEKLEAQYEQQLASARKQ------AQAVIAEAEAEADKLAAEALAEAQAEAQA------SKEKARREIEQ 112
|
90
....*....|....*..
gi 1927222982 2206 HKKLAEQTLKQkfQVEQ 2222
Cdd:PRK07353 113 QKQAALAQLEQ--QVDA 127
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2081-2480 |
9.58e-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: 42.25 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2081 ILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEeyeKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQE 2160
Cdd:COG5185 187 GLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLE---KAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2161 AANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLD-ETDKQKS 2239
Cdd:COG5185 264 DLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETEtGIQNLTA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2240 VLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQmEELLKLKLRIEEENQRLIKKDKD---NTQKFLAKEADNMKKLAEDA 2316
Cdd:COG5185 344 EIEQGQESLTENLEAIKEEIENIVGEVELSKSS-EELDSFKDTIESTKESLDEIPQNqrgYAQEILATLEDTLKAADRQI 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2317 ARL-------SVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQaiqeaSRLRAEAEMLQRQKDLAQEQAQKLLEDKQLM 2389
Cdd:COG5185 423 EELqrqieqaTSSNEEVSKLLNELISELNKVMREADEESQSRLE-----EAYDEINRSVRSKKEDLNEELTQIESRVSTL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2390 QQRLDEETEEYQKSLEAERKrQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEK 2469
Cdd:COG5185 498 KATLEKLRAKLERQLEGVRS-KLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQY 576
|
410
....*....|.
gi 1927222982 2470 LEVARLTSSKE 2480
Cdd:COG5185 577 LSTIESQQARE 587
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
2398-2580 |
9.62e-03 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 41.86 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2398 EEYQKSLEAERKRQLEIIAEsEKLKLQVSQLsEAQAKAQEEAKKFKKQADSIASRLHETElatqekmtvVEKLEVARLTS 2477
Cdd:COG4487 25 KQRRAEFEKELAERLADAAK-REAALELAEA-KAKAQLQEQVAEKDAEIAELRARLEAEE---------RKKALAVAEEK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2478 SKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRL-ESQF 2556
Cdd:COG4487 94 EKELAALQEALAEKDAKLAELQAKELELLKKERELEDAKREAELTVEKERDEELDELKEKLKKEEEEKQLAEKSLkVAEY 173
|
170 180
....*....|....*....|....*...
gi 1927222982 2557 EEEVKKAK----ALKDEQERQKQQMEDE 2580
Cdd:COG4487 174 EKQLKDMQeqieELKRKKEQGSTQLQGE 201
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1697-2021 |
9.83e-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: 41.44 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1697 AHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKltaeqelirlradfdnaeQQRSL 1776
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEER------------------EQKRQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1777 LEDELYRLKNEVVAAQQQRKQLEDELAKvrsemdvliQLKSKAEKETMSNSERSKQLLEV--EATKMRDLAEEASKLRAI 1854
Cdd:pfam13868 91 EEYEEKLQEREQMDEIVERIQEEDQAEA---------EEKLEKQRQLREEIDEFNEEQAEwkELEKEEEREEDERILEYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1855 AEEAKHQRQVAEEEAARQRAEAERI--LKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQH 1932
Cdd:pfam13868 162 KEKAEREEEREAEREEIEEEKEREIarLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 1933 KQQIEEKIVLLkkssEAEMERQRAivdDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEET-QQSKLRAE 2011
Cdd:pfam13868 242 EEQIELKERRL----AEEAEREEE---EFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQrAAEREEEL 314
|
330
....*....|
gi 1927222982 2012 EEAEKLRKLA 2021
Cdd:pfam13868 315 EEGERLREEE 324
|
|
| vATP-synt_E |
pfam01991 |
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ... |
2166-2308 |
9.91e-03 |
|
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as well as the archaebacterial ATP synthase E subunit.
Pssm-ID: 396537 [Multi-domain] Cd Length: 199 Bit Score: 40.44 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222982 2166 KAQEDAERLRKEAEFEAAKraqaENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETdkQKSVLDEEL 2245
Cdd:pfam01991 5 EAEEKAEEIRAKAEEEFAI----EKAELVQEAEEKIDEIYEKKEKQAEMQKKIIISNAKNEARLKVLEA--REEILDEVF 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222982 2246 QRLKDEVDDAVKQRGQVEEELLKVKVQ-MEELL--KLKLRIEEENQRLIKKDKDNTQKFLAKEADN 2308
Cdd:pfam01991 79 NEAEKKLAELEEDTDEYKDLLRKLIVQaLVKLGepEVIVRCRKRDEELVESALDKAAEEYKAKTKK 144
|
|
| |
