|
Name |
Accession |
Description |
Interval |
E-value |
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
19-135 |
2.91e-73 |
|
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: 240.00 E-value: 2.91e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 19 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprekGRMRFHKLQNVQIALD 98
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRER------------GRMRFHRLQNVQTALD 68
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237982 99 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 135
Cdd:cd21188 69 FLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
16-146 |
2.02e-70 |
|
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409084 Cd Length: 119 Bit Score: 232.61 E-value: 2.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 16 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpreKGRMRFHKLQNVQI 95
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE------------KGRMRFHKLQNVQI 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1920237982 96 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 146
Cdd:cd21235 69 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
148-253 |
1.14e-69 |
|
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: 229.91 E-value: 1.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 148 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 227
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1920237982 228 PEDVDVPQPDEKSIITYVSSLYDAMP 253
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
15-144 |
5.85e-69 |
|
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: 228.72 E-value: 5.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 15 KDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpreKGRMRFHKLQNVQ 94
Cdd:cd21236 11 KDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPRE------------KGRMRFHRLQNVQ 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1920237982 95 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 144
Cdd:cd21236 79 IALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
149-253 |
3.98e-64 |
|
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: 213.79 E-value: 3.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 149 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 228
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1920237982 229 EDVDVPQPDEKSIITYVSSLYDAMP 253
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
16-145 |
1.91e-60 |
|
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: 204.11 E-value: 1.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 16 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGdslprerdvirsSRLPREKGRMRFHKLQNVQI 95
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSG------------VKLPREKGRMRFHRLQNVQI 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1920237982 96 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 145
Cdd:cd21237 69 ALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
149-253 |
1.42e-56 |
|
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: 192.51 E-value: 1.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 149 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 228
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1920237982 229 EDVDVPQPDEKSIITYVSSLYDAMP 253
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
147-253 |
6.24e-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: 173.30 E-value: 6.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 147 DMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 226
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1920237982 227 DPEDVDVPQPDEKSIITYVSSLYDAMP 253
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
21-136 |
9.79e-48 |
|
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: 167.17 E-value: 9.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 21 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGdslprerdvirsSRLPREKGRMRFHKLQNVQIALDY 99
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTG------------KKLKPEKGRMRVHHLNNVNRALQV 69
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237982 100 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 136
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 ... |
11-132 |
6.03e-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: 6.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 11 ISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMRFHKL 90
Cdd:cd21246 6 IKALADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKP-----------TKGKMRIHCL 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237982 91 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 132
Cdd:cd21246 75 ENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
149-249 |
6.64e-45 |
|
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: 159.11 E-value: 6.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 149 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 228
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1920237982 229 EDVDVPQPDEKSIITYVSSLY 249
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
11-132 |
1.21e-43 |
|
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: 155.92 E-value: 1.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 11 ISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMRFHKL 90
Cdd:cd21193 6 IRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKP-----------NRGRLRVQKI 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237982 91 QNVQIALDYLrHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 132
Cdd:cd21193 75 ENVNKALAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
20-360 |
3.21e-43 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 170.12 E-value: 3.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 20 RVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLprerdvIRSSRLPRekgrMRFHKLQNVQIALD 98
Cdd:COG5069 8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNA------GEYNETPE----TRIHVMENVSGRLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 99 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGCQ-GLRCDNFTTSW 177
Cdd:COG5069 78 FIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 178 RDGRLFNAIIHRHKPTLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS------SL 248
Cdd:COG5069 155 RDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyiirfGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 249 YD----AMPRVPDVQDGVKANElQLRwQEYRELVLLLLQWIRAHTAGFEERRFPSSFEEIEILWCQFLKFKETE--LPAK 322
Cdd:COG5069 235 LEkidiALHRVYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCsrAPLE 312
|
330 340 350
....*....|....*....|....*....|....*....
gi 1920237982 323 EAD-KNRSKGIYQSLEgAVQAGQLKVPPGYHPLDVEKEW 360
Cdd:COG5069 313 TTDlHSLAGQILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
149-249 |
4.62e-43 |
|
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: 153.71 E-value: 4.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 149 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 228
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1920237982 229 EDVDVPQPDEKSIITYVSSLY 249
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
17-136 |
9.70e-42 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 150.22 E-value: 9.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 17 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDslprerdvirssRLPREKGRM--RFHKLQN 92
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGE------------KLPCEKGRRlkRVHFLSN 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1920237982 93 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 136
Cdd:cd21241 69 INTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
148-253 |
5.45e-41 |
|
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: 147.85 E-value: 5.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 148 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 227
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1920237982 228 PEDVDVPQPDEKSIITYVSSLYDAMP 253
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
17-136 |
7.37e-41 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 147.72 E-value: 7.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 17 ERDRVQKKTFTKWVNKHLikaQRH-----ISDLYEDLRDGHNLISLLEVLSGDslprerdvirssRLPREKGRM--RFHK 89
Cdd:cd21190 1 EQERVQKKTFTNWINSHL---AKLsqpivINDLFVDIKDGTALLRLLEVLSGQ------------KLPIESGRVlqRAHK 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237982 90 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 136
Cdd:cd21190 66 LSNIRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
136-251 |
8.61e-40 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 144.81 E-value: 8.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 136 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 215
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237982 216 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 251
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
11-132 |
1.94e-39 |
|
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: 144.78 E-value: 1.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 11 ISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMRFHKL 90
Cdd:cd21318 28 IKALADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKP-----------TRGRMRIHSL 96
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237982 91 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 132
Cdd:cd21318 97 ENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
11-132 |
2.74e-38 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 141.34 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 11 ISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMRFHKL 90
Cdd:cd21317 21 IKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKP-----------TKGRMRIHCL 89
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237982 91 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 132
Cdd:cd21317 90 ENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1292-1867 |
1.27e-37 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 156.25 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1292 DLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEErERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRM 1371
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE-AELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1372 QEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLrIEEEIRVVRLQLEATERQRGGAEGELQA 1451
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1452 LRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEA 1531
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1532 ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAtrraqqqaEAERARAEAERELERWQLK 1611
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL--------AGLRGLAGAVAVLIGVEAA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1612 ANEALRLRLQAeevAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIR 1691
Cdd:COG1196 536 YEAALEAALAA---ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1692 LRAETEQGEqqrqLLEEELARLQREAAAATqkRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfr 1771
Cdd:COG1196 613 ARYYVLGDT----LLGRTLVAARLEAALRR--AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE---- 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1772 ELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR 1851
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570
....*....|....*.
gi 1920237982 1852 RLLEEQAAQHKADIEA 1867
Cdd:COG1196 763 EELERELERLEREIEA 778
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
19-132 |
1.49e-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: 137.91 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 19 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerdvirssrlPREKGRMRFHKLQNVQIALD 98
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLP-----------KPERGKMRFHKIANVNKALD 71
|
90 100 110
....*....|....*....|....*....|....
gi 1920237982 99 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 132
Cdd:cd21214 72 FIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
145-249 |
2.06e-37 |
|
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: 138.27 E-value: 2.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 145 SEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 224
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1920237982 225 LLDPEDVDVPQPDEKSIITYVSSLY 249
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
145-249 |
4.46e-37 |
|
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: 137.06 E-value: 4.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 145 SEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 224
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1920237982 225 LLDPEDVDVPQPDEKSIITYVSSLY 249
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1320-2025 |
1.04e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 154.53 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1320 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSiqEELQHL 1399
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKA--EDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1400 RQSSEAEIQAKARQVEAAERSRlRIEEEIRVVRLQlEATERQRGGAEGELQALRaRAEEAeaqkRQAQEEAERLRRQVQD 1479
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDAR-KAEAARKAEEER-KAEEARKAEDAKKAEAVK-KAEEA----KKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1480 ETQRKRQAEAELALRVQAEAEAAREKQRAlqalEELRlQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASF 1559
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKA----DELK-KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1560 AEKTAQ-LERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEAlrlRLQAEEVAQQKSLTQaeaek 1638
Cdd:PTZ00121 1327 AKKKADaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA---KKKAEEKKKADEAKK----- 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1639 qkeeaerearrrgKAEEQAVRQRELAEQELEKQR-QLAEGTAQQRLAAEqELIRLRAETEQGEQQRQLLE-----EELAR 1712
Cdd:PTZ00121 1399 -------------KAEEDKKKADELKKAAAAKKKaDEAKKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEeakkaEEAKK 1464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1713 LQREAAAATQKRRELE----AELAKVRAEmevllASKARAEEESRSTSEKSKqrleAEAGRFRELAEEAARLRAlAEEAK 1788
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEeakkADEAKKKAE-----EAKKKADEAKKAAEAKKK----ADEAKKAEEAKKADEAKK-AEEAK 1534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1789 RQRQLAEEDAVRQRAEAERvlAEKLAAISEatrlKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEAR 1868
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKK--AEELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1869 LAQLRKASESELERQKGLVEDTLRQRrqveEEILALKGSFEKAAAGKAELELELGRIRGT-----AEDTLRSKEQA--EQ 1941
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKK----VEQLKKKEAEEKKKAEELKKAEEENKIKAAeeakkAEEDKKKAEEAkkAE 1684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1942 EAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE----VERLKAKVEEARRLRERAEQESARQLQLAQEAA 2017
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
....*...
gi 1920237982 2018 QKRLQAEE 2025
Cdd:PTZ00121 1765 EEEKKAEE 1772
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
21-134 |
1.24e-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: 135.61 E-value: 1.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 21 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprEKGRMRFHKLQNVQIALDYL 100
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYN----------KNPKMRVQKLENVNKALEFI 73
|
90 100 110
....*....|....*....|....*....|....
gi 1920237982 101 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 134
Cdd:cd21215 74 KSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1325-1926 |
1.89e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 152.40 E-value: 1.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1325 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKaQAEReAQGLQrrmqeevarreevaveAQEQKRSIQEELQHLRQSs 1403
Cdd:COG1196 177 AERKLEATEENLERLEDILgELERQLEPLERQAE-KAER-YRELK----------------EELKELEAELLLLKLREL- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1404 EAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQR 1483
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1484 KRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALEtaQRSAEAELQSEHASFAEKT 1563
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1564 AQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEA 1643
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1644 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIR------LRAETEQGEQQRQLLEEELARLQREA 1717
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgavavlIGVEAAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1718 AAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1797
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1798 AVRQRAEAERVLAEKLAA--ISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKA 1875
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGegGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1920237982 1876 SESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIR 1926
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
17-136 |
6.77e-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: 133.42 E-value: 6.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 17 ERDRVQKKTFTKWVNKHLIKAQ--RHISDLYEDLRDGHNLISLLEVLSGDslprerdvirssRLPREKGRMRFHKLQNVQ 94
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQ------------QLPREKGHNVFQCRSNIE 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237982 95 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 136
Cdd:cd21242 69 TALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
148-249 |
1.15e-35 |
|
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: 132.68 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 148 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 227
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1920237982 228 PEDVDVPQPDEKSIITYVSSLY 249
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1452-2052 |
3.95e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 148.16 E-value: 3.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1452 LRARAEEAEAQKRQAQEEAERL---RRQVqdETQR---KRQAE-AELALRVQAEAEAaREKQRALQALEELRLQAEEAER 1524
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLeplERQAEkAERYRELKEELKE-LEAELLLLKLRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1525 RLRQAEAERARqvqvaLETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAvvQLREEATRRAQQQAEAERARAEAERE 1604
Cdd:COG1196 247 ELEELEAELEE-----LEAELAELEAELEELRLELEELELELEEAQAEEYEL--LAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1605 LERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA 1684
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---------AELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1685 AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1764
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1765 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLA----AISEATRLKTEAEIALKEKEAENERL 1840
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagAVAVLIGVEAAYEAALEAALAAALQN 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1841 RRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELEL 1920
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1921 ELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRE 2000
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 2001 RAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLER 2052
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
152-253 |
1.22e-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: 129.47 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 152 EKLLL-WSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 230
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1920237982 231 VDVPQPDEKSIITYVSSLYDAMP 253
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
133-249 |
1.54e-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: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 133 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQA 212
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237982 213 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 249
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1655-2223 |
2.90e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 145.46 E-value: 2.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1655 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1734
Cdd:COG1196 210 EKAERYRELKEELKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1735 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAVRQRAEAERVLAEKLA 1814
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1815 AISEATRLKTEAEIALKEKEAENERLRRlaedEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQR 1894
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALR----AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1895 RQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEA 1974
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1975 ARQRKAALEEVERLKAKVEEAR---RLRERAEQESARQLQLAQEAAQKRL-----QAEEKAHAFAVQQKEQELQQTLQQE 2046
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAAlaaALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAV 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2047 QSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2126
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2127 EQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2206
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
570
....*....|....*..
gi 1920237982 2207 LRVQMEELGKLKARIEA 2223
Cdd:COG1196 762 LEELERELERLEREIEA 778
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
16-136 |
6.57e-34 |
|
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: 127.73 E-value: 6.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 16 DERDRVQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGdslprerdvirsSRLPREKGRMRFHKLQNVQ 94
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTG------------QKLVKEKGSTRVHALNNVN 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237982 95 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 136
Cdd:cd21231 69 KALQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
149-249 |
5.64e-32 |
|
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: 122.13 E-value: 5.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 149 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 228
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1920237982 229 EDVDVPQPDEKSIITYVSSLY 249
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
20-137 |
6.02e-32 |
|
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: 122.56 E-value: 6.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpREKGRMRFHKLQNVQIALDY 99
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKF----------NKRPTFRSQKLENVSVALKF 83
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237982 100 LRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 137
Cdd:cd21311 84 LEEDEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
21-136 |
1.08e-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: 121.24 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 21 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRerdVIRssrlpreKGRMRFHKLQNVQIALDYL 100
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGR---VIK-------KPLNQHQKLENVTLALKAM 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237982 101 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 136
Cdd:cd21227 74 AEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
11-132 |
1.92e-31 |
|
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: 122.46 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 11 ISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMRFHKL 90
Cdd:cd21316 43 IKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKP-----------TKGRMRIHCL 111
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237982 91 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 132
Cdd:cd21316 112 ENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
148-246 |
4.46e-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: 119.45 E-value: 4.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 148 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 227
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1920237982 228 PEDVDVPQPDEKSIITYVS 246
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1313-1917 |
1.21e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 134.50 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1313 ETLRRMEEEERLAEQQRAE------------ERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREE 1380
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEavkkaeeakkdaEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1381 V--AVEAQ--EQKRSIQEELQHLRQSSEAEiQAKARQVEA---AERSRLRIEEEirvvRLQLEATERQRGGAEGELQALR 1453
Cdd:PTZ00121 1289 KkkADEAKkaEEKKKADEAKKKAEEAKKAD-EAKKKAEEAkkkADAAKKKAEEA----KKAAEAAKAEAEAAADEAEAAE 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1454 ARAEEAEAQKRQAQEEAERLRRQVQ-----DETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRlQAEEAERRLRQ 1528
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEekkkaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEE 1442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1529 A--------EAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLR--EEATRRAQQQAEAERAR 1598
Cdd:PTZ00121 1443 AkkadeakkKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKKAEEAK 1522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1599 AEAERELERWQLKANEALRlrlqAEEVAQQKSLTQAEAEKQKEEAEREARRRgKAEEqavrQRELAEQELEKQRQLAEGT 1678
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKK----AEEKKKADELKKAEELKKAEEKKKAEEAK-KAEE----DKNMALRKAEEAKKAEEAR 1593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1679 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEK 1758
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1759 SKQRLEAEagrfRELAEEAARLRALAEEAKRQRQLAEedaVRQRAEAERVLAEKLAAISEATRLKteAEIALKEKEAENE 1838
Cdd:PTZ00121 1674 KKKAEEAK----KAEEDEKKAAEALKKEAEEAKKAEE---LKKKEAEEKKKAEELKKAEEENKIK--AEEAKKEAEEDKK 1744
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 1839 RLRRLAEDEAFQRRLleeqaAQHKADIEARLAQLRKASESELErqKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAE 1917
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKI-----AHLKKEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
136-251 |
1.59e-30 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 118.40 E-value: 1.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 136 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 215
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237982 216 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 251
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
148-246 |
1.65e-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: 118.01 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 148 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 227
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1920237982 228 PEDVDVPQPDEKSIITYVS 246
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
152-253 |
1.79e-30 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 117.75 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 152 EKLLL-WSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 230
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1920237982 231 VDVPQPDEKSIITYVSSLYDAMP 253
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1313-1945 |
1.89e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 134.11 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1313 ETLRRMEEEERLAEQQRAEERERLAEVEAALE--KQRQLAEAHAQAKAQAEREAQGLQR----------RMQEEVARREE 1380
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRKAEElrKAEDARKAEAARKAEEERKAEEARKaedakkaeavKKAEEAKKDAE 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1381 VAVEAQEQKRSIQ-EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRlQLEATERQRGGAEGELQALRAR-AEE 1458
Cdd:PTZ00121 1241 EAKKAEEERNNEEiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKkADE 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1459 AEAQKRQAQEEAERLRRQVQdETQRKRQAEAELALRVQAEAEAAREKQRALQ-ALEELRLQAEEAERRlrqaeAERARQV 1537
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkKKEEAKKKADAAKKK-----AEEKKKA 1393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1538 QVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARaeaerelerwqlKANEALR 1617
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------------EAKKAEE 1461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1618 LRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELiRLRAETE 1697
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA-KKADEAK 1540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1698 QGEQQR---QLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEaEAGRFRELA 1774
Cdd:PTZ00121 1541 KAEEKKkadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAK 1619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1775 EEAARLRALAEEAKRQRQLAEEDA--------VRQRAEAERVLAEKLAAISEATrlKTEAEIALKEKEAENERLRRLAED 1846
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAeekkkaeeLKKAEEENKIKAAEEAKKAEED--KKKAEEAKKAEEDEKKAAEALKKE 1697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1847 EAFQRRLleEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVeEEILALKGSFEKAAAGKAELELELGRIR 1926
Cdd:PTZ00121 1698 AEEAKKA--EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA-EEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
650
....*....|....*....
gi 1920237982 1927 GTAEDTLRSKEQAEQEAAR 1945
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRR 1793
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
868-945 |
4.38e-30 |
|
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: 115.78 E-value: 4.38e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237982 868 LAWQSLGRDMQLIRSWSLATFRTLKPEEQRQALRSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSRHYQQLLQS 945
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
21-136 |
6.03e-30 |
|
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: 116.26 E-value: 6.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 21 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprekGRMRFHKLQNVQIALDY 99
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKER------------GSTRVHALNNVNRVLQV 69
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237982 100 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 136
Cdd:cd21232 70 LHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1722-2433 |
1.45e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 130.06 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1722 QKRRELEAELAKVRAEMEvllaskaRAEEEsrsTSEKSKQ--RLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEedav 1799
Cdd:COG1196 172 ERKEEAERKLEATEENLE-------RLEDI---LGELERQlePLERQA----EKAERYRELKEELKELEAELLLLK---- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1800 RQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAqhkadiEARLAQLRKASESE 1879
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL------LAELARLEQDIARL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1880 LERQkglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRRE 1959
Cdd:COG1196 308 EERR----RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1960 AEERVQKSLAAEEEAARQRKAALEEVERLKAkvEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQEL 2039
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLE--RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2040 QQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQE 2119
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2120 AARRAQAEQAALRQKQAAdaemekhkqfAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRgq 2199
Cdd:COG1196 542 AALAAALQNIVVEDDEVA----------AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR-- 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2200 vEEELFSLRVQMEELGklkarieaenRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2279
Cdd:COG1196 610 -EADARYYVLGDTLLG----------RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2280 ALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERL 2359
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2360 RLRVAEMSRAQARAEEDARRFRK-------QAEDIGERLyrTELATQekvmlVQTLETQRqqsdrdaERLREAIAELEHE 2432
Cdd:COG1196 759 PPDLEELERELERLEREIEALGPvnllaieEYEELEERY--DFLSEQ-----REDLEEAR-------ETLEEAIEEIDRE 824
|
.
gi 1920237982 2433 K 2433
Cdd:COG1196 825 T 825
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
152-254 |
3.04e-29 |
|
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: 114.64 E-value: 3.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 152 EKLLL-WSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 229
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1920237982 230 DVDVPQPDEKSIITYVSSLYDAMPR 254
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
154-249 |
3.43e-29 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 113.98 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 154 LLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 232
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1920237982 233 VPQPDEKSIITYVSSLY 249
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
17-138 |
3.89e-29 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 114.21 E-value: 3.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 17 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRErdvIRSSRlprekgrMRFHKLQNVQ 94
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQE---YKPSS-------HRIFRLNNIA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1920237982 95 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 138
Cdd:cd21191 71 KALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
20-134 |
7.16e-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: 113.34 E-value: 7.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlprEKGRMRFHKLQNVQIALDY 99
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYN---------RRPAFQQHYLENVSTALKF 73
|
90 100 110
....*....|....*....|....*....|....*
gi 1920237982 100 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 134
Cdd:cd21183 74 IEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
134-251 |
3.55e-28 |
|
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: 112.10 E-value: 3.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 134 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAF 213
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237982 214 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 251
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1168-1786 |
3.96e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.43 E-value: 3.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1168 QTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVpLANSQAVREQLRQEKALLED-IERHGEKveecqrfa 1246
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELeLEEAQAE-------- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1247 kqyinaikdyELQLVTYKAQLEPVASPAKkpkvqsgsESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAE 1326
Cdd:COG1196 290 ----------EYELLAELARLEQDIARLE--------ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1327 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAqglqrrmqeEVARREEVAVEAQEQKRSIQEELQHLRQSSEAE 1406
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL---------EALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1407 IQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRqvQDETQRKRQ 1486
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA--RLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1487 AEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAE----K 1562
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflplD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1563 TAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEE 1642
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1643 AEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQ 1722
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 1723 KRRELEAELAKVRAEMEvllaskaraEEESRSTSEKSKQRLEAEAGRF--------RELAEEAARLRALAEE 1786
Cdd:COG1196 741 LLEEEELLEEEALEELP---------EPPDLEELERELERLEREIEALgpvnllaiEEYEELEERYDFLSEQ 803
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1482-2197 |
4.50e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.43 E-value: 4.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1482 QRKRQAEAELAlrvQAEAEAAR--------EKQralqaLEELRLQAEEAERRLRQAEAERARQVQVALetaqrsaeAELQ 1553
Cdd:COG1196 172 ERKEEAERKLE---ATEENLERledilgelERQ-----LEPLERQAEKAERYRELKEELKELEAELLL--------LKLR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1554 SEHASFAEKTAQLERTLKEEHVAVVQLREEATRRaqqqaeaeraraeaerelerwqlkanEALRLRLQAEEvaqqksltq 1633
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAEL--------------------------EELRLELEELE--------- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1634 aeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARL 1713
Cdd:COG1196 281 ------------------LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1714 QREAAAATQKRRELEAELAKVRAEmevLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQL 1793
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEA---LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1794 AEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLR 1873
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1874 KASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEE 1953
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1954 ERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQ 2033
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2034 QKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLR 2113
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2114 KEAEQEAARRAQAEQAALRQKQAADAEMEKHKqfAEQALRQKAQV----EQELTALRLQLEETDHQKSILDEELQRLK-- 2187
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELER--LEREIEALGPVnllaIEEYEELEERYDFLSEQREDLEEARETLEea 817
|
730
....*....|.
gi 1920237982 2188 -AEVTEAARQR 2197
Cdd:COG1196 818 iEEIDRETRER 828
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1696-2586 |
1.05e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 121.40 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1696 TEQGEQQRQLLEEELARLQREAAAATqkRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFREL-- 1773
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgk 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1774 AEEAARlralAEEAKRQrqlAEEdaVRQRAEAERvlAEKLAAISEATRLKTE--AEIALKEKEAENERLRRLAEDeafQR 1851
Cdd:PTZ00121 1111 AEEARK----AEEAKKK---AED--ARKAEEARK--AEDARKAEEARKAEDAkrVEIARKAEDARKAEEARKAED---AK 1176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1852 RLLEEQAAqhkadIEARLA-QLRKASESelerqkglvedtlrqrRQVEEeilalkgsfekaaAGKAELELELGRIRgTAE 1930
Cdd:PTZ00121 1177 KAEAARKA-----EEVRKAeELRKAEDA----------------RKAEA-------------ARKAEEERKAEEAR-KAE 1221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1931 DTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQL 2010
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR---KADELKKAEEKKKADEAKKA 1298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2011 QLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERlrseaeaarraaeeaeaareraereaaqsRRQVEEAER 2090
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE-----------------------------AKKAAEAAK 1349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2091 LKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQaLRQKAQVEQELTALRLQLE 2170
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAE 1428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2171 ETDHQksildEELQRLKAEVTEAARQRGQVEEelfslRVQMEELGKlkaRIEAENRALVLRDKDSAQRLLQE---EAEKM 2247
Cdd:PTZ00121 1429 EKKKA-----DEAKKKAEEAKKADEAKKKAEE-----AKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEakkKAEEA 1495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2248 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQED 2323
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2324 KeQMAQQLAQETQgfqktlETERQRQLEMSAEAERLRLRVAEmsraQARAEEDARrfrKQAEDIGErlyrtelaTQEKVM 2403
Cdd:PTZ00121 1576 K-NMALRKAEEAK------KAEEARIEEVMKLYEEEKKMKAE----EAKKAEEAK---IKAEELKK--------AEEEKK 1633
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2404 LVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQalqqsflsekdslLQRErci 2483
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA-------------LKKE--- 1697
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2484 EQEKAKLEQL---FQDEVAKAQALREEQQRQQQqmqqekqqlaaSMEEARRRQHE----AEEgVRRQQEELQRLAQQQQQ 2556
Cdd:PTZ00121 1698 AEEAKKAEELkkkEAEEKKKAEELKKAEEENKI-----------KAEEAKKEAEEdkkkAEE-AKKDEEEKKKIAHLKKE 1765
|
890 900 910
....*....|....*....|....*....|....
gi 1920237982 2557 QEKLLAEENQR----LRERLQHLEEERRAALARS 2586
Cdd:PTZ00121 1766 EEKKAEEIRKEkeavIEEELDEEDEKRRMEVDKK 1799
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
152-251 |
1.12e-26 |
|
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: 106.99 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 152 EKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 230
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1920237982 231 VDVPQPDEKSIITYVSSLYDA 251
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
136-251 |
1.65e-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: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 136 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 215
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237982 216 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 251
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
20-134 |
4.05e-26 |
|
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: 105.65 E-value: 4.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlprEKGRMRFHKLQNVQIALDY 99
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYN---------KRPTFRQMKLENVSVALEF 73
|
90 100 110
....*....|....*....|....*....|....*
gi 1920237982 100 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 134
Cdd:cd21228 74 LERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
136-251 |
8.28e-26 |
|
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: 105.19 E-value: 8.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 136 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 215
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237982 216 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 251
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1862-2590 |
1.14e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 118.32 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1862 KADIEARLAQLRKASESELERQKGLVEDTlRQRRQVEEEilalKGSFE---KAAAGKAELELELGRIRGTAEDTLRSKE- 1937
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDN-RADEATEEA----FGKAEeakKTETGKAEEARKAEEAKKKAEDARKAEEa 1133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1938 -QAE-----QEAARQRQLAAEEERRRREAEERVQKSLAAEE----EAARQ----RKAA----LEEVERLKA--KVEEARR 1997
Cdd:PTZ00121 1134 rKAEdarkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDakkaEAARKaeevRKAEelrkAEDARKAEAarKAEEERK 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1998 LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAERE 2077
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2078 AAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADA--EMEKHKQFAEQALRQK 2155
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAadEAEAAEEKAEAAEKKK 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2156 AQVEQELTALRLQLEETDHQksildEELQRLKAEVTEAARQRGQVEEElfslrvqmeelgKLKARiEAENRALVLRDKDS 2235
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKA-----DEAKKKAEEDKKKADELKKAAAA------------KKKAD-EAKKKAEEKKKADE 1435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2236 AQRLLQE--EAEKMKQVAEEAARLSVAAQEAARLRQlAEEdlAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELA 2313
Cdd:PTZ00121 1436 AKKKAEEakKADEAKKKAEEAKKAEEAKKKAEEAKK-ADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2314 QEqARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRlRVAEMSRAQA--RAEEDARRFRKQAEDigerL 2391
Cdd:PTZ00121 1513 DE-AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK-KAEEKKKAEEakKAEEDKNMALRKAEE----A 1586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2392 YRTELATQEKVM-LVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFL 2470
Cdd:PTZ00121 1587 KKAEEARIEEVMkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2471 SEKDsllqrerciEQEKAKLEQLFQDEVAKAQAlrEEQQRQQQQMQQEKQQLAASMEEARRRQHE---AEEGVRRQQEEL 2547
Cdd:PTZ00121 1667 AKKA---------EEDKKKAEEAKKAEEDEKKA--AEALKKEAEEAKKAEELKKKEAEEKKKAEElkkAEEENKIKAEEA 1735
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1920237982 2548 QRLAQQ-QQQQEKLLAEENQrlRERLQHL--EEERRAALARSEEIA 2590
Cdd:PTZ00121 1736 KKEAEEdKKKAEEAKKDEEE--KKKIAHLkkEEEKKAEEIRKEKEA 1779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1388-2190 |
1.62e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 117.55 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1388 QKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEaEAQKRQAQ 1467
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE-ARKAEEAK 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1468 EEAERLR-----RQVQD--ETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAE----AERARQ 1536
Cdd:PTZ00121 1122 KKAEDARkaeeaRKAEDarKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEelrkAEDARK 1201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1537 VQVAletaqRSAEAELQSEHASFAEKTAQLERTLKEEHVAvvQLREEATRRAQQQAEAERARAEAERELERWQLKANEAL 1616
Cdd:PTZ00121 1202 AEAA-----RKAEEERKAEEARKAEDAKKAEAVKKAEEAK--KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1617 RLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQavRQRELAEQELEKQRQLAEGTAQQrlaAEQEliRLRAET 1696
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKKADAAKKK---AEEA--KKAAEA 1347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1697 EQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEmEVLLA--SKARAEEESRSTSEKSKQrlEAEAGRFRELA 1774
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-EKKKAdeAKKKAEEDKKKADELKKA--AAAKKKADEAK 1424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1775 EEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVlAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLL 1854
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1855 EEQAAQHKADiEARLAQLRKASEsELERQKglvedtlrQRRQVEEeilaLKGSFEKAAAGKAELELELGRirgtAEDTlR 1934
Cdd:PTZ00121 1504 KAAEAKKKAD-EAKKAEEAKKAD-EAKKAE--------EAKKADE----AKKAEEKKKADELKKAEELKK----AEEK-K 1564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1935 SKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRlrerAEQESARQLQLaq 2014
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK----AEEEKKKVEQL-- 1638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2015 eaaqKRLQAEEKAHAFAVQQKEQELQQTLqqeqsvlERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQs 2094
Cdd:PTZ00121 1639 ----KKKEAEEKKKAEELKKAEEENKIKA-------AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE- 1706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2095 aeeQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADaemEKHKQFAEQALRQKAQVEQELTALRLQLEETDH 2174
Cdd:PTZ00121 1707 ---LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE---EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
810
....*....|....*.
gi 1920237982 2175 QKSILDEELQRLKAEV 2190
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEV 1796
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
20-137 |
2.57e-25 |
|
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: 103.96 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlPREKgrMRFHKLQNVQIALDY 99
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYH-------PRPN--FRQMKLENVSVALEF 85
|
90 100 110
....*....|....*....|....*....|....*...
gi 1920237982 100 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 137
Cdd:cd21310 86 LDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
11-136 |
4.24e-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: 103.30 E-value: 4.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 11 ISSLKDERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMRFH 88
Cdd:cd21247 10 IRKLQEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRP-----------SRGKMRVH 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1920237982 89 KLQNVQIALDYLRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 136
Cdd:cd21247 79 FLENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
136-251 |
2.32e-24 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 100.92 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 136 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 215
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237982 216 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 251
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1325-2536 |
3.34e-24 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 113.00 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1325 AEQQRAEERERLAEVEAalEKQRQLAE-AHAQAKAQAEREAQGLQRRMQ--EEVARREEvAVEAQEQKRSIQEELQHLRQ 1401
Cdd:NF041483 85 ADQLRADAERELRDARA--QTQRILQEhAEHQARLQAELHTEAVQRRQQldQELAERRQ-TVESHVNENVAWAEQLRART 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1402 SSEA-----EIQAKARQVEAAERSRlrieeeirVVRLQLEAteRQRGGAEGElqalRARAEeAEAQKRQAQEEAERLRRQ 1476
Cdd:NF041483 162 ESQArrlldESRAEAEQALAAARAE--------AERLAEEA--RQRLGSEAE----SARAE-AEAILRRARKDAERLLNA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1477 VQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQaeEAERRLRQAEAERARQVQVALETA-QRSAEAELQSE 1555
Cdd:NF041483 227 ASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAAaKQLASAESANE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1556 hasfaektaQLERTLKEEhvaVVQLREEATRRAQQQAEAERARAEAERELERWQL-KANEALRLRLQAEEVAQQKSLTQA 1634
Cdd:NF041483 305 ---------QRTRTAKEE---IARLVGEATKEAEALKAEAEQALADARAEAEKLVaEAAEKARTVAAEDTAAQLAKAART 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1635 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ-RLAAEQELIRLRAETEQgeqqrqlLEEELARL 1713
Cdd:NF041483 373 AEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVE-------LQEEARRL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1714 QREAAaatQKRRELEAELAKVRAEmevllaskARAEeesrstsekSKQRLEAEAGRFRELAEEAarlRALAEEAKRQrql 1793
Cdd:NF041483 446 RGEAE---QLRAEAVAEGERIRGE--------ARRE---------AVQQIEEAARTAEELLTKA---KADADELRST--- 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1794 aeedavrQRAEAERVLAEklaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAA-QHKADIEARLAQL 1872
Cdd:NF041483 500 -------ATAESERVRTE---AIERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAArELREETERAIAAR 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1873 RKASESELERQKGLVEdtlrQRRQVEEEilALKGSFEKAAAGKAELELELGRIRGTAEDTLRS-KEQAEQEAARQRqlaa 1951
Cdd:NF041483 570 QAEAAEELTRLHTEAE----ERLTAAEE--ALADARAEAERIRREAAEETERLRTEAAERIRTlQAQAEQEAERLR---- 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1952 eeerrRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE-ARRLR-------ERAEQESARQLQLAQ-EAAQKRLQ 2022
Cdd:NF041483 640 -----TEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQEsADRVRaeaaaaaERVGTEAAEALAAAQeEAARRRRE 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2023 AEE---KAHAFAVQQKEQELQQTLQQEQSVLERLrseaeaarraaeeaeaareraEREAAQSRRQVEEAERlkqsaeeqa 2099
Cdd:NF041483 715 AEEtlgSARAEADQERERAREQSEELLASARKRV---------------------EEAQAEAQRLVEEADR--------- 764
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2100 qaqaqaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEET-DHQKSI 2178
Cdd:NF041483 765 --------------------------------RATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAaERTRTE 812
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2179 LDEELQRLKAEvteAARQRGQVEEELFSLRVQ-MEELGKLKARIEAEnralVLRDKDSAQRLLQEEAEKMKQVAEEAA-R 2256
Cdd:NF041483 813 AQEEADRVRSD---AYAERERASEDANRLRREaQEETEAAKALAERT----VSEAIAEAERLRSDASEYAQRVRTEASdT 885
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2257 LSVAAQEAARLRQLAEEDLAQQRALA---EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAq 2333
Cdd:NF041483 886 LASAEQDAARTRADAREDANRIRSDAaaqADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIA- 964
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2334 etqgfqktleterqrqlEMSAEAERLRLRVAE-MSRAQARAE---EDARRFRKQAEDIGERLyRTELATQEKVMLVQTLE 2409
Cdd:NF041483 965 -----------------EATGEAERLRAEAAEtVGSAQQHAErirTEAERVKAEAAAEAERL-RTEAREEADRTLDEARK 1026
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2410 TQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLL----QETQALQQSFLSEKDSLLQRERcieq 2485
Cdd:NF041483 1027 DANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVgaarKEAERIVAEATVEGNSLVEKAR---- 1102
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|.
gi 1920237982 2486 ekAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLaasMEEARRRQHEA 2536
Cdd:NF041483 1103 --TDADELLVGARRDATAIRERAEELRDRITGEIEEL---HERARRESAEQ 1148
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
154-249 |
6.39e-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: 99.15 E-value: 6.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 154 LLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 232
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1920237982 233 VPQPDEKSIITYVSSLY 249
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
24-133 |
6.41e-24 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 98.93 E-value: 6.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 24 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVirssrlprEKGRMRFHKLQNVQIALDYLRH 102
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVD-KKKV--------AASLSRFKKIENINLALSFAEK 71
|
90 100 110
....*....|....*....|....*....|.
gi 1920237982 103 RQVKLVNIRNDDIADGnPKLTLGLIWTIILH 133
Cdd:smart00033 72 LGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
148-254 |
6.79e-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: 6.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 148 MTAKEKLLLWSQRMVEGC-QGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 224
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1920237982 225 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 254
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1362-2222 |
1.05e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 111.30 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1362 REAQGLQRRMQEEVARREEVAVEAQEQKRSIQ------EELQHLR-QSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ 1434
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKaELRELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1435 LEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEE 1514
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1515 LRLQAEEAERRLrqaeaerarqvqvaletaqrsaeAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATrraqqqaea 1594
Cdd:TIGR02168 335 LAEELAELEEKL-----------------------EELKEELESLEAELEELEAELEELESRLEELEEQLE--------- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1595 eraraeaerelerwQLKANEALRLRLQAEEVAQQKSLTQAEaekqkeeaerearrrgkaeEQAVRQRELAEQELEKQRQL 1674
Cdd:TIGR02168 383 --------------TLRSKVAQLELQIASLNNEIERLEARL-------------------ERLEDRRERLQQEIEELLKK 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1675 AEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRS 1754
Cdd:TIGR02168 430 LE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1755 TSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaeEDAVRQRAEAERVLAEKLAAiSEATRLKTEAEIALKE 1832
Cdd:TIGR02168 508 VKAllKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRL---QAVVVENLNAAKKAIAFLKQ-NELGRVTFLPLDSIKG 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1833 KEAENERLRRLAEDEAFQRRL--LEEQAAQHKADIEARLAQLRKASEselerqkglVEDTLRQRRQVEEEIL-------- 1902
Cdd:TIGR02168 584 TEIQGNDREILKNIEGFLGVAkdLVKFDPKLRKALSYLLGGVLVVDD---------LDNALELAKKLRPGYRivtldgdl 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1903 -----ALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQlaaeeerRRREAEERVQKSLAAEEEAARQ 1977
Cdd:TIGR02168 655 vrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK-------ELEELEEELEQLRKELEELSRQ 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1978 RKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAfaVQQKEQELQQTLQQEQSVLERLRSEA 2057
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREAL 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2058 EAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAA 2137
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2138 DAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLK---AEVTEAARQRGQVEEELFSLRVQMEEL 2214
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvriDNLQERLSEEYSLTLEEAEALENKIED 965
|
....*...
gi 1920237982 2215 GKLKARIE 2222
Cdd:TIGR02168 966 DEEEARRR 973
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
21-136 |
3.61e-23 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 96.97 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 21 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLPrerdvirssrlPREKGRMRFHKLQNVQIALD 98
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVD-----------KKKLNKSEFDKLENINLALD 70
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237982 99 YLRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 136
Cdd:pfam00307 71 VAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1288-2024 |
7.35e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.61 E-value: 7.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1288 QEYVDLRTRYSELS-TLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAAL--------EKQRQLAEA------ 1352
Cdd:TIGR02168 213 ERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLeelrlevsELEEEIEELqkelya 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1353 HAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQE------ELQHLRQSSEAEIQAKARQVEAAERSRLRIEE 1426
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDElaeelaELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1427 EIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELALRVQAEAEAAREKQ 1506
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI--EELLKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1507 RALQALEELRLQAEEAERRLRQAEAERarqvqvaletaqRSAEAELQsEHASFAEKTAQLERTLKEEHVAVVQLREEAtr 1586
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQAL------------DAAERELA-QLQARLDSLERLQENLEGFSEGVKALLKNQ-- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1587 raQQQAEAERARAEAERELERWQLKANEALRLRLQA---EEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQREL 1663
Cdd:TIGR02168 516 --SGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1664 AEQELEKQRQLA---EGTAQQRLAAEQELIRLR-AETEQG--EQQRQLLEEELA------------RLQREAAAATQKRR 1725
Cdd:TIGR02168 594 LKNIEGFLGVAKdlvKFDPKLRKALSYLLGGVLvVDDLDNalELAKKLRPGYRIvtldgdlvrpggVITGGSAKTNSSIL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1726 ELEAELAKVRAEMEvLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEA 1805
Cdd:TIGR02168 674 ERRREIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1806 ERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAED-----EAFQRRLLEEQAAQHKADIEARLAQLRKAS-ESE 1879
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeelKALREALDELRAELTLLNEEAANLRERLESlERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1880 LERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELgrirgtaEDTLRSKEQAEQEAARQRQLAAEEERRRRE 1959
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-------EALLNERASLEEALALLRSELEELSEELRE 905
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237982 1960 AEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE-ARRLRERA--EQESARQLQLAQEAAQKRLQAE 2024
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYslTLEEAEALENKIEDDEEEARRR 973
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1680-2472 |
8.14e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.22 E-value: 8.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1680 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAtQKRRELEAELAKVRAEmevLLASKARAEEESRSTSEKS 1759
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKA-ERYKELKAELRELELA---LLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1760 KQRLEAEagrFRELAEEAARLRALAEEAKRQRQLAEEDAvrqrAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENER 1839
Cdd:TIGR02168 248 LKEAEEE---LEELTAELQELEEKLEELRLEVSELEEEI----EELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1840 LRRLAEDEAFQRRLLEEQAAQHKADIEaRLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFekaaagkAELE 1919
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV-------AQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1920 LELGRIRGTAEDTLRSKEQAEQEAARQRQ-LAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRL 1998
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1999 RERAEQESARQLQLAQE--AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAER 2076
Cdd:TIGR02168 473 AEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2077 EAAQSRRQVEEAerLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAaDAEMEKHKQFAeqaLRQKA 2156
Cdd:TIGR02168 553 ENLNAAKKAIAF--LKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKF-DPKLRKALSYL---LGGVL 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2157 QVEQELTALRLQlEETDHQKSI--LDEELQRLKAEVTEAARQRGQVeeeLFSLRVQMEELGKLKARIEAENRAL--VLRD 2232
Cdd:TIGR02168 627 VVDDLDNALELA-KKLRPGYRIvtLDGDLVRPGGVITGGSAKTNSS---ILERRREIEELEEKIEELEEKIAELekALAE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2233 KDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE-----------KMQAVQEATRLKA 2301
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaeieeleerLEEAEEELAEAEA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2302 EAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRlrvaEMSRAQARAEEDARRFR 2381
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE----DLEEQIEELSEDIESLA 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2382 KQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTvRQEQLLQE 2461
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL-RLEGLEVR 937
|
810
....*....|.
gi 1920237982 2462 TQALQQSFLSE 2472
Cdd:TIGR02168 938 IDNLQERLSEE 948
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
150-249 |
9.84e-23 |
|
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: 95.71 E-value: 9.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 150 AKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 229
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1920237982 230 D-VDVPQPDEKSIITYVSSLY 249
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1851-2492 |
1.20e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.72 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1851 RRLLEEQA--AQHKADIEARLAQLRKASE---------SELERQKglveDTLRQRRQVEEEILALKGSFEKAaagkaELE 1919
Cdd:COG1196 158 RAIIEEAAgiSKYKERKEEAERKLEATEEnlerledilGELERQL----EPLERQAEKAERYRELKEELKEL-----EAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1920 LELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR 1999
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2000 ERAEQESARQLQLAQEAAQKRLQAEEKAhafavqqkeqelqqtlqqeqsvlERLRSEAEAARRAAEEAEAARERAEREAA 2079
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELE-----------------------EELEELEEELEEAEEELEEAEAELAEAEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2080 QSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVE 2159
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2160 QELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAenrALVLRDKDSAQRL 2239
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG---VKAALLLAGLRGL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2240 LQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARR 2319
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2320 LQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQ 2399
Cdd:COG1196 603 LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2400 EKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQR 2479
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
650
....*....|...
gi 1920237982 2480 ERcIEQEKAKLEQ 2492
Cdd:COG1196 763 EE-LERELERLER 774
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1316-2027 |
1.39e-22 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 107.60 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1316 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLA-EAHAQAKAQAEREAQGLQRRMQEEVARreeVAVEAQEQKRSIQE 1394
Cdd:NF041483 254 RQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAkEAAAKQLASAESANEQRTRTAKEEIAR---LVGEATKEAEALKA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1395 ELQHLRQSSEAEiqAKARQVEAAERSRLRIEEEirvvrlqlEATERQRGGAEGElQALRARAEEAEAQKRQAQEEAERLR 1474
Cdd:NF041483 331 EAEQALADARAE--AEKLVAEAAEKARTVAAED--------TAAQLAKAARTAE-EVLTKASEDAKATTRAAAEEAERIR 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1475 RQVQDETQRKRQAEAELALRVQAEAEAAREKQRAlqalEELRLQaEEAeRRLRqAEAERARqvqvaletaqrsaeaelqs 1554
Cdd:NF041483 400 REAEAEADRLRGEAADQAEQLKGAAKDDTKEYRA----KTVELQ-EEA-RRLR-GEAEQLR------------------- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1555 ehasfAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELErwqlkANEALRLRLQAEEVAqqKSLTQA 1634
Cdd:NF041483 454 -----AEAVAEGERIRGEARREAVQQIEEAARTAEELLTKAKADADELRSTA-----TAESERVRTEAIERA--TTLRRQ 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1635 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA-AEQELIRLRAETEQ----GEQQRQLLEEE 1709
Cdd:NF041483 522 AEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEErltaAEEALADARAE 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1710 LARLQREAAAATQKRRELEAE-----LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrelAEEAARLRALA 1784
Cdd:NF041483 602 AERIRREAAEETERLRTEAAErirtlQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEA------AAEAERLKSEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1785 EE-AKRQRQLAEEDAVRQRAEAERVLAeklAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrllEEQAAQHKA 1863
Cdd:NF041483 676 QEsADRVRAEAAAAAERVGTEAAEALA---AAQEEAARRRREAEETLGSARAEADQERERAREQS------EELLASARK 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1864 DIEARLAQLRKASESELERQKGLV---EDTLRQRR--------QVEEEILALKGSFEKAAA-GKAELELELGRIRGtaeD 1931
Cdd:NF041483 747 RVEEAQAEAQRLVEEADRRATELVsaaEQTAQQVRdsvaglqeQAEEEIAGLRSAAEHAAErTRTEAQEEADRVRS---D 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1932 TLRSKEQAEQEAARQRQlaaeeerrrreaeERVQKSLAAEEEAARQRKAALEEVERLKAKVEE-ARRLRERAeqeSARQL 2010
Cdd:NF041483 824 AYAERERASEDANRLRR-------------EAQEETEAAKALAERTVSEAIAEAERLRSDASEyAQRVRTEA---SDTLA 887
|
730
....*....|....*..
gi 1920237982 2011 QLAQEAAQKRLQAEEKA 2027
Cdd:NF041483 888 SAEQDAARTRADAREDA 904
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
152-252 |
1.69e-22 |
|
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: 94.84 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 152 EKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 231
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1920237982 232 DVPQPDEKSIITYVSSLYDAM 252
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
149-247 |
2.08e-22 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 94.61 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 149 TAKEKLLLWSQRMVEGCqglRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 227
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1920237982 228 PEDVDVPQPDEKSIITYVSS 247
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1659-2429 |
2.57e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 106.68 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1659 RQRELAEQELEKQRQLAEgtaqqrlaAEQELIRLRAETeqgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVRAEM 1738
Cdd:TIGR02168 207 RQAEKAERYKELKAELRE--------LELALLVLRLEE---------LREELEELQEELKEAEEELEELTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1739 EVLLASKARAEEEsrstsekskqrLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISE 1818
Cdd:TIGR02168 270 EELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1819 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQH---KADIEARLAQLRKASeSELERQKGLVEDTLRQRR 1895
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetlRSKVAQLELQIASLN-NEIERLEARLERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1896 QVEEEILALKGSFEKAAagKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRrreaeervQKSLAAEEEAA 1975
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA--------LDAAERELAQL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1976 RQRKAALEEV-ERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAA-QKRLQA------EEKAHAFAVQQK 2035
Cdd:TIGR02168 488 QARLDSLERLqENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAAlGGRLQAvvvenlNAAKKAIAFLKQ 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2036 EQELQQTLQQEQSVLER-LRSEAEAARRAAEEAEAARERAEREAAQSRRQVEE-------AERLKQSAEEQAQAQAQAQA 2107
Cdd:TIGR02168 568 NELGRVTFLPLDSIKGTeIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYRI 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2108 AAEKLRKEAEQEAARRAQAEQAALRQKQaaDAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLK 2187
Cdd:TIGR02168 648 VTLDGDLVRPGGVITGGSAKTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2188 AEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAEnRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQ----- 2262
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE-IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrea 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2263 ------------EAARLRQLAEEDLAQQRALAEKML----KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQ 2326
Cdd:TIGR02168 805 ldelraeltllnEEAANLRERLESLERRIAATERRLedleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2327 MAQQLAQ---ETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDigerLYRTELATQEKvm 2403
Cdd:TIGR02168 885 LEEALALlrsELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE----EYSLTLEEAEA-- 958
|
810 820
....*....|....*....|....*.
gi 1920237982 2404 LVQTLETQRQQSDRDAERLREAIAEL 2429
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1312-2028 |
2.84e-22 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 106.83 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1312 SETLRRMEEEERL---AEQQRAE---ERERLaEVEAALEKQRQLAEAHAQAK---AQAEREAQGLQRRMQEEVAR-REEV 1381
Cdd:NF041483 433 AKTVELQEEARRLrgeAEQLRAEavaEGERI-RGEARREAVQQIEEAARTAEellTKAKADADELRSTATAESERvRTEA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1382 AVEAQEQKRSIQEELQHLRqsSEAEiQAKARQVEAAERSRLRIEEEIRVVRLQLE-ATERQRGGAEGELQALRARAEE-- 1458
Cdd:NF041483 512 IERATTLRRQAEETLERTR--AEAE-RLRAEAEEQAEEVRAAAERAARELREETErAIAARQAEAAEELTRLHTEAEErl 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1459 --AEAQKRQAQEEAERLRRQVQDETQRKRQAEAE--LALRVQAEAEAAREKQRALQALEELRLQAEEAERRLR-QAEAER 1533
Cdd:NF041483 589 taAEEALADARAEAERIRREAAEETERLRTEAAEriRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLRsEAAAEA 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1534 ARQVQVALETAQRsaeaeLQSEHASFAEKTAQlertlkeehvavvqlreeatrraqqqaeaeraraeaerelerwqlKAN 1613
Cdd:NF041483 669 ERLKSEAQESADR-----VRAEAAAAAERVGT---------------------------------------------EAA 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1614 EALrlrlqaeevaqqksltqaeaekqkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELI--- 1690
Cdd:NF041483 699 EAL----------------------------------AAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasa 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1691 RLRAETEQGEQQRqLLEEELARLQREAAAATQKRRELEAELAKV--RAEMEV--LLASKARAEEESRSTSEKSKQRLEAE 1766
Cdd:NF041483 745 RKRVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSVAGLqeQAEEEIagLRSAAEHAAERTRTEAQEEADRVRSD 823
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1767 AGRFRELA-EEAARLRALA-EEAKRQRQLAEEDAVRQRAEAERVLAEklaAISEATRLKTEAEIALKEKEAENERLRRLA 1844
Cdd:NF041483 824 AYAERERAsEDANRLRREAqEETEAAKALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADA 900
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1845 EDEAFQRRllEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAElelelgR 1924
Cdd:NF041483 901 REDANRIR--SDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAE------R 972
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1925 IRGTAEDTLRSkeqAEQEAARQRQLAAEEERRrreaeervqkslaAEEEAARQRKAALEEVERL--KAKVEEARRLRERA 2002
Cdd:NF041483 973 LRAEAAETVGS---AQQHAERIRTEAERVKAE-------------AAAEAERLRTEAREEADRTldEARKDANKRRSEAA 1036
|
730 740
....*....|....*....|....*.
gi 1920237982 2003 EQESARQLQLAQEAAQKRLQAEEKAH 2028
Cdd:NF041483 1037 EQADTLITEAAAEADQLTAKAQEEAL 1062
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
149-249 |
2.97e-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: 94.41 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 149 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 228
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 1920237982 229 EDVDVPQ-PDEKSIITYVSSLY 249
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1966-2581 |
4.66e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.79 E-value: 4.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1966 KSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQ 2045
Cdd:COG1196 203 EPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2046 EQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQ 2125
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2126 AEQAALRQKQAADAEMEKHKQFAEQALRQkaqvEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELF 2205
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEA----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2206 SLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM 2285
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2286 LKEKMQAVQEATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRV 2363
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2364 AEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLL 2443
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2444 QLKSEEMQTVRQEQLLQETQALQQsflsekdsLLQRERCIEQEKAKLEQlfqdevakaqalreeqqrqqqqmqqekqqlA 2523
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAE--------EEEERELAEAEEERLEE------------------------------E 720
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237982 2524 ASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRA 2581
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1763-2578 |
6.44e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.52 E-value: 6.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1763 LEAEAGRFRELAEEAA---RLRALAEEAKRQRQLAEEDAVR------------QRAEAERVLAEKLAAISEATRlKTEAE 1827
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAgisKYKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYKELKAELR-ELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1828 IALKEKEAENERLRRLAEDEAFQRRLLEEQAAQhKADIEARLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEILAL 1904
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAE-LQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1905 KGSFEKAAAGKAELELELgrirgtaEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 1984
Cdd:TIGR02168 308 RERLANLERQLEELEAQL-------EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1985 VERLKAKVEEARR--LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQ-QKEQELQQTLQQEQSVLERLRSEAEAAR 2061
Cdd:TIGR02168 381 LETLRSKVAQLELqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2062 RAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQaeqaaLRQKQAADAEM 2141
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV-----LSELISVDEGY 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2142 EKHKQFAEQALRQKAQVEQELTALRLQleetDHQKsilDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARI 2221
Cdd:TIGR02168 536 EAAIEAALGGRLQAVVVENLNAAKKAI----AFLK---QNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2222 EAENRA-----------LVLRDKDSAQRLLQEEAEKMKQVAEEAARLS---VAAQEAARLRQLAeedLAQQRALAEkmLK 2287
Cdd:TIGR02168 609 KFDPKLrkalsyllggvLVVDDLDNALELAKKLRPGYRIVTLDGDLVRpggVITGGSAKTNSSI---LERRREIEE--LE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2288 EKMQAVQEAtrlkaEAELLQQQKELAQEQarrlqedkeqmaQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMS 2367
Cdd:TIGR02168 684 EKIEELEEK-----IAELEKALAELRKEL------------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2368 RAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKS 2447
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2448 EEMQTvRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQMQQEKQQLAASME 2527
Cdd:TIGR02168 827 ESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELR 904
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1920237982 2528 EARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEE 2578
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
990-1535 |
6.95e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.02 E-value: 6.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 990 ARECAQRITEQQKAQAEVDGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1069
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1070 RSTQEAEEVLRAHEEQLKEAQAvpATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVE 1149
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1150 RWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALL 1229
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1230 EDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaSPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIR 1309
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL---LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1310 FISETLRRMEEEERLAEQQRAE----ERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEA 1385
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRATflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1386 QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegELQALRARAEEAEAQKRQ 1465
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE-----EELELEEALLAEEEEERE 708
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1466 AQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERAR 1535
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
149-253 |
7.18e-22 |
|
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: 93.32 E-value: 7.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 149 TAKEKLLLWSQRMVEGcQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 228
Cdd:cd21245 3 KAIKALLNWVQRRTRK-YGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1920237982 229 EDVDVPQPDEKSIITYVSSLYDAMP 253
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
20-137 |
4.21e-21 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 92.07 E-value: 4.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlprEKGRMRFHKLQNVQIALDY 99
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHN---------QRPTFRQMQLENVSVALEF 89
|
90 100 110
....*....|....*....|....*....|....*...
gi 1920237982 100 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 137
Cdd:cd21308 90 LDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
20-137 |
6.06e-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: 6.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlpREKGRMRFHKLQNVQIALDY 99
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKY---------HQRPTFRQMQLENVSVALEF 86
|
90 100 110
....*....|....*....|....*....|....*...
gi 1920237982 100 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 137
Cdd:cd21309 87 LDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1459-2593 |
9.24e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 101.83 E-value: 9.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1459 AEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAE--AEAAREKQRALQALEELRLQAE-EAERRLRQAEAERAR 1535
Cdd:NF041483 81 AQIQADQLRADAERELRDARAQTQRILQEHAEHQARLQAElhTEAVQRRQQLDQELAERRQTVEsHVNENVAWAEQLRAR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1536 QVQVA---LETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVvqlREEATRRAQQQAEAERARAEAERELERWQLKA 1612
Cdd:NF041483 161 TESQArrlLDESRAEAEQALAAARAEAERLAEEARQRLGSEAESA---RAEAEAILRRARKDAERLLNAASTQAQEATDH 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1613 NEALRLRLQAE-EVAQQKSltqaeaekqkeeaereaRRRGKAEEQAVRQrelAEQELEKQRQLAEGTAQQrlAAEQELIR 1691
Cdd:NF041483 238 AEQLRSSTAAEsDQARRQA-----------------AELSRAAEQRMQE---AEEALREARAEAEKVVAE--AKEAAAKQ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1692 LRAETEQGEQQRQLLEEELARLQREAAA-ATQKRRELEAELAKVRAEMEVLLAS---KARAEEESRSTSEKSKQRLEAEA 1767
Cdd:NF041483 296 LASAESANEQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEaaeKARTVAAEDTAAQLAKAARTAEE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1768 GRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAI---------------SEATRLKTEAEIALKE 1832
Cdd:NF041483 376 VLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvelqEEARRLRGEAEQLRAE 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1833 KEAENERLRRLAEDEAFQR-----RLLEEQAAQHKADIEarlaQLRKASESELERQKG-LVEDTLRQRRQVEEeilALKG 1906
Cdd:NF041483 456 AVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADAD----ELRSTATAESERVRTeAIERATTLRRQAEE---TLER 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1907 SFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQ------LAAEEERRRREAEERVQKSLAAEEEAARQRKA 1980
Cdd:NF041483 529 TRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQaeaaeeLTRLHTEAEERLTAAEEALADARAEAERIRRE 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1981 ALEEVERLKAKV-EEARRLRERAEQESARqlqLAQEAAQKRLQAEEKAHAFAVqqkeqelqqtlqqeqsvleRLRSEAEa 2059
Cdd:NF041483 609 AAEETERLRTEAaERIRTLQAQAEQEAER---LRTEAAADASAARAEGENVAV-------------------RLRSEAA- 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2060 arraaeeaeaareraereaaqsrrqvEEAERLKqsaeeqaqaqAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQaada 2139
Cdd:NF041483 666 --------------------------AEAERLK----------SEAQESADRVRAEAAAAAERVGTEAAEALAAAQ---- 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2140 emekhkqfaEQALRQKAQVEQELTALRLQLEEtdhqksildeelqrlkaevtEAARQRGQVEEELFSLRVQMEELGKLKA 2219
Cdd:NF041483 706 ---------EEAARRRREAEETLGSARAEADQ--------------------ERERAREQSEELLASARKRVEEAQAEAQ 756
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2220 RI--EAENRA--LVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAA-RLRQLAEEDLAQQRALAekmLKEKMQAVQ 2294
Cdd:NF041483 757 RLveEADRRAteLVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAAeRTRTEAQEEADRVRSDA---YAERERASE 833
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2295 EATRLKAEAellQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLemsAEAERlrlrvaEMSRAQARAE 2374
Cdd:NF041483 834 DANRLRREA---QEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTL---ASAEQ------DAARTRADAR 901
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2375 EDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREaiaelehEKDKLKQEAQLLQLKSEEMQTVR 2454
Cdd:NF041483 902 EDANRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERV-------RADAAAQAEQLIAEATGEAERLR 974
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2455 QEQLLQETQALQQSflsekdsllqrerciEQEKAKLEQLFQDEVAKAQALReeqqrqqqqmqqekqqlAASMEEARRRQH 2534
Cdd:NF041483 975 AEAAETVGSAQQHA---------------ERIRTEAERVKAEAAAEAERLR-----------------TEAREEADRTLD 1022
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 2535 EAeegvrrQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIAPSR 2593
Cdd:NF041483 1023 EA------RKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTM 1075
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1071-1875 |
1.36e-20 |
|
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: 100.90 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1071 STQEAEEVLRAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVER 1150
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1151 WRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLE 1230
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1231 DIERhgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQyirf 1310
Cdd:TIGR02168 401 EIER-----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE---- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1311 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQE-EVARREEVAVEAQ--- 1386
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELiSVDEGYEAAIEAAlgg 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1387 -------EQKRSIQEELQHLRQSSE------AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALR 1453
Cdd:TIGR02168 546 rlqavvvENLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1454 ARAEEAEAQKRQAQEEAERLR-------------------RQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEE 1514
Cdd:TIGR02168 626 LVVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1515 LRLQAEEAERRLRQAEAERARQVqvaleTAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQqqaea 1594
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQI-----SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE----- 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1595 eraraeaerelerwQLKANEALRLRLQAeEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELaEQELEKQRQL 1674
Cdd:TIGR02168 776 --------------ELAEAEAEIEELEA-QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL-ERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1675 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAE---EE 1751
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRrelEE 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1752 SRSTSEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEDAVRQRAEAERvLAEKLAAISEATRLkteaeiAL 1830
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AI 992
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1920237982 1831 KEKEAENERLRRLaedeafqrrlleeqaAQHKADIEARLAQLRKA 1875
Cdd:TIGR02168 993 EEYEELKERYDFL---------------TAQKEDLTEAKETLEEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1972-2591 |
3.20e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.63 E-value: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1972 EEAARQRKAALEEVERLKAKVEEARR----LRERAEQ-ESARQLQlaqeAAQKRLQAEEKAHAFAVQQKEqelqqtlqqe 2046
Cdd:COG1196 175 EEAERKLEATEENLERLEDILGELERqlepLERQAEKaERYRELK----EELKELEAELLLLKLRELEAE---------- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2047 qsvLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQsaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQA 2126
Cdd:COG1196 241 ---LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE-------------EAQAEEYELLAELARLEQDI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2127 EQAALRQKQAADAEMEKHKQfAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2206
Cdd:COG1196 305 ARLEERRRELEERLEELEEE-LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2207 LRVQMEELgklkARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2286
Cdd:COG1196 384 LAEELLEA----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2287 KEKmQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAER---LRLRV 2363
Cdd:COG1196 460 ALL-ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveAAYEA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2364 AEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLL 2443
Cdd:COG1196 539 ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2444 Q--LKSEEMQTVRQEQLLQETQALQQSFLS---EKDSLLQRERCIEQEKAKLEQlfqdEVAKAQALREEQQRQQQQMQQE 2518
Cdd:COG1196 619 GdtLLGRTLVAARLEAALRRAVTLAGRLREvtlEGEGGSAGGSLTGGSRRELLA----ALLEAEAELEELAERLAEEELE 694
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237982 2519 KQQLAASMEEARRRQHEAEEGVRRQQEELQRLAqqqqqqEKLLAEENQRLRERLQHLEEERRAALARSEEIAP 2591
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALE------EQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1073-1842 |
8.46e-20 |
|
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: 98.59 E-value: 8.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1073 QEAEEVLRAHEEQLKEAQAVpatlpeLEATKAALKKLRAQAEAQQPvFDALRDELRgaqevgerlqqrHGERDVEVERWR 1152
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDI------LNELERQLKSLERQAEKAER-YKELKAELR------------ELELALLVLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1153 ErvtlLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVRE---QLRQEKALL 1229
Cdd:TIGR02168 236 E----LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1230 EDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPV-----ASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLT 1304
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEElesleAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1305 SQYIRFISETLRRMEEE-ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAV 1383
Cdd:TIGR02168 392 ELQIASLNNEIERLEARlERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1384 EAQEQKRSIQEELQHLR------QSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAE----GELQALR 1453
Cdd:TIGR02168 472 EAEQALDAAERELAQLQarldslERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalgGRLQAVV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1454 ARAEEAEAQKRQAQEEAERLRR----------QVQDETQRKRQAEAELALRVQAEAEAAREK-QRALQALEELRLQAEEA 1522
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQNELGRVtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKlRKALSYLLGGVLVVDDL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1523 ERRLRQAEAERARQVQVALE---------TAQRSAEAEL-----QSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRA 1588
Cdd:TIGR02168 632 DNALELAKKLRPGYRIVTLDgdlvrpggvITGGSAKTNSsilerRREIEELEEKIEELEEKIAELEKALAELRKELEELE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1589 QQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQEL 1668
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1669 EKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARA 1748
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1749 EEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE------DAVRQRAEAERVLAEKLAAISEATRL 1822
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEElreklaQLELRLEGLEVRIDNLQERLSEEYSL 951
|
810 820
....*....|....*....|.
gi 1920237982 1823 KTEAEIALKEK-EAENERLRR 1842
Cdd:TIGR02168 952 TLEEAEALENKiEDDEEEARR 972
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
153-250 |
1.89e-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: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 153 KLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 231
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1920237982 232 DVPQPDEKSIITYVSSLYD 250
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1319-2055 |
2.05e-19 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 97.20 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1319 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaQAKAQAEREAQGLQRRMQEEVARreeVAVEAQEQKRSIQEELQh 1398
Cdd:NF041483 560 EETERAIAARQAEAAEELTRLHTEAEERLTAAE---EALADARAEAERIRREAAEETER---LRTEAAERIRTLQAQAE- 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1399 lrqsSEAEiqaKARQVEAAERSRLRIEEEIRVVRLQLEA-TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQV 1477
Cdd:NF041483 633 ----QEAE---RLRTEAAADASAARAEGENVAVRLRSEAaAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQ 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1478 QDETQRKRQAEAELAlrvQAEAEAAREKQRALQALEELrlqAEEAERRLRQAEAERARQVqvalETAQRSAeaelqSEHA 1557
Cdd:NF041483 706 EEAARRRREAEETLG---SARAEADQERERAREQSEEL---LASARKRVEEAQAEAQRLV----EEADRRA-----TELV 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1558 SFAEKTAQLERTlkeehvAVVQLREEATRraqqqaeaeraraeaerelerwqlkanEALRLRLQAEEVAQQksLTQAEAE 1637
Cdd:NF041483 771 SAAEQTAQQVRD------SVAGLQEQAEE---------------------------EIAGLRSAAEHAAER--TRTEAQE 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1638 KQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQ--------------- 1702
Cdd:NF041483 816 EADRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSE---AIAEAERLRSDASEYAQRvrteasdtlasaeqd 892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1703 ----RQLLEEELARLQREAAA-----ATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrel 1773
Cdd:NF041483 893 aartRADAREDANRIRSDAAAqadrlIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEA------ 966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1774 AEEAARLRALAEEAKRQrqlAEEDAVRQRAEAERVLAEklaAISEATRLKTEAEialkekeAENERLRRLAEDEAFQRR- 1852
Cdd:NF041483 967 TGEAERLRAEAAETVGS---AQQHAERIRTEAERVKAE---AAAEAERLRTEAR-------EEADRTLDEARKDANKRRs 1033
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1853 ---------LLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELG 1923
Cdd:NF041483 1034 eaaeqadtlITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVEKARTDADELLVGAR 1113
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1924 R----IRGTAEDtLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLK--------AK 1991
Cdd:NF041483 1114 RdataIRERAEE-LRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANseaskvriAA 1192
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1992 VEEARRLRERAEQESARQLQLAQ------EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRS 2055
Cdd:NF041483 1193 VKKAEGLLKEAEQKKAELVREAEkikaeaEAEAKRTVEEGKRELDVLVRRREDINAEISRVQDVLEALES 1262
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
149-248 |
1.41e-18 |
|
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: 83.68 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 149 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 228
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1920237982 229 ED-VDVPQPDEKSIITYVSSL 248
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
767-833 |
3.38e-18 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 81.15 E-value: 3.38e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237982 767 QLKPRSpaHPMRGRVPLLAVCDYKQVEVTVHKGDECQMVGPAQPFYWKVLGSSCSEAAMPSVCFLVP 833
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
149-249 |
4.06e-18 |
|
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: 82.78 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 149 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 228
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1920237982 229 EDVDV--PQPDEKSIITYVSSLY 249
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
145-250 |
4.13e-18 |
|
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: 82.69 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 145 SEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 224
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1920237982 225 LLDPEDV-DVPQPDEKSIITYVSSLYD 250
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
152-248 |
4.60e-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: 82.36 E-value: 4.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 152 EKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 227
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1920237982 228 PEDVDVPQPDEKSIITYVSSL 248
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1313-1901 |
5.57e-18 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 92.29 E-value: 5.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1313 ETLRRMEEEERLAEQQR------AEERERLAEVEAALEKQRQLAEAHAQAKAQAERE-AQGLQRRMQEEVARREEVAVEA 1385
Cdd:COG4913 235 DDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRLWFAQRRLElLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1386 QEQKRSIQEELQHLRQ-----------SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATE-----------RQRG 1443
Cdd:COG4913 315 EARLDALREELDELEAqirgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAeefaalraeaaALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1444 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELrLQAEEAE 1523
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGEL-IEVRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1524 RRLRQAeAERarqvqvALETAQRSaeaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAER 1603
Cdd:COG4913 474 ERWRGA-IER------VLGGFALT----LLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDF 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1604 ELERWQLKANEALRLR---LQAEEVAQ----QKSLTQAEAEKQKEEAEREARRRGKAEE-----QAVRQRELAEQELEK- 1670
Cdd:COG4913 543 KPHPFRAWLEAELGRRfdyVCVDSPEElrrhPRAITRAGQVKGNGTRHEKDDRRRIRSRyvlgfDNRAKLAALEAELAEl 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1671 QRQLAEGTAQ-QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA---ELAKVRAEMEVLLASKA 1746
Cdd:COG4913 623 EEELAEAEERlEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1747 RAEEESRSTSEKsKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRlKTEA 1826
Cdd:COG4913 703 ELEEELDELKGE-IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERID-ALRA 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1827 EIALKEKEAENERLRRLAEDEAFQ-------------RRLLEEQAAQHKADIEARLAQLRKasESELERQKGLVEDTLRQ 1893
Cdd:COG4913 781 RLNRAEEELERAMRAFNREWPAETadldadleslpeyLALLDRLEEDGLPEYEERFKELLN--ENSIEFVADLLSKLRRA 858
|
....*...
gi 1920237982 1894 RRQVEEEI 1901
Cdd:COG4913 859 IREIKERI 866
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1311-1882 |
2.56e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 90.10 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1311 ISETLRRMEEEERLAEQQR----------AEERERLAEVEAALEKQRQlaeahaqAKAQAEREAQGLQRRMQEEVARREE 1380
Cdd:PRK02224 218 LDEEIERYEEQREQARETRdeadevleehEERREELETLEAEIEDLRE-------TIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1381 vaveaqeqkrsIQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAE 1457
Cdd:PRK02224 291 -----------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1458 EAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELALRVQAEAEAAREKQRalQALEELRLQAEEAERRLRQAEAErarqv 1537
Cdd:PRK02224 360 ELREEAAELESELEEAREAV--EDRREEIEELEEEIEELRERFGDAPVDL--GNAEDFLEELREERDELREREAE----- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1538 qvaLETAQRSAEAELQSEHASFAE-KTAQLERTLKE-EHVAVVQLREEatrraqqqaeaeraraeaerelerwQLKANEA 1615
Cdd:PRK02224 431 ---LEATLRTARERVEEAEALLEAgKCPECGQPVEGsPHVETIEEDRE-------------------------RVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1616 LRLRLQAEEVAQQKSLTQAEAEKqkeeaerearrrgKAEEQAVR---QRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1692
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAEDLV-------------EAEDRIERleeRREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1693 RAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAeMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRE 1772
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERRER 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1773 LAEEAARLRALAEEAKRQRqLAEEDAVRQRAEA--ERVlAEKLAAISEAtRLKTEAEIALKEKEAEN-ERLR-RLAEDEA 1848
Cdd:PRK02224 629 LAEKRERKRELEAEFDEAR-IEEAREDKERAEEylEQV-EEKLDELREE-RDDLQAEIGAVENELEElEELReRREALEN 705
|
570 580 590
....*....|....*....|....*....|....*.
gi 1920237982 1849 FQRRL--LEEQAAQHKADIEARLAQLRKASESELER 1882
Cdd:PRK02224 706 RVEALeaLYDEAEELESMYGDLRAELRQRNVETLER 741
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1371-2276 |
4.83e-17 |
|
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: 89.26 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1371 MQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERsrlriEEEIRVVRLQLEATERQRGGAEGELQ 1450
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA-----KKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1451 ALRARAEEAEAQKRQAQEEAERLRRQVQDetqrKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAE 1530
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIE----KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1531 AERARQVQVALETAQRSAEAELQSEHASFAEKtaqleRTLKEEHVAVVQLREEatrraqqqaeaeraraeaerelerwql 1610
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEEL-----EKELKELEIKREAEEE--------------------------- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1611 kANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELI 1690
Cdd:pfam02463 357 -EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1691 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEA----- 1765
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKvllal 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1766 -EAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLA 1844
Cdd:pfam02463 516 iKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIA 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1845 EDEAFQRRLLeeqAAQHKADIEARLAQ---------LRKASESELERQKGLVEDTLRQRRQVEEEILALKG---SFEKAA 1912
Cdd:pfam02463 596 VLEIDPILNL---AQLDKATLEADEDDkrakvvegiLKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEvkaSLSELT 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1913 AGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKV 1992
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1993 EEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAhafAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARE 2072
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK---VEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2073 RAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQaadAEMEKHKQFAEQAL 2152
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKE---EKEKEEKKELEEES 906
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2153 RQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEvteaarQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRD 2232
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE------EADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAI 980
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 1920237982 2233 KDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLA 2276
Cdd:pfam02463 981 EEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
23-132 |
5.15e-17 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 79.30 E-value: 5.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 23 KKTFTKWVNKHL-IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpREKGRMRFHKLQNVQIALDYLR 101
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKI----------NKKPKSPFKKRENINLFLNACK 70
|
90 100 110
....*....|....*....|....*....|...
gi 1920237982 102 HRQV-KLVNIRNDDI-ADGNPKLTLGLIWTIIL 132
Cdd:cd00014 71 KLGLpELDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
22-134 |
5.47e-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: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 22 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPRerdvirssrlPREKGRMRFHKLQNVQIALDY 99
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPG----------IHSRPKTRAQKLENIQACLQF 70
|
90 100 110
....*....|....*....|....*....|....*
gi 1920237982 100 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 134
Cdd:cd21212 71 LAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1318-2189 |
5.86e-17 |
|
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: 89.26 E-value: 5.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1318 MEEEERLAEQQRAEERERLAEVEaaLEKQRQLAEAHAQAKAQAEREAQGLqrRMQEEVARREEVAVEAQEQKRSIQEELQ 1397
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELK--LKEQAKKALEYYQLKEKLELEEEYL--LYLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1398 HLRQSSEAEIQakarqvEAAERSRLRIEEE--IRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1475
Cdd:pfam02463 255 SSKQEIEKEEE------KLAQVLKENKEEEkeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1476 QVQDETQRKRQAEAELAL--RVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERA--RQVQVALETAQRSAEAE 1551
Cdd:pfam02463 329 ELKKEKEEIEELEKELKEleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAakLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1552 LQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSL 1631
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1632 TQAEAEKQKEEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEE 1708
Cdd:pfam02463 489 LLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1709 ELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEaeagrfRELAEEAARLRALAEEAK 1788
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKV------VEGILKDTELTKLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1789 RQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEAR 1868
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1869 LAQLRKaseSELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQ 1948
Cdd:pfam02463 723 LADRVQ---EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1949 laaeeerrrreaeervQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAH 2028
Cdd:pfam02463 800 ----------------EEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEI 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2029 AFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAA 2108
Cdd:pfam02463 864 TKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2109 AEKLRKEAEQEAARRAQAEQAALRQKQAadAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKA 2188
Cdd:pfam02463 944 EADEKEKEENNKEEEEERNKRLLLAKEE--LGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
.
gi 1920237982 2189 E 2189
Cdd:pfam02463 1022 F 1022
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
940-1849 |
5.96e-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: 88.97 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 940 QQLLQSLEQGEQEESRCQRCISELKDiRLQLEACETRTVHRLRLPLDKEPARECAQRITEQQKAQAEVDGLGKGVARLSA 1019
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1020 EAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL---------KTISLVIRSTQEAEEVLRAHEEQLKEAQ 1090
Cdd:TIGR02169 252 ELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvkEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1091 AVPATL-PELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERvtlllerwqavlaqT 1169
Cdd:TIGR02169 322 ERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE--------------L 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1170 DVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAvplansqavreqlrqekalleDIERHGEKVEECQRFAKQY 1249
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1250 INAIKDYELQLVTYKAQLepvaspakkpkvqsgsESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQR 1329
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1330 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGlqrRMQEEVARREEVAVEAQEQKRS-------------IQEEL 1396
Cdd:TIGR02169 511 AVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGN---RLNNVVVEDDAVAKEAIELLKRrkagratflplnkMRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1397 QHLRQSSEA--------------EIQAKARQ-------VEAAERSRlRIEEEIRVVRLQLEATERQ---RGGA-EGELQA 1451
Cdd:TIGR02169 588 RDLSILSEDgvigfavdlvefdpKYEPAFKYvfgdtlvVEDIEAAR-RLMGKYRMVTLEGELFEKSgamTGGSrAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1452 LRARAEEAEAQkrQAQEEAERLRRQVQDETQRKRQAEAELalrvqaeAEAAREKQRALQALEELRLQAEEAERRlRQAEA 1531
Cdd:TIGR02169 667 LFSRSEPAELQ--RLRERLEGLKRELSSLQSELRRIENRL-------DELSQELSDASRKIGEIEKEIEQLEQE-EEKLK 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1532 ERARQVQVALETAQRSAEAElQSEHASFAEKTAQLERTLKEEHVAVVQLREEatrraqqqaeaeraraeaeRELERWQLK 1611
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENV-KSELKELEARIEELEEDLHKLEEALNDLEAR-------------------LSHSRIPEI 796
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1612 ANEalrLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAEQELIR 1691
Cdd:TIGR02169 797 QAE---LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEE 872
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1692 LRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRStsekskqrLEAEAGRFR 1771
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE--------IEDPKGEDE 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1772 ELAEEAARLRALAEEAKR-QRQLAEEDAVRQRA--EAERVLAEKLAAISEATRLKTEAEiALKEKEAENERLRRLAEDEA 1848
Cdd:TIGR02169 945 EIPEEELSLEDVQAELQRvEEEIRALEPVNMLAiqEYEEVLKRLDELKEKRAKLEEERK-AILERIEEYEKKKREVFMEA 1023
|
.
gi 1920237982 1849 F 1849
Cdd:TIGR02169 1024 F 1024
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1289-1942 |
9.80e-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: 88.20 E-value: 9.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1289 EYVDLRTR-----YSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAERE 1363
Cdd:TIGR02169 212 RYQALLKEkreyeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL---LEELNKKIKDLGEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1364 AQGLQRRMQEEVARREEvAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAaersrlrIEEEIRVVRLQLEATERQRG 1443
Cdd:TIGR02169 289 QLRVKEKIGELEAEIAS-LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE-------LEREIEEERKRRDKLTEEYA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1444 GAEGELQALRARAEEAEAQKR--------------QAQEEAERLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRAL 1509
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAetrdelkdyrekleKLKREINELKRELDRLQEELQRLSEELA-DLNAAIAGIEAKINEL 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1510 QA-LEELRLQAEEAERRLRQAEAER--ARQVQVALETAQRSAEAELQS--EHASFAEKTAQLERTLKEEHVAVVQLREEa 1584
Cdd:TIGR02169 440 EEeKEDKALEIKKQEWKLEQLAADLskYEQELYDLKEEYDRVEKELSKlqRELAEAEAQARASEERVRGGRAVEEVLKA- 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1585 trraqQQAEAERARAEAERELERWQLKANEALRLRLQA-----EEVAQQK---------------SLTQAEAEKQKEEAE 1644
Cdd:TIGR02169 519 -----SIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvvedDAVAKEAiellkrrkagratflPLNKMRDERRDLSIL 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1645 REARRRGKA---------EEQAVR---QRELAEQELEKQRQL--------------------------AEGTAQQRLAAE 1686
Cdd:TIGR02169 594 SEDGVIGFAvdlvefdpkYEPAFKyvfGDTLVVEDIEAARRLmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEP 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1687 QELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLL----ASKARAEEESRSTSEKSKQR 1762
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEqeeeKLKERLEELEEDLSSLEQEI 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1763 LEAEAgrfrELAEEAARLRALaEEAKRQRQLAEED--------AVRQRAEAERVLAEKLAAISEATRlktEAEIALKEKE 1834
Cdd:TIGR02169 754 ENVKS----ELKELEARIEEL-EEDLHKLEEALNDlearlshsRIPEIQAELSKLEEEVSRIEARLR---EIEQKLNRLT 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1835 AENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKAsESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAG 1914
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
730 740
....*....|....*....|....*...
gi 1920237982 1915 KAELELELGRIRGTAEDTLRSKEQAEQE 1942
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
149-248 |
1.20e-16 |
|
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: 78.36 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 149 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 228
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1920237982 229 ED-VDVPQPDEKSIITYVSSL 248
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1404-2330 |
5.07e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.89 E-value: 5.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1404 EAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEA-----QKRQAQEEAERLRRQVQ 1478
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellkEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1479 DETQRKRQAEAELALRVQAEAEAAR------EKQRALQALEELRLQAEEAE-----RRLRQAEAERARQVQVALETaqrs 1547
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEleaeiASLERSIAEKERELEDAEER---- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1548 aEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQaeaeraraeaerelerwqlkanEALRLRLQAEEVAQ 1627
Cdd:TIGR02169 324 -LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL----------------------EDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1628 QKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1706
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1707 EEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAEAGRFRELAEeaarlral 1783
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGVHGTVAQLGS-------- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1784 aeeAKRQRQLAEEDAVRQRAEAERVLAEKLAAiseatrlktEAEIALKEKEAENER---LRRLAEDEAFQRRLLEEQAAQ 1860
Cdd:TIGR02169 533 ---VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKMRDERRDLSILSEDGVIG 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1861 HKADIEARLAQLRKASESELeRQKGLVEDTLRQRRQVEE-EILALKGS-FEKAAA--GKAElelelgRIRGTAEDTLRSK 1936
Cdd:TIGR02169 601 FAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLMGKyRMVTLEGElFEKSGAmtGGSR------APRGGILFSRSEP 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1937 EQAEQEAARqrqlaaeeerrrreaeervqkslaaEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ-----ESARQLQ 2011
Cdd:TIGR02169 674 AELQRLRER-------------------------LEGLKRELSSLQSELRRIENRLDELSQELSDASRkigeiEKEIEQL 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2012 LAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRseaeaarraAEEAEAARERAEREAAQSRRQVEEAERL 2091
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE---------EDLHKLEEALNDLEARLSHSRIPEIQAE 799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2092 KQSAEeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEE 2171
Cdd:TIGR02169 800 LSKLE--------------EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2172 tdhqksiLDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRlLQEEAEKMKQVA 2251
Cdd:TIGR02169 866 -------LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEIE 937
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 2252 EEAARLSVAAQEAARLRQLAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQ 2330
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1098-2024 |
5.12e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 86.18 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1098 ELEATKAALKKLRAQAEAQQPVFDALRDELRGaqevgerlqqrhgerdveverwrervtlllerwqavlaqtdvRQRELE 1177
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQ------------------------------------------ELKLKE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1178 QLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALL-EDIERHGEKVEECQRFAKQYINAIKDY 1256
Cdd:pfam02463 205 QAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSkQEIEKEEEKLAQVLKENKEEEKEKKLQ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1257 ELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRtryselstltsqyIRFISETLRRMEEEERLAEQQRAEERERL 1336
Cdd:pfam02463 285 EEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE-------------KKKAEKELKKEKEEIEELEKELKELEIKR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1337 AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQsseaeiQAKARQVEA 1416
Cdd:pfam02463 352 EAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQ------LEDLLKEEK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1417 AERSRLRIEEEIRVVRLQLEATERQrggaegelqaLRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQ 1496
Cdd:pfam02463 426 KEELEILEEEEESIELKQGKLTEEK----------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1497 AEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ-LERTLKEEHV 1575
Cdd:pfam02463 496 EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQkLVRALTELPL 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1576 AVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGK--A 1653
Cdd:pfam02463 576 GARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVslE 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1654 EEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAK 1733
Cdd:pfam02463 656 EGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKIN 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1734 VRAEMEVLLASKARAEEESRSTSEKSKQRLEAEagrfRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKL 1813
Cdd:pfam02463 736 EELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE----LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1814 AAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDT-LR 1892
Cdd:pfam02463 812 EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELeSK 891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1893 QRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAArQRQLAAEEERRRREAEERVQKSLAAEE 1972
Cdd:pfam02463 892 EEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE-EADEKEKEENNKEEEEERNKRLLLAKE 970
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 1973 EAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAE 2024
Cdd:pfam02463 971 ELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1116-2026 |
8.77e-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: 85.23 E-value: 8.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1116 QQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQA----------VLAQTDVRQRELEQLGRQLRY 1185
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeeMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1186 YRESADPLGAWLRDAKQR-QEQIQAVP--LANSQAVREQLRQEKALLE-DIERHGEKVEECQRFAKQYINAIKDYELQLV 1261
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKmQQHIQDLEeqLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1262 TYKAQLEPVASPAKK-PKVQSGSESIIQEyVDLRTRYSElstltsqyirfisETLRRMEEEERLAEQQRAEERERLAEVE 1340
Cdd:pfam01576 163 EFTSNLAEEEEKAKSlSKLKNKHEAMISD-LEERLKKEE-------------KGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1341 AalekqrQLAEAHAQAkAQAEREAQGLQRRMQEEVARREevavEAQEQKRSIQEELQHLRQSSEAEIQAKARqveaAERS 1420
Cdd:pfam01576 229 A------QIAELRAQL-AKKEEELQAALARLEEETAQKN----NALKKIRELEAQISELQEDLESERAARNK----AEKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1421 RLRIEEEIRVVRLQLEATErqrgGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELalrvqaeA 1499
Cdd:pfam01576 294 RRDLGEELEALKTELEDTL----DTTAAQQELRSKREqEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-------T 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1500 EAAREKQRALQALEELRlQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEktAQLERTLKEEHVAVVQ 1579
Cdd:pfam01576 363 EQLEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAEKLSKLQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1580 LREEATRRAQQQAEAERARAEAERELERWQLKANEALRlrlqAEEVAQQKSLTQAEAEKqkeeaerearrrgkaEEQAVR 1659
Cdd:pfam01576 440 SELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL----QEETRQKLNLSTRLRQL---------------EDERNS 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1660 QRELAEQELEKQRQLaegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAK------ 1733
Cdd:pfam01576 501 LQEQLEEEEEAKRNV----ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektkn 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1734 -VRAEMEVLLAS-------------------KARAEEESRSTS-EKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQ 1792
Cdd:pfam01576 577 rLQQELDDLLVDldhqrqlvsnlekkqkkfdQMLAEEKAISARyAEERDRAEAEA---REKETRALSLARALEEALEAKE 653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1793 LAEEDAVRQRAEAERVLAEKLAA---ISEATRLKTEAEIALKEKEAENERLR-RLAEDEAFQRRL---LEEQAAQHKADI 1865
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVgknVHELERSKRALEQQVEEMKTQLEELEdELQATEDAKLRLevnMQALKAQFERDL 733
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1866 EARlaqlrkaSESELERQKGLVedtlRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAAR 1945
Cdd:pfam01576 734 QAR-------DEQGEEKRRQLV----KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1946 QRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAE 2024
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQD 882
|
..
gi 1920237982 2025 EK 2026
Cdd:pfam01576 883 EK 884
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
153-250 |
1.03e-15 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 76.07 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 153 KLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 231
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1920237982 232 DVPQPDEKSIITYVSSLYD 250
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1331-1893 |
1.24e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 84.58 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1331 EERERLAEVEAALEKQRQLAEAHAQAKAQAEreaqglQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRqsseaeIQAK 1410
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDARE------QIELLEPIRELAERYAAARERLAELEYLRAALR------LWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1411 ARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE-AQKRQAQEEAERLRRQvQDETQRKRQAEA 1489
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERE-LEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1490 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQS-------EHASFAEK 1562
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASlerrksnIPARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1563 TAQLERTLKEEHVAV------VQLREEAtrraqqqaeaeraraeaerelERWQLKANEAL---RLRL--------QAEEV 1625
Cdd:COG4913 446 RDALAEALGLDEAELpfvgelIEVRPEE---------------------ERWRGAIERVLggfALTLlvppehyaAALRW 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1626 AQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEK--QRQLAEGTAQQRLAAEQELIRL-RAETEQG--- 1699
Cdd:COG4913 505 VNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFDYVCVDSPEELRRHpRAITRAGqvk 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1700 ------------------------EQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRST 1755
Cdd:COG4913 585 gngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1756 S-EKSKQRLEAEagrFRELAEEAARLRALAEEAKRQRQlAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKE 1834
Cdd:COG4913 665 SaEREIAELEAE---LERLDASSDDLAALEEQLEELEA-ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 1835 AENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRkaseSELERQKGLVEDTLRQ 1893
Cdd:COG4913 741 DLARLELRALLEERFAAALGDAVERELRENLEERIDALR----ARLNRAEEELERAMRA 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
895-1583 |
1.30e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 84.72 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 895 EQRQALRSLELHYQA----FLRDSQDAGgfgPEDRLQAEREYGSCSRHYQQLLQSLEQGEQE----ESRCQRCISELKDI 966
Cdd:TIGR02168 217 ELKAELRELELALLVlrleELREELEEL---QEELKEAEEELEELTAELQELEEKLEELRLEvselEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 967 RLQLEACETRTVH---RLRlPLDKEPARECAQRITEQQKAQAEVDGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELEL 1043
Cdd:TIGR02168 294 ANEISRLEQQKQIlreRLA-NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1044 TLGKL-EQVRSLSAIYLEKLKTISLvIRSTQEaeeVLRAHEEQLKEAQAVPATlpelEATKAALKKLRAQAEAQQPVFDA 1122
Cdd:TIGR02168 373 RLEELeEQLETLRSKVAQLELQIAS-LNNEIE---RLEARLERLEDRRERLQQ----EIEELLKKLEEAELKELQAELEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1123 LRDELRGAQEVGERLQQRHGERDVEVERWRERVTLL---LERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRD 1199
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1200 AKQR---------------QEQIQAVPLANSQAVR---EQLRQEK----ALLEDIERHGEKVEECQRFAKQYINAIKDYE 1257
Cdd:TIGR02168 525 LSELisvdegyeaaieaalGGRLQAVVVENLNAAKkaiAFLKQNElgrvTFLPLDSIKGTEIQGNDREILKNIEGFLGVA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1258 LQLVTYKAQLEPVASP---------------AKKPKVQSGSESIIQEYVDLRTRYS--------ELSTL-TSQYIRFISE 1313
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYllggvlvvddldnalELAKKLRPGYRIVTLDGDLVRPGGVitggsaktNSSILeRRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1314 TLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQ 1393
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1394 EELQHLRQSSEAEiqakarqvEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1473
Cdd:TIGR02168 765 ELEERLEEAEEEL--------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1474 RRQVQDETQRKRQAEAELAlrvqaeaeaarekqRALQALEELRLQAEEAERRLRQAEAERArQVQVALETAqRSAEAELQ 1553
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIE--------------SLAAEIEELEELIEELESELEALLNERA-SLEEALALL-RSELEELS 900
|
730 740 750
....*....|....*....|....*....|..
gi 1920237982 1554 SEHASFAEKTAQLERTLKE--EHVAVVQLREE 1583
Cdd:TIGR02168 901 EELRELESKRSELRRELEElrEKLAQLELRLE 932
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1288-1944 |
2.55e-15 |
|
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: 83.73 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1288 QEYVDLRTRYSELSTLTSQYIRFISETLRRMEE-EERLAE--QQRAEERERLAEVEAALEKQRQLAEAhAQAKAQAEREA 1364
Cdd:pfam12128 248 QEFNTLESAELRLSHLHFGYKSDETLIASRQEErQETSAElnQLLRTLDDQWKEKRDELNGELSAADA-AVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1365 QGLQRRMQEEVarREEVAVEAQEQKRSIQEELQHLRQSSEAeIQAKARQVEAA-ERSRLRIEEEIR--VVRL------QL 1435
Cdd:pfam12128 327 LEDQHGAFLDA--DIETAAADQEQLPSWQSELENLEERLKA-LTGKHQDVTAKyNRRRSKIKEQNNrdIAGIkdklakIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1436 EATERQRGGAEGELQALRAR-AEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEA-----EAAREKQ--- 1506
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENfderiERAREEQeaa 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1507 -----RALQALEELRLQAEEAERRLRQAEAeRARQVQVALETAQR-------------SAEAELQSEHASFAEKTAQLER 1568
Cdd:pfam12128 484 naeveRLQSELRQARKRRDQASEALRQASR-RLEERQSALDELELqlfpqagtllhflRKEAPDWEQSIGKVISPELLHR 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1569 TLKEEHVAVVQLREEATRRaqqqaeaeraraeaerelerwqlkaneALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREAR 1648
Cdd:pfam12128 563 TDLDPEVWDGSVGGELNLY---------------------------GVKLDLKRIDVPEWAASEEELRERLDKAEEALQS 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1649 RRGKAEEQAvRQRELAEQELEKQrQLAEGTAQQRLA-AEQELIRLraeTEQGEQQRQLLEEELARLQREaaaATQKRREL 1727
Cdd:pfam12128 616 AREKQAAAE-EQLVQANGELEKA-SREETFARTALKnARLDLRRL---FDEKQSEKDKKNKALAERKDS---ANERLNSL 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1728 EAELAKVraEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQraeaer 1807
Cdd:pfam12128 688 EAQLKQL--DKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRD------ 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1808 vLAEKlaAISEATRLKTEAEIalKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASeSELERQKG-L 1886
Cdd:pfam12128 760 -LASL--GVDPDVIAKLKREI--RTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAI-SELQQQLArL 833
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237982 1887 VEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTlrSKEQAEQEAA 1944
Cdd:pfam12128 834 IADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDA--NSEQAQGSIG 889
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2779-2817 |
2.57e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 72.36 E-value: 2.57e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1920237982 2779 LLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEMNRVL 2817
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3438-3476 |
5.82e-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: 5.82e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1920237982 3438 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFDEEMNRVL 3476
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4016-4054 |
5.82e-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: 5.82e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1920237982 4016 LLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEMNEIL 4054
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
16-133 |
7.74e-15 |
|
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: 73.47 E-value: 7.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 16 DERDrvqKKTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLsgDSLprERDVIRSSRLPREKGRMRFHKLQNVQI 95
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKI--QPGCVNWKKVNKPKPLNKFKKVENCNY 69
|
90 100 110
....*....|....*....|....*....|....*...
gi 1920237982 96 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 133
Cdd:cd21219 70 AVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
151-262 |
8.73e-15 |
|
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: 73.49 E-value: 8.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 151 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 230
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 1920237982 231 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 262
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1722-2589 |
9.38e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.04 E-value: 9.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1722 QKRRELEAELAKVrAEMEvllASKARAEEESrstsEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEdavRQ 1801
Cdd:TIGR02169 153 VERRKIIDEIAGV-AEFD---RKKEKALEEL----EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE---KR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1802 RAEAERVLAEKLAAisEATRLKTEAEIAlkEKEAENERLRRLAEDeafqrrlLEEQAAQHKADIEARLAQLRKASESELE 1881
Cdd:TIGR02169 222 EYEGYELLKEKEAL--ERQKEAIERQLA--SLEEELEKLTEEISE-------LEKRLEEIEQLLEELNKKIKDLGEEEQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1882 RQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDtlrSKEQAEQEAARQRQLAAEEERRRREAE 1961
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1962 ERVQKSLAAEEEAARQR---KAALEEVERLKAKVEE----ARRLRERAEQESARQLQLAQ-----EAAQKRLQAEEKAHA 2029
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRdelKDYREKLEKLKREINElkreLDRLQEELQRLSEELADLNAaiagiEAKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2030 FAVQQKEQELQQTLQQEQSVLERLRseaeaarraaeeaeaareraerEAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAA 2109
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELY----------------------DLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2110 EKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTAlrlqleetdhQKSIldEELQRLKA- 2188
Cdd:TIGR02169 506 VRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVA----------KEAI--ELLKRRKAg 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2189 EVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENR-----------ALVLRDKDSAQRLLQ---------EEAEKMK 2248
Cdd:TIGR02169 574 RATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdTLVVEDIEAARRLMGkyrmvtlegELFEKSG 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2249 QVA----EEAARLSVAAQEAARLRQLAEE---------DLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2315
Cdd:TIGR02169 654 AMTggsrAPRGGILFSRSEPAELQRLRERleglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2316 QARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARaeEDARRFRKQAEDIGERLYRTE 2395
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2396 LATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQalqqsfLSEKDS 2475
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD------LESRLG 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2476 LLQRERC-IEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEG---------VRRQQE 2545
Cdd:TIGR02169 886 DLKKERDeLEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsledvqaeLQRVEE 965
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 1920237982 2546 ELQRLAQQQQQQEKLLAEENQR---LRERLQHLEEERRAALARSEEI 2589
Cdd:TIGR02169 966 EIRALEPVNMLAIQEYEEVLKRldeLKEKRAKLEEERKAILERIEEY 1012
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
19-130 |
9.43e-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: 73.33 E-value: 9.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 19 DRVQKKTFTKWVNKHLIKAQ-RHISDLYEDLRDGHNLISLLEVLSGDSLPRERDVIRSSRLPRekgrmrfhkLQNVQIAL 97
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEPKNRIQM---------IQNLHLAM 72
|
90 100 110
....*....|....*....|....*....|....
gi 1920237982 98 DYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTI 130
Cdd:cd21225 73 LFIEEDlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
837-1567 |
1.15e-14 |
|
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: 81.64 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 837 QEAQEAIARLEAQHQALVALWHQLHTEMKSLLAWQSLGRDMQLIRSWSLATFRTLKpEEQRQALRSLELHYQAFLRDSQD 916
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL-EELKEELESLEAELEELEAELEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 917 AggfgpEDRLQA-EREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQ 995
Cdd:TIGR02168 370 L-----ESRLEElEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 996 RITEQQKAQAEVDGLGKGVARLSAE-AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLS---AIYLEKLKTISLVIRS 1071
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREElEEAEQALDAAERELAQLQARLDSLERLQENLEGFSegvKALLKNQSGLSGILGV 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1072 TQEAEEVlrahEEQLKeaQAVPATLPE---------LEATKAALKKLrAQAEAQQPVFDALrDELRGAQEVGERLQQRHG 1142
Cdd:TIGR02168 525 LSELISV----DEGYE--AAIEAALGGrlqavvvenLNAAKKAIAFL-KQNELGRVTFLPL-DSIKGTEIQGNDREILKN 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1143 ERDV-----EVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYR------ESADPLGAWLRDAKQRqeqiQAVP 1211
Cdd:TIGR02168 597 IEGFlgvakDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRivtldgDLVRPGGVITGGSAKT----NSSI 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1212 LANSQAVREqLRQEKALLEDIERHGEKveecqrfakqyinAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYV 1291
Cdd:TIGR02168 673 LERRREIEE-LEEKIEELEEKIAELEK-------------ALAELRKELEELEEELE---------QLRKELEELSRQIS 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1292 DLRTRYSELST---LTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQ 1368
Cdd:TIGR02168 730 ALRKDLARLEAeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1369 ---RRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQR 1442
Cdd:TIGR02168 810 aelTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelsEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1443 GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA-LRVQAEAEAAREKQRALQALEELRLQAEE 1521
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1920237982 1522 AERRLRQAEAERARQVQVALEtaqrsAEAELQSEHASFAEKTAQLE 1567
Cdd:TIGR02168 970 ARRRLKRLENKIKELGPVNLA-----AIEEYEELKERYDFLTAQKE 1010
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1218-1882 |
1.29e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 81.50 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1218 VREQLRQEKALLEDIERhgekveecqrfAKQYINAIKDYELQLVTYKAQ---LEPVaspakkpkvqsgsESIIQEYVDLR 1294
Cdd:COG4913 213 VREYMLEEPDTFEAADA-----------LVEHFDDLERAHEALEDAREQielLEPI-------------RELAERYAAAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1295 TRYSELSTLTSQY-IRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ----LAEAHAQAKAQAEREAQGLQR 1369
Cdd:COG4913 269 ERLAELEYLRAALrLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREeldeLEAQIRGNGGDRLEQLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1370 RMQEEVARREEVAVEAQEQKRSI--------------QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQL 1435
Cdd:COG4913 349 RLERELEERERRRARLEALLAALglplpasaeefaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1436 EATERQRGGAEGELQALRARAEEAeaqkrqAQEEAERLR-----RQVQDETQRKRQAeAELALRVQA-----EAEAAREK 1505
Cdd:COG4913 429 ASLERRKSNIPARLLALRDALAEA------LGLDEAELPfvgelIEVRPEEERWRGA-IERVLGGFAltllvPPEHYAAA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1506 QRALQALE-ELRLQAEEAERRLRQAEAER------ARQVQVALETAQRSAEAELQSehaSFAEKTAQLERTLKEEHVAV- 1577
Cdd:COG4913 502 LRWVNRLHlRGRLVYERVRTGLPDPERPRldpdslAGKLDFKPHPFRAWLEAELGR---RFDYVCVDSPEELRRHPRAIt 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1578 --VQLREEATrraqqqaeaERARAEAERELERWQL-KANEALRLRLQAEEVAQQKSLTQAEAEKQKEeaerearrrgKAE 1654
Cdd:COG4913 579 raGQVKGNGT---------RHEKDDRRRIRSRYVLgFDNRAKLAALEAELAELEEELAEAEERLEAL----------EAE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1655 EQAVRQRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQREAAAATQKRRELEAEL 1731
Cdd:COG4913 640 LDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEI 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1732 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAE 1811
Cdd:COG4913 716 GRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 1812 -KLAAISEATRLKTEAEiALKEKEAENERLR--RLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELER 1882
Cdd:COG4913 796 fNREWPAETADLDADLE-SLPEYLALLDRLEedGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1073-1573 |
1.31e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.24 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1073 QEAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRaqaeaqqpvfDALRDELRGAQEVGERLQQRHGERDVEVERWR 1152
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAETERER----------EELAEEVRDLRERLEELEEERDDLLAEAGLDD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1153 ERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQ---AVPLANSQAVREQLRQEKALL 1229
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRREEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1230 EDIERHGEKVEEcqRFAKqyinaikdyelqlvtykaqlepvaSPAKKPKVQSGSESIIQEYVDLRTRYSELSTLtsqyir 1309
Cdd:PRK02224 387 EELEEEIEELRE--RFGD------------------------APVDLGNAEDFLEELREERDELREREAELEAT------ 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1310 fISETLRRMEEEERLAEQQR-----------------AEERERLAEVEAALE----KQRQLAEAHAQAK--AQAEREAQG 1366
Cdd:PRK02224 435 -LRTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEdleeEVEEVEERLERAEdlVEAEDRIER 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1367 LQRR---MQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvRLQLEATERQRG 1443
Cdd:PRK02224 514 LEERredLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1444 GAEGELQALRARAE---EAEAQKRQAQEEAERLRR-QVQDETQRKRQAEAELAlrvQAEAEAARE-KQRALQALeelrlq 1518
Cdd:PRK02224 592 ERIRTLLAAIADAEdeiERLREKREALAELNDERReRLAEKRERKRELEAEFD---EARIEEAREdKERAEEYL------ 662
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 1519 aEEAERRLRQAEAERAR-QVQVALETAQRSAEAELQSEHASFAEKTAQLErTLKEE 1573
Cdd:PRK02224 663 -EQVEEKLDELREERDDlQAEIGAVENELEELEELRERREALENRVEALE-ALYDE 716
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
151-250 |
1.94e-14 |
|
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: 72.31 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 151 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 230
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1920237982 231 VDV--PQPDEKSIITYVSSLYD 250
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1033-1786 |
1.96e-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: 80.78 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1033 AAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLkeaqavPATLPELEATKAALKKLRAQ 1112
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCM------PDTYHERKQVLEKELKHLRE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1113 AEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEverwrervtllLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdp 1192
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAR-----------IEELRAQEAVLEETQERINRARKAAPLAAHIK-- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1193 lgAWLRDAKQRQEQIQAvpLANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVAS 1272
Cdd:TIGR00618 301 --AVTQIEQQAQRIHTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1273 PAKKPKVQSGSESIIQEyvDLRTRYSELSTLTSQYIRFISETLRRMEEEERL--AEQQRAEERERLAEVEAALEKQRQ-- 1348
Cdd:TIGR00618 377 LTQHIHTLQQQKTTLTQ--KLQSLCKELDILQREQATIDTRTSAFRDLQGQLahAKKQQELQQRYAELCAAAITCTAQce 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1349 -LAEAHAQAKAQAERE-------AQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEA--EIQAKARQVEAAE 1418
Cdd:TIGR00618 455 kLEKIHLQESAQSLKEreqqlqtKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDidNPGPLTRRMQRGE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1419 RSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRaRAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAE 1498
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ-QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1499 AEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVV 1578
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLT 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1579 QLREEATRRAQQQAEAERARAEAERELERWQLkANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREArrrgkaEEQAV 1658
Cdd:TIGR00618 694 YWKEMLAQCQTLLRELETHIEEYDREFNEIEN-ASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE------AHFNN 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1659 RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR-----QLLEEELARLQREAAAATQKRRELEAELAK 1733
Cdd:TIGR00618 767 NEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsdeDILNLQCETLVQEEEQFLSRLEEKSATLGE 846
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1920237982 1734 VRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEE 1786
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE 899
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1313-1804 |
2.08e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 80.20 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1313 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHA--QAKAQAEREAQGLQRRMQEEVARREEVAvEAQEQKR 1390
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELR-ELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1391 SIQEELQHLRQSSEaeiqakarqvEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1470
Cdd:COG4717 167 ELEAELAELQEELE----------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1471 ER--LRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSA 1548
Cdd:COG4717 237 EAaaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1549 EAElqsehasfaektaQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAqq 1628
Cdd:COG4717 317 EEE-------------ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV-- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1629 ksltqaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQqrqlLEE 1708
Cdd:COG4717 382 -----------------------EDEEELRAALEQAEEYQELKEELEE--LEEQLEELLGELEELLEALDEEE----LEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1709 ELARLQREAAAATQKRRELEAELAKVRAEMEVLlaskaraeeESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAK 1788
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQL---------EEDGELAELLQELEELKAELRELAEEWAALKLALELLE 503
|
490
....*....|....*....
gi 1920237982 1789 RQRQLAEED---AVRQRAE 1804
Cdd:COG4717 504 EAREEYREErlpPVLERAS 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
923-1462 |
3.68e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 923 EDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLrlpldkeparecAQRITEQQK 1002
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL------------EELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1003 AQAEVDGLGKGVARLSAEAEKVLAlpepspaapTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAH 1082
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEE---------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1083 EEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERw 1162
Cdd:COG1196 413 LERLERLEE------ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE- 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1163 qavlaqtdvRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEkALLEDIERHGEKVEEC 1242
Cdd:COG1196 486 ---------LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA-LEAALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1243 QRFAKQYINAIKDYELQLVT-YKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEE 1321
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1322 ERLAEQQRAEERERLAEVEAALEKQRqLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQ 1401
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGS-LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237982 1402 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1462
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1307-2026 |
4.02e-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: 79.63 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1307 YIRFISETLRRMEEEERLAEQQRAEERERLAEVEAaLEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQ 1386
Cdd:TIGR00618 140 YKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFP-LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1387 EQKRSIQEELQHLR--QSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQAL---RARAEEAEA 1461
Cdd:TIGR00618 219 ERKQVLEKELKHLReaLQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERInraRKAAPLAAH 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1462 QKRQAQEEAERLRRQVQ-DETQRKRQAEAELALRVQAEAEAAREKQRALQAL--EELRLQAEEAERRLRQAEAERARQVQ 1538
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTElQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLhsQEIHIRDAHEVATSIREISCQQHTLT 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1539 VALETAQRSAEAELQSEHASFAEKTaqlertlkeehvavvQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRL 1618
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELD---------------ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELC 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1619 RLQAEEVAQQKSLTQAEAEKQKEEAerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtaqQRLAAEQELIRLRAETEQ 1698
Cdd:TIGR00618 444 AAAITCTAQCEKLEKIHLQESAQSL--------KEREQQLQTKEQIHLQETRKKAVVL----ARLLELQEEPCPLCGSCI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1699 GEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLAS----KARAEEESRSTSEKSKQR---------LEA 1765
Cdd:TIGR00618 512 HPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQraslKEQMQEIQQSFSILTQCDnrskedipnLQN 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1766 EAGRFRELAEEAARLR-ALAEEAKRQ-RQLAEEDAVRQRAEAERVLAEKLAaiSEATRLKTEAEIALKEKEAENERLRRL 1843
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEdMLACEQHALlRKLQPEQDLQDVRLHLQQCSQELA--LKLTALHALQLTLTQERVREHALSIRV 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1844 AEDEAFQRRLLEEQAAQHKADieaRLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELG 1923
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKE---QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1924 RIRGTAEDTLRSKEQAEQEAARQrqlaaeeerrRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAE 2003
Cdd:TIGR00618 747 ELMHQARTVLKARTEAHFNNNEE----------VTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE 816
|
730 740
....*....|....*....|....
gi 1920237982 2004 QE-SARQLQLAQEAAQKRLQAEEK 2026
Cdd:TIGR00618 817 DIlNLQCETLVQEEEQFLSRLEEK 840
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
22-134 |
4.30e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 71.17 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 22 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerDVIRSsrlPREKGRMRfhklQNVQIALDY 99
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLP---GIDWN---PTTDAERK----ENVEKVLQF 70
|
90 100 110
....*....|....*....|....*....|....*
gi 1920237982 100 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 134
Cdd:cd21213 71 MASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
149-246 |
5.08e-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: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 149 TAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI----DMNKVYRqtnLENLDQAFSVAERDLGVTR 224
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
|
90 100
....*....|....*....|..
gi 1920237982 225 LLDPEDVDVPQPDEKSIITYVS 246
Cdd:cd21230 75 LITPEEIINPNVDEMSVMTYLS 96
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
151-254 |
5.17e-14 |
|
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: 71.23 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 151 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 230
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1920237982 231 VDV--PQPDEKSIITYVSSLYDAMPR 254
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1125-1904 |
5.42e-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: 79.34 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1125 DELRGAQEVGERLQQRHGERDvEVERWRERVTLLLERwqaVLAQTDVRQRELEQLGRqlryYREsadplgawLRDAKQRQ 1204
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELE-EVEENIERLDLIIDE---KRQQLERLRREREKAER----YQA--------LLKEKREY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1205 EQiqAVPLANSQAVREQLRQEKALLEDIERHGEKVEEcqrfakqyinAIKDYELQLVTYKAQLEPVASPAKKpkvqSGSE 1284
Cdd:TIGR02169 224 EG--YELLKEKEALERQKEAIERQLASLEEELEKLTE----------EISELEKRLEEIEQLLEELNKKIKD----LGEE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1285 SIIQEYVDLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREA 1364
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERS-IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1365 QGLQRRMQEEVARREEVAVEAQEQKRSIqEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGG 1444
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKL-EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1445 AEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRALQALEEL---RLQA-- 1519
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVlkaSIQGvh 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1520 ----------EEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFA-----EKTAQLERTLKEEHVA-------- 1576
Cdd:TIGR02169 525 gtvaqlgsvgERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRAtflplNKMRDERRDLSILSEDgvigfavd 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1577 --------------------VVQLREEATRRAQQQAEAERA--------------RAEAERELERWQLKAnEALRLRLQA 1622
Cdd:TIGR02169 605 lvefdpkyepafkyvfgdtlVVEDIEAARRLMGKYRMVTLEgelfeksgamtggsRAPRGGILFSRSEPA-ELQRLRERL 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1623 EEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAV---RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG 1699
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGeieKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1700 EQQRQLLEEELARLQreAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTsEKSKQRLEAEAGRFRELAEEAAR 1779
Cdd:TIGR02169 764 EARIEELEEDLHKLE--EALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI-EQKLNRLTLEKEYLEKEIQELQE 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1780 LRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAA 1859
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1860 QHKADIEA---RLAQLRKASESELERQKGL--VEDTLRQRRQVEEEILAL 1904
Cdd:TIGR02169 921 ELKAKLEAleeELSEIEDPKGEDEEIPEEElsLEDVQAELQRVEEEIRAL 970
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
154-249 |
6.04e-14 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 70.85 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 154 LLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 232
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1920237982 233 VPQPDEKSIITYVSSLY 249
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1300-2211 |
7.81e-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: 78.68 E-value: 7.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1300 LSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEV----EAALEKQRQLAEAHAQAkAQAEREAQGLQRRMQEEV 1375
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEStdlqEQIAELQAQIAELRAQL-AKKEEELQAALARLEEET 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1376 ARREEvaveAQEQKRSIQEELQHLRQSSEAEIQAKARqveaAERSRLRIEEEIRVVRLQLEATErqrgGAEGELQALRAR 1455
Cdd:pfam01576 257 AQKNN----ALKKIRELEAQISELQEDLESERAARNK----AEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1456 AE-EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlrvqaeaEAAREKQRALQALEELRlQAEEAERRLRQAEAERA 1534
Cdd:pfam01576 325 REqEVTELKKALEEETRSHEAQLQEMRQKHTQALEELT-------EQLEQAKRNKANLEKAK-QALESENAELQAELRTL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1535 RQVQVALETAQRSAEAELQSEHASFAEktAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANE 1614
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1615 ALRlrlqAEEVAQQKSLTQAEAEKqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAegtaQQRLAAEQELIRLRA 1694
Cdd:pfam01576 475 ELL----QEETRQKLNLSTRLRQL---------------EDERNSLQEQLEEEEEAKRNVE----RQLSTLQAQLSDMKK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1695 ETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAK-------VRAEMEVLLAS-------------------KARA 1748
Cdd:pfam01576 532 KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrLQQELDDLLVDldhqrqlvsnlekkqkkfdQMLA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1749 EEESRSTS-EKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAA---ISEATRLKT 1824
Cdd:pfam01576 612 EEKAISARyAEERDRAEAEA---REKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVgknVHELERSKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1825 EAEIALKEKEAENERLR-RLAEDEAFQRRL---LEEQAAQHKADIEARlaqlrkaSESELERQKGLVedtlRQRRQVEEE 1900
Cdd:pfam01576 689 ALEQQVEEMKTQLEELEdELQATEDAKLRLevnMQALKAQFERDLQAR-------DEQGEEKRRQLV----KQVRELEAE 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1901 ILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 1980
Cdd:pfam01576 758 LEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKN 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1981 ALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAEEKAHAFA-VQQKEQELQQTLQQEQSVLERLRSEAE 2058
Cdd:pfam01576 838 LEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELLNDRLRKSTL 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2059 AARR---AAEEAEAARERAEREAAQSRRQVEEAeRLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQ 2135
Cdd:pfam01576 918 QVEQlttELAAERSTSQKSESARQQLERQNKEL-KAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKL 996
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2136 AADAE---------MEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2206
Cdd:pfam01576 997 VRRTEkklkevllqVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVST 1076
|
....*
gi 1920237982 2207 LRVQM 2211
Cdd:pfam01576 1077 LKSKL 1081
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3697-3735 |
1.19e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 67.35 E-value: 1.19e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1920237982 3697 LLEAQAATGFLLDPVKGERLAVDEAVRKGLVGPELHDRL 3735
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1049-1552 |
1.52e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.65 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1049 EQVRSLSAI--YLEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPatlpELEATKAALKKLRAQAEAQQPVFDALRDE 1126
Cdd:COG4913 249 EQIELLEPIreLAERYAAARERLAELEYLRAALRLWFAQRRLELLEA----ELEELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1127 LRGAQEV-----GERLQQRhgERDVE-VERWRERVTLLLERWQAVLAQTDVR---------------QRELEQLGRQLRY 1185
Cdd:COG4913 325 LDELEAQirgngGDRLEQL--EREIErLERELEERERRRARLEALLAALGLPlpasaeefaalraeaAALLEALEEELEA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1186 YRESADPLGAWLRDAKQRQEQIQA-----------VPlANSQAVREQLRQEKALLED---------------------IE 1233
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAeiaslerrksnIP-ARLLALRDALAEALGLDEAelpfvgelievrpeeerwrgaIE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1234 R--HGEK----VEEcQRFAK--QYINAIKDyELQLVTYKAQLEPVASPAKKPKVQS------GSESIIQEYVD--LRTRY 1297
Cdd:COG4913 482 RvlGGFAltllVPP-EHYAAalRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSlagkldFKPHPFRAWLEaeLGRRF 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1298 S--------ELST----LTSQYIRFISETLRRMEEEERL---------AEQQRAEERERLAEVEAALEKQRQLAEAHAQA 1356
Cdd:COG4913 560 DyvcvdspeELRRhpraITRAGQVKGNGTRHEKDDRRRIrsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1357 KAQAEREAQGLQRRmqEEVARREEVAVEAQEQKRSIQEELQHLRQSSeAEIQAKARQVEAAERSRLRIEEEIRVVRLQLE 1436
Cdd:COG4913 640 LDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIG 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1437 ATERQRGGAEGELQALRARAEEAE------------------AQKRQAQEEAERLRRQVQDETQRKRQAEAEL------- 1491
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEdlarlelralleerfaaaLGDAVERELRENLEERIDALRARLNRAEEELeramraf 796
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237982 1492 -------ALRVQAEAEAAREKQRALQALEELRL---QAEEAERRLRQAEAERArQVQVALETAQRSAEAEL 1552
Cdd:COG4913 797 nrewpaeTADLDADLESLPEYLALLDRLEEDGLpeyEERFKELLNENSIEFVA-DLLSKLRRAIREIKERI 866
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1609-2469 |
1.98e-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: 77.42 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1609 QLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA---- 1684
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLersi 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1685 --AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1762
Cdd:TIGR02169 311 aeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1763 LEAEAGRFRELAEEAARLRALAEEAKRQRQlaeedavrQRAEAERVLAEKLAAISEatrLKTEAEIALKEKEAENERLRR 1842
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSE--------ELADLNAAIAGIEAKINE---LEEEKEDKALEIKKQEWKLEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1843 LAED-EAFQRRLLEEQAAQhkADIEARLAQLRKaSESELERQKGLVEDTLRQRRQVEEeilalkgsfekaaagkaELELE 1921
Cdd:TIGR02169 460 LAADlSKYEQELYDLKEEY--DRVEKELSKLQR-ELAEAEAQARASEERVRGGRAVEE-----------------VLKAS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1922 LGRIRGTAEDTLRSKEQ---AEQEAARQRqlaaeeerrrrEAEERVQKSLAAEE--EAARQRK---AALEEVERLKAKVE 1993
Cdd:TIGR02169 520 IQGVHGTVAQLGSVGERyatAIEVAAGNR-----------LNNVVVEDDAVAKEaiELLKRRKagrATFLPLNKMRDERR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1994 EARRLRERAEQESARQLqlaQEAAQKRlqaeEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARER 2073
Cdd:TIGR02169 589 DLSILSEDGVIGFAVDL---VEFDPKY----EPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRA 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2074 AEREAAQSRRQVEEAERL---KQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQ 2150
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLrerLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2151 ALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQveEELFSLRVQMEELGKLKARIEAENRALvl 2230
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREI-- 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2231 rDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAELLQQQK 2310
Cdd:TIGR02169 818 -EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGDLKKER 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2311 ELAQEQARRLQEDKEQMAQQlaqetqgfqktLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRfRKQAEDIGER 2390
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQ-----------IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAE 959
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 2391 LYRTELAtqekvmlVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSF 2469
Cdd:TIGR02169 960 LQRVEEE-------IRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENF 1031
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1040-1562 |
2.18e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.26 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1040 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEvLRAHEEQLKEAQAvpaTLPELEATKAALKKLRAQAEAQQpv 1119
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAE-LARLEAELERLEA---RLDALREELDELEAQIRGNGGDR-- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1120 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTdvrQRELEQLGRQLRYYRESADPLGAWLRD 1199
Cdd:COG4913 340 LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA---AALLEALEEELEALEEALAEAEAALRD 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1200 AKQRQEQIQA-----------VPlANSQAVREQLRQEKALLED---------------------IER--HGEK----VEE 1241
Cdd:COG4913 417 LRRELRELEAeiaslerrksnIP-ARLLALRDALAEALGLDEAelpfvgelievrpeeerwrgaIERvlGGFAltllVPP 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1242 cQRFAK--QYINAIKDyELQLVTYKAQLEPVASPAKKPKVQSGSEsiiqeyvdlrtrysELSTLTSQYIRFISETLRRM- 1318
Cdd:COG4913 496 -EHYAAalRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSLAG--------------KLDFKPHPFRAWLEAELGRRf 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1319 -----EEEERLAEQQRAEERERLA-EVEAALEK--QRQLAEAH------AQAKAQAEREAQGLQRRMQEEVARREEVAvE 1384
Cdd:COG4913 560 dyvcvDSPEELRRHPRAITRAGQVkGNGTRHEKddRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALE-A 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1385 AQEQKRSIQEELQHLRQSSEAEIQakarqVEAAERSRLRIEEEIRvvrlQLEAterqrggAEGELQALRARAEEAEAQKR 1464
Cdd:COG4913 639 ELDALQERREALQRLAEYSWDEID-----VASAEREIAELEAELE----RLDA-------SSDDLAALEEQLEELEAELE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1465 QAQEEAERLRRQVQDETQRKRQAEAEL-ALRVQAEAEAAREKQRALQALEELRlqAEEAERRLRQAEAERARQVQVALET 1543
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELdELQDRLEAAEDLARLELRALLEERF--AAALGDAVERELRENLEERIDALRA 780
|
570
....*....|....*....
gi 1920237982 1544 AQRSAEAELQSEHASFAEK 1562
Cdd:COG4913 781 RLNRAEEELERAMRAFNRE 799
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1690-2503 |
2.92e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.93 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1690 IRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAE--MEVLLASKARAEEESRSTSEKSKQRLEAea 1767
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtfTRVVLLPQGEFAQFLKAKSKEKKELLMN-- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1768 grfrelAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAErvlAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 1847
Cdd:TIGR00618 172 ------LFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQ---LLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1848 AFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEeilalkgsfeKAAAGKAELELELGRIRG 1927
Cdd:TIGR00618 243 AYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAP----------LAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1928 TAEdtLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2007
Cdd:TIGR00618 313 HTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2008 rQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEE 2087
Cdd:TIGR00618 391 -LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2088 AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRL 2167
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2168 QLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLkarIEAENRAlvlrdKDSAQRLLQEEAEKm 2247
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL---TEKLSEA-----EDMLACEQHALLRK- 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2248 KQVAEEAARLSVAAQEAARLRQLAEEDLAQqraLAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQA--RRLQEDKE 2325
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHA---LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSekEQLTYWKE 697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2326 QMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEdigERLYRTELATQEKVMLV 2405
Cdd:TIGR00618 698 MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK---ARTEAHFNNNEEVTAAL 774
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2406 QTLeTQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQ 2485
Cdd:TIGR00618 775 QTG-AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
810
....*....|....*...
gi 1920237982 2486 EKAKLEQlfQDEVAKAQA 2503
Cdd:TIGR00618 854 YEECSKQ--LAQLTQEQA 869
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2131-2590 |
3.69e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.63 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2131 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQ 2210
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2211 MEELGKLKARIEAEnRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2290
Cdd:TIGR02168 311 LANLERQLEELEAQ-LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2291 QAVQEATRLKAEAELLQQQKE-LAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA 2369
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLErLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2370 QARAEEDARRFRKQAEDIGERLYRTE-----------------------------LATQEKV------------------ 2402
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLErlqenlegfsegvkallknqsglsgilgvLSELISVdegyeaaieaalggrlqa 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2403 MLVQTLETQRQ--QSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEE-----------------------MQTVRQEQ 2457
Cdd:TIGR02168 550 VVVENLNAAKKaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEgflgvakdlvkfdpklrkalsylLGGVLVVD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2458 LLQETQALQ------------------------QSFLSEKDSLLQRERCIEQEKAKLEQLfQDEVAKAQALREEQQRQQQ 2513
Cdd:TIGR02168 630 DLDNALELAkklrpgyrivtldgdlvrpggvitGGSAKTNSSILERRREIEELEEKIEEL-EEKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237982 2514 QMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIA 2590
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1330-2436 |
4.88e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 76.15 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1330 AEERERLaeVEAALEKQRQLAEAHAQAKAQAEReaqglqrrmQEEVARREEvavEAQEQKRSIQEELQ----HLRQSSEA 1405
Cdd:PRK04863 278 ANERRVH--LEEALELRRELYTSRRQLAAEQYR---------LVEMARELA---ELNEAESDLEQDYQaasdHLNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1406 EIQAKA--RQVEAAERSRLRIEEEIRVVRlqlEATERQrggaegelqalraraEEAEAQKRQAQEEAERLRRQVQDETQr 1483
Cdd:PRK04863 344 LRQQEKieRYQADLEELEERLEEQNEVVE---EADEQQ---------------EENEARAEAAEEEVDELKSQLADYQQ- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1484 krqaeaelALRVQAEAeaAREKQRALQALEELR-------LQAEEAERRLRQAEAERARQVQVALETAQRSAEAElqsEH 1556
Cdd:PRK04863 405 --------ALDVQQTR--AIQYQQAVQALERAKqlcglpdLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ---AA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1557 ASFAEKTAQLERTLKEEHVavvqlREEAtrraqqqaeaeraraeaerelerWQlKANEALRlrlqaeevaqqksltqaea 1636
Cdd:PRK04863 472 HSQFEQAYQLVRKIAGEVS-----RSEA-----------------------WD-VARELLR------------------- 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1637 ekqkeeaerearrrgkaeeQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQRE 1716
Cdd:PRK04863 504 -------------------RLREQRHLAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1717 AAAAtqkRRELEAELAKVRAEMEVLlaskaRAEEESrstSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1796
Cdd:PRK04863 563 LEAR---LESLSESVSEARERRMAL-----RQQLEQ---LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1797 dAVRQRAEAERVLAEKLAAISEA-TRLKTEAEIALKEKEAENERLRRLAEDeaFQRRLLEEQ----AAQHKADIEARLAQ 1871
Cdd:PRK04863 632 -YMQQLLERERELTVERDELAARkQALDEEIERLSQPGGSEDPRLNALAER--FGGVLLSEIyddvSLEDAPYFSALYGP 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1872 LRKASeseLERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAG--KAElELELGRIRGTAEDTLR-SKEQAEQ---EAAR 1945
Cdd:PRK04863 709 ARHAI---VVPDLSDAAEQLAGLEDCPEDLYLIEGDPDSFDDSvfSVE-ELEKAVVVKIADRQWRySRFPEVPlfgRAAR 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1946 QRQLaaeeerrrreaeervqkslaaeEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLA---------QEA 2016
Cdd:PRK04863 785 EKRI----------------------EQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpeaelRQL 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2017 AQKRLQAEEKahafavqqkeqelqqtlqqeqsvLERLRSeaeaarraaeeaeaareraerEAAQSRRQVEEAERLKQSae 2096
Cdd:PRK04863 843 NRRRVELERA-----------------------LADHES---------------------QEQQQRSQLEQAKEGLSA-- 876
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2097 eqaqaqaqaqaaaekLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRlqleeTDhqk 2176
Cdd:PRK04863 877 ---------------LNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQ-----SD--- 933
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2177 silDEELQRLKAEVTEAARQRGQVEEELFSLrvqmEELGKLKARIEAENRALVLRDKDSAQRLLQ---EEAEKMKQVAEE 2253
Cdd:PRK04863 934 ---PEQFEQLKQDYQQAQQTQRDAKQQAFAL----TEVVQRRAHFSYEDAAEMLAKNSDLNEKLRqrlEQAEQERTRARE 1006
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2254 AARlsvaaQEAARLRQLAE--EDLAQQRALAEKMLKEKMQAVQEAT-RLKAEAE-LLQQQKELAQEQARRLQEDKEQMAQ 2329
Cdd:PRK04863 1007 QLR-----QAQAQLAQYNQvlASLKSSYDAKRQMLQELKQELQDLGvPADSGAEeRARARRDELHARLSANRSRRNQLEK 1081
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2330 QLaqetqgfqkTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEkvmlvqtLE 2409
Cdd:PRK04863 1082 QL---------TFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRELAYLS-------AD 1145
|
1130 1140
....*....|....*....|....*..
gi 1920237982 2410 TQRQQSDRDAERLREAIAELEHEKDKL 2436
Cdd:PRK04863 1146 ELRSMSDKALGALRLAVADNEHLRDVL 1172
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
24-137 |
6.79e-13 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 68.03 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 24 KTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLsgdslprERDVIRSSRLPREKGRMR--FHKLQNVQIALDYLR 101
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKI-------KPGVVDWSRVNKPFKKLGanMKKIENCNYAVELGK 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237982 102 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 137
Cdd:cd21298 80 KLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
151-246 |
6.80e-13 |
|
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: 67.80 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 151 KEKLLLWSQRMVEGCqglRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 229
Cdd:cd21229 5 KKLMLAWLQAVLPEL---KITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1920237982 230 DVDVPQPDEKSIITYVS 246
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1096-1555 |
7.49e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.19 E-value: 7.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1096 LPELEATKAALKKLRAQAEAqqpvFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTL--LLERWQAVLAQTDVRQ 1173
Cdd:COG4717 70 LKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1174 RELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQekaLLEDIERHGEKVEECQRFAKQYINAI 1253
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1254 KDYELQLVTYKAQLEPVASPAK--KPKVQSGSESII-------QEYVDLRTRYSELSTLTSQYIRFISETLRRMEE--EE 1322
Cdd:COG4717 223 EELEEELEQLENELEAAALEERlkEARLLLLIAAALlallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAslGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1323 RLAEQQRAEERERL--AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKrsIQEELQHLR 1400
Cdd:COG4717 303 EAEELQALPALEELeeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1401 QSSEAEIQAKARQVEAAErsrlRIEEEIRVVRLQLEA--TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ 1478
Cdd:COG4717 381 VEDEEELRAALEQAEEYQ----ELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 1479 DETQRKRQAEAElalrvqaeaeaarekqralQALEELRLQAEEAERRLRQAEAERARQ--VQVALETAQRSAEAELQSE 1555
Cdd:COG4717 457 ELEAELEQLEED-------------------GELAELLQELEELKAELRELAEEWAALklALELLEEAREEYREERLPP 516
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3031-3069 |
8.36e-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: 8.36e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1920237982 3031 LLEAQAGTGHIIDPTTSARLTVDEAVRAGLVGPELHEKL 3069
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
151-252 |
9.22e-13 |
|
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: 67.80 E-value: 9.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 151 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 230
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1920237982 231 -VDVPQPDEKSIITYVSSLYDAM 252
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
149-249 |
1.19e-12 |
|
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: 67.41 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 149 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 228
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1920237982 229 ED-VDVPQPDEKSIITYVSSLY 249
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1299-1516 |
1.28e-12 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 73.37 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1299 ELSTLTSQYIR-----FISETLRRMEEEERLAEQQRAEeRERLAEVEAAlEKQRQLAEAHAQAKAQAER----EAQGLQR 1369
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAIA-QANREAEEAELEQEREIETariaEAEAELA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1370 RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrlqLEATERQRGGAEGEL 1449
Cdd:COG2268 248 KKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAE-------LEADVRKPAEAEKQA 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237982 1450 QALRARAeEAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELALRVQAEAEAAREKQRALQALEELR 1516
Cdd:COG2268 321 AEAEAEA-EAEAIRAKGLAEAEGKRALA--EAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2132-2663 |
1.33e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2132 RQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRV-Q 2210
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVrK 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2211 MEELGKLKA--RIEAENRALVLRDKDSAQRllQEEAEKMKQV--AEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2286
Cdd:PTZ00121 1190 AEELRKAEDarKAEAARKAEEERKAEEARK--AEDAKKAEAVkkAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFAR 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2287 KEKMQAVQEATrlKAEaELLQQQKELAQEQARRLQEDKEqmAQQLAQETQGFQKTLETERQRQlEMSAEAERLRLRVAEM 2366
Cdd:PTZ00121 1268 RQAAIKAEEAR--KAD-ELKKAEEKKKADEAKKAEEKKK--ADEAKKKAEEAKKADEAKKKAE-EAKKKADAAKKKAEEA 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2367 SRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLEtQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQlK 2446
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK-KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK-K 1419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2447 SEEMQTvRQEQLLQETQALQQSFLSEKDSLLQRErciEQEKAKLEQLFQ--DEVAKAQALREEQQRqqqqmqqekqqlAA 2524
Cdd:PTZ00121 1420 ADEAKK-KAEEKKKADEAKKKAEEAKKADEAKKK---AEEAKKAEEAKKkaEEAKKADEAKKKAEE------------AK 1483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2525 SMEEARRRQHEAeegvRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALAR-SEEIAPSRA-AAARALPN 2602
Cdd:PTZ00121 1484 KADEAKKKAEEA----KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkAEEKKKADElKKAEELKK 1559
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237982 2603 GQDAADGPAAAAEPEHAFDGLRR-----KVPAQRLQEVGVL-------SAEELQQLAQGRTTVAELAQREDVR 2663
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKaeeakKAEEARIEEVMKLyeeekkmKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1074-1570 |
1.37e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.57 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1074 EAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELrgAQEVGERLQQRHGERDVEVERWRE 1153
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1154 RVTLLLERWQAVLAQ-TDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDI 1232
Cdd:COG4913 317 RLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1233 ERHGEKVEECQRFAKQyinAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRFIS 1312
Cdd:COG4913 397 EEELEALEEALAEAEA---ALRDLRRELRELEAEIA---------SLERRKSNIPARLLALRDALAEALGLDEAELPFVG 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1313 ETLRRMEEEERLaeqQRAEER-------------ERLAEVEAALEKQR-------QLAEAHAQAKAQAEREAQGLQRRM- 1371
Cdd:COG4913 465 ELIEVRPEEERW---RGAIERvlggfaltllvppEHYAAALRWVNRLHlrgrlvyERVRTGLPDPERPRLDPDSLAGKLd 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1372 ----------QEEVARREEVA-VEAQEQ----KRSIQEELQ--------------HLRQ------SSEAEIQAKARQVEA 1416
Cdd:COG4913 542 fkphpfrawlEAELGRRFDYVcVDSPEElrrhPRAITRAGQvkgngtrhekddrrRIRSryvlgfDNRAKLAALEAELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1417 AERSRLRIEEEIRVVRLQLEATERQRGGAEG---------ELQALRARAEEAEAQKRQAQE---EAERLRRQVQDETQRK 1484
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1485 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV--QVALETAQRSAEAELQSEHASFAEK 1562
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEERIDALRAR 781
|
....*...
gi 1920237982 1563 TAQLERTL 1570
Cdd:COG4913 782 LNRAEEEL 789
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1316-1818 |
1.86e-12 |
|
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: 74.22 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1316 RRMEEEERLAEQQRAEERERLAE----VEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRS 1391
Cdd:COG3096 242 RMTLEAIRVTQSDRDLFKHLITEatnyVAADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSAR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1392 iQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEeirvVRLQLEATERQRGGAEGELqalraraEEAEAQKRQAQE 1468
Cdd:COG3096 322 -ESDLEQDYQAASdhlNLVQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1469 EAERLRRQVQDETQrkrqaeaelALRVQAEAeaAREKQRALQALEELR-------LQAEEAERRLRQAEAERARQVQVAL 1541
Cdd:COG3096 390 EVDSLKSQLADYQQ---------ALDVQQTR--AIQYQQAVQALEKARalcglpdLTPENAEDYLAAFRAKEQQATEEVL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1542 ETAQRSAEAElqsEHASFAEKTAQLERTLKEEHVavvqlREEAtrraqqqaeaeraraeaerelerWQlKANEALR---- 1617
Cdd:COG3096 459 ELEQKLSVAD---AARRQFEKAYELVCKIAGEVE-----RSQA-----------------------WQ-TARELLRryrs 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1618 LRLQAEEVAQQKSltqaeaekqkeeaerearRRGKAEEQAVRQRELAEQelekQRQLAEGTAQQRLAAEQelirLRAETE 1697
Cdd:COG3096 507 QQALAQRLQQLRA------------------QLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEE----LEELLA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1698 QGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEA 1767
Cdd:COG3096 561 ELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLERER 640
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1920237982 1768 GRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISE 1818
Cdd:COG3096 641 EATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERLGGVLLSEIYD 691
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1317-2441 |
2.15e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 74.06 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1317 RMEEEERLAEQQRAEERERLAEVEAAL----EKQRQLAEAHAQAKAQAEREAqglqrrmqEEVARREEVAVEAQEQKRSI 1392
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELkeleKKHQQLCEEKNALQEQLQAET--------ELCAEAEEMRARLAARKQEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1393 QEELQHLrqssEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRARAEEAEAQKRQAQEEAER 1472
Cdd:pfam01576 74 EEILHEL----ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAAR-------QKLQLEKVTTEAKIKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1473 LRRQVQDETQRKRQAE---AELALRVQAEAEAA------REKQRALQALEELRLQAEEAERRlrqaEAERARQVQVALET 1543
Cdd:pfam01576 143 LEDQNSKLSKERKLLEeriSEFTSNLAEEEEKAkslsklKNKHEAMISDLEERLKKEEKGRQ----ELEKAKRKLEGEST 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1544 AQRSAEAELQsehASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAeaeraraeaerelerwQLKANEALRLRLQaE 1623
Cdd:pfam01576 219 DLQEQIAELQ---AQIAELRAQLAKKEEELQAALARLEEETAQKNNALK----------------KIRELEAQISELQ-E 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1624 EVAQQKSltqaeaekqkeeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGT-----AQQRLAA--EQELIRLR--- 1693
Cdd:pfam01576 279 DLESERA----------------------ARNKAEKQRRDLGEELEALKTELEDTldttaAQQELRSkrEQEVTELKkal 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1694 -AETEQGEQQRQ-----------LLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEEsRSTSEKSKQ 1761
Cdd:pfam01576 337 eEETRSHEAQLQemrqkhtqaleELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHK-RKKLEGQLQ 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1762 RLEA---EAGRFR-ELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERV---LAEKLAAISEATRLKTEAEIALKEKE 1834
Cdd:pfam01576 416 ELQArlsESERQRaELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLesqLQDTQELLQEETRQKLNLSTRLRQLE 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1835 AENERLRRLAEDEAFQRRLLEEQAAQHkadiEARLAQLRKASESELERQKGLVEDtlrqRRQVEEEILALKGSFEKAAAG 1914
Cdd:pfam01576 496 DERNSLQEQLEEEEEAKRNVERQLSTL----QAQLSDMKKKLEEDAGTLEALEEG----KKRLQRELEALTQQLEEKAAA 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1915 KAELELELGRIRGTAEDTLRSKEQaeqeaarQRQLAAEEERRRREAEErvqksLAAEEEAARQRKAALEEVERLKAKVEE 1994
Cdd:pfam01576 568 YDKLEKTKNRLQQELDDLLVDLDH-------QRQLVSNLEKKQKKFDQ-----MLAEEKAISARYAEERDRAEAEAREKE 635
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1995 ARRLRERAEQESARQLQLAQEAAQKRLQAEekahafavqqkeqelqqtlqqeqsvLERLRSEAEAARRAAEEAEAARERA 2074
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAE-------------------------MEDLVSSKDDVGKNVHELERSKRAL 690
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2075 EREAAQSRRQVEEAERLKQSaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQAeqaalRQKQAADAEMEKHKQfaeQALRQ 2154
Cdd:pfam01576 691 EQQVEEMKTQLEELEDELQA------------TEDAKLRLEVNMQALKAQFE-----RDLQARDEQGEEKRR---QLVKQ 750
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2155 KAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKD 2234
Cdd:pfam01576 751 VRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKE 830
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2235 SAQRLLQEEAEKMkQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2314
Cdd:pfam01576 831 SEKKLKNLEAELL-QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLN 909
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2315 EQARRLQEDKEQMAQQLAQETQGFQKtLETERQrqlEMSAEAERLRLRVAEMSRAQ---------------ARAEEDARR 2379
Cdd:pfam01576 910 DRLRKSTLQVEQLTTELAAERSTSQK-SESARQ---QLERQNKELKAKLQEMEGTVkskfkssiaaleakiAQLEEQLEQ 985
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 2380 FRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQ 2441
Cdd:pfam01576 986 ESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEAS 1047
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1447-2025 |
2.78e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.54 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1447 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqaEAELALRVQAEAEAAREKQRALQALEELRLQAEEA--ER 1524
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKE--EKDLHERLNGLESELAELDEEIERYEEQREQARETrdEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1525 RLRQAEAERARQVQVALETA---QRSAEAELQSEHASFAEKTAQLERTLKEehvavvqLREEATRRAQQQAEAERARAEA 1601
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEiedLRETIAETEREREELAEEVRDLRERLEE-------LEEERDDLLAEAGLDDADAEAV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1602 ERELERWQlKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEaerearrrgKAEEQAVRQRELA---EQELEKQRQLAEGT 1678
Cdd:PRK02224 313 EARREELE-DRDEELRDRLEECRVAAQAHNEEAESLREDAD---------DLEERAEELREEAaelESELEEAREAVEDR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1679 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVR---AEMEVLLA------------ 1743
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEagkcpecgqpve 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1744 --SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--EDAVRQRAEAERVLAEKLAAISEA 1819
Cdd:PRK02224 463 gsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEEKRERAEEL 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1820 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIE---------ARLAQLRKASESELERQKGLVE-- 1888
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllAAIADAEDEIERLREKREALAEln 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1889 ----DTLRQRRqveEEILALKGSFEKAAAGKAELELElgrirgTAEDTLRSKEQAEQEAARQRqlaaeeerrrreaeERV 1964
Cdd:PRK02224 623 derrERLAEKR---ERKRELEAEFDEARIEEAREDKE------RAEEYLEQVEEKLDELREER--------------DDL 679
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237982 1965 QKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2025
Cdd:PRK02224 680 QAEIGAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLE 740
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3773-3811 |
3.21e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.50 E-value: 3.21e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1920237982 3773 LLDAQLATGGIVDPRLGFHLPLDVAYQRGYLDKDTHDQL 3811
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3362-3400 |
4.94e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 4.94e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1920237982 3362 LLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKL 3400
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4285-4323 |
5.14e-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: 5.14e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1920237982 4285 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 4323
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
151-250 |
5.93e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 65.05 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 151 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 226
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1920237982 227 DPEDVdVPQPDEKSIITYVSSLYD 250
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1652-1873 |
7.07e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 70.56 E-value: 7.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1652 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1731
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1732 AKVRAE----------------MEVLLASKARAEEESRSTSEKS-KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1794
Cdd:COG4942 100 EAQKEElaellralyrlgrqppLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 1795 EEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdeafqrRLLEEQAAQHKADIEARLAQLR 1873
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA------RLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1850-2590 |
8.82e-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: 71.93 E-value: 8.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1850 QRRLLEEQAA---QHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIR 1926
Cdd:pfam02463 153 ERRLEIEEEAagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1927 GTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQES 2006
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2007 ARQLQLAQE---AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRR 2083
Cdd:pfam02463 313 EEKLKESEKekkKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2084 QVEEAErlKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELT 2163
Cdd:pfam02463 393 KEEELE--LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2164 ALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEE 2243
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2244 AEKMKQVAEEAARLSVAAQEAARLRQLAEedlaqqralaekmlkekmqavqeaTRLKAEAELLQQQKELAQEQARRLQED 2323
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTELPLGARK------------------------LRLLIPKLKLPLKSIAVLEIDPILNLA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2324 KEQMAQQLAQETQGFQKTLETERQRQLEMSaeaERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVM 2403
Cdd:pfam02463 607 QLDKATLEADEDDKRAKVVEGILKDTELTK---LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2404 LVQTLETQRQQSdrdaERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCI 2483
Cdd:pfam02463 684 KAESELAKEEIL----RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKK 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2484 EQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGvrrQQEELQRLAQQQQQQEKLLAE 2563
Cdd:pfam02463 760 EEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAE---LLEEEQLLIEQEEKIKEEELE 836
|
730 740
....*....|....*....|....*..
gi 1920237982 2564 ENQRLRERLQHLEEERRAALARSEEIA 2590
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEELERLEEEI 863
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2149-2473 |
8.86e-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: 71.69 E-value: 8.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2149 EQALRQKAQVEQELTALRLQLEETDHQKSIlDEELQRLKAEVTEAARQRGQVEEELFSL--RVQMEELGKLK-------A 2219
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAV-SERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARqaemdrqA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2220 RIEAENRALVLRDKDSAQRLLQEEaekmKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALAEKMLKEKMQAVQEATRL 2299
Cdd:pfam17380 334 AIYAEQERMAMERERELERIRQEE----RKRELERIRQEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2300 KAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQgfQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARR 2379
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER--AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2380 fRKQAEDIGERLYRTELATQEKVM--------LVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQ 2451
Cdd:pfam17380 486 -RKRAEEQRRKILEKELEERKQAMieeerkrkLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE 564
|
330 340
....*....|....*....|..
gi 1920237982 2452 TVRQEQLLQETQALQQSFLSEK 2473
Cdd:pfam17380 565 RSRLEAMEREREMMRQIVESEK 586
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
991-1576 |
9.83e-12 |
|
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: 71.91 E-value: 9.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 991 RECAQRITEQQKAQAEVDGLGKGVARLSAEAEkvlalpepspaaptlrsELELTLGKLEqvrslsaiylEKLKTISLVIR 1070
Cdd:COG3096 522 AELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-----------------ELEELLAELE----------AQLEELEEQAA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1071 STQEAEEVLRAHEEQLKE-AQAVPATLPELEATKAALKKLRAQAEAQqpvFDALRDELRGAQEVGERLQQRHGERDvEVE 1149
Cdd:COG3096 575 EAVEQRSELRQQLEQLRArIKELAARAPAWLAAQDALERLREQSGEA---LADSQEVTAAMQQLLEREREATVERD-ELA 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1150 RWRERVTLLLERWQAVLAQTDVRQREL-EQLGRQL--RYYR----ESADPLGAWLRDAKQrqeqiqAVPLANSQAVREQL 1222
Cdd:COG3096 651 ARKQALESQIERLSQPGGAEDPRLLALaERLGGVLlsEIYDdvtlEDAPYFSALYGPARH------AIVVPDLSAVKEQL 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1223 RQEKALLED---IERHGEKVEECQRFAKQYINAI--KDYELQLVTYKAQLEPV----ASPAKKPKVQSGSESIIQEYVDL 1293
Cdd:COG3096 725 AGLEDCPEDlylIEGDPDSFDDSVFDAEELEDAVvvKLSDRQWRYSRFPEVPLfgraAREKRLEELRAERDELAEQYAKA 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1294 RTRYSELSTLTSQYIRFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAQGLQRRMQE 1373
Cdd:COG3096 805 SFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQLDQLKEQLQLLNKLLP 881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1374 EV---------ARREEVAVE---AQEQKRSIQEELQHLRQSSE--AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATE 1439
Cdd:COG3096 882 QAnlladetlaDRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALS 961
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1440 --RQR------GGAEGEL-------QALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAARE 1504
Cdd:COG3096 962 evVQRrphfsyEDAVGLLgensdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQE 1041
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 1505 -KQRALQALEELRLQAEEaERRLRQAEAERARQVQVALETAQRSAEAELQSEHASF--AEKTAQLERTLKEEHVA 1576
Cdd:COG3096 1042 lEELGVQADAEAEERARI-RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLrkAERDYKQEREQVVQAKA 1115
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3940-3978 |
1.17e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 1.17e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1920237982 3940 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 3978
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3107-3145 |
1.30e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 1.30e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1920237982 3107 LLDAQLSTGGIVDPSKSHRVPLDVACARGYLDKETSAAL 3145
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1348-1718 |
1.61e-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: 70.92 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1348 QLAEAHAQAKAQAEREAQGLQRRMQEEVARREevaveaqeqKRSIQEELQHLRQSSEAEiqaKARQVEA-------AERS 1420
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQE---------KEEKAREVERRRKLEEAE---KARQAEMdrqaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1421 RLRIEEEIRVVRLQLEatERQRggaegELQALRaraEEAEAQKRQAQEEAERLRRQVQDETQRKRQaEAELALRVQ-AEA 1499
Cdd:pfam17380 341 RMAMERERELERIRQE--ERKR-----ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1500 EAAREKQRALQALEELRLQAEEA-ERRLRQAEAERARQVQ-VALETAQRSAEAE-LQSEHASFAEKTAQLERTLKEEHVA 1576
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAREMErVRLEEQERQQQVErLRQQEEERKRKKLELEKEKRDRKRA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1577 VVQLREeatrraqqqaeaeraraeaereLERWQLKANEalrlRLQAEEVAQQKSLTQAEAEKQKEEAEREARRrgKAEEQ 1656
Cdd:pfam17380 490 EEQRRK----------------------ILEKELEERK----QAMIEEERKRKLLEKEMEERQKAIYEEERRR--EAEEE 541
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 1657 AVRQrelaeQELEKQRQLAEgtaqQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA 1718
Cdd:pfam17380 542 RRKQ-----QEMEERRRIQE----QMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
149-249 |
1.63e-11 |
|
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: 63.90 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 149 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 228
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1920237982 229 ED-VDVPQPDEKSIITYVSSLY 249
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
17-128 |
1.66e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 63.98 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 17 ERDRvQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSgdslPRERDVIRSSRLPREKGRMRFHKLQNVQIA 96
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVI----PGSVNWKKVNKAPASAEISRFKAVENTNYA 76
|
90 100 110
....*....|....*....|....*....|..
gi 1920237982 97 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIW 128
Cdd:cd21300 77 VELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1381-1584 |
1.92e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.41 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1381 VAVEAQEQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE 1460
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1461 AQKRQAQEEAERLRRQVQDET----QRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRL-----RQAEA 1531
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLaelaaLRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1920237982 1532 ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEA 1584
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2175-2582 |
2.04e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2175 QKSILDEELQRLKAEVTEAARQRG---QVEEELFSLRVQMEELGKLKARIEAENRAL--------VLRDKDSAQRLLQEE 2243
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEELREELEKLekllqllpLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2244 AEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQED 2323
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2324 KEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEED---------------ARRFRKQAEDIG 2388
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2389 ERLYRTELATQEkvmlvQTLETQRQQSDRDAERLREAI--AELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQAL- 2465
Cdd:COG4717 302 KEAEELQALPAL-----EELEEEELEELLAALGLPPDLspEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALl 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2466 QQSFLSEKDSLLQRERCIEQEKAKLEQLfqdEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQE 2545
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELRE 453
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1920237982 2546 ELQRLAQQQQQQEK-----LLAEENQRLRERLQHLEEERRAA 2582
Cdd:COG4717 454 ELAELEAELEQLEEdgelaELLQELEELKAELRELAEEWAAL 495
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1287-1785 |
2.08e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 71.14 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1287 IQEYVDLRTRYSELSTLTSQYirFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAqg 1366
Cdd:COG3096 248 IRVTQSDRDLFKHLITEATNY--VAADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARES-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1367 lqrrmqeevarreevAVEAQEQKRSiqeelQHLrqsseAEIQAKARQVEAAERSRLRIEEeirvVRLQLEATERQRGGAE 1446
Cdd:COG3096 324 ---------------DLEQDYQAAS-----DHL-----NLVQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1447 GELqalraraEEAEAQKRQAQEEAERLRRQVQDETQrkrqaeaelALRVQaeAEAAREKQRALQALEELR-------LQA 1519
Cdd:COG3096 375 EQL-------AEAEARLEAAEEEVDSLKSQLADYQQ---------ALDVQ--QTRAIQYQQAVQALEKARalcglpdLTP 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1520 EEAERRLRQAEAERARQVQVALETAQRSAEAElqsEHASFAEKTAQLERTLKEEHVavvqlREEATRRAQQQAEAERARA 1599
Cdd:COG3096 437 ENAEDYLAAFRAKEQQATEEVLELEQKLSVAD---AARRQFEKAYELVCKIAGEVE-----RSQAWQTARELLRRYRSQQ 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1600 EAERELERWQLKANEA-LRLRLQAEEVAQQKSLtqaeaekqkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGT 1678
Cdd:COG3096 509 ALAQRLQQLRAQLAELeQRLRQQQNAERLLEEF-------------------CQRIGQQLDAAEELEELLAELEAQLEEL 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1679 AQQRLAAEQELIRLRAETEQGEQQRQLLeEELARLQREAAAATQKRRELEAE----LAKVRAEMEVLLaSKARAEEESRS 1754
Cdd:COG3096 570 EEQAAEAVEQRSELRQQLEQLRARIKEL-AARAPAWLAAQDALERLREQSGEaladSQEVTAAMQQLL-EREREATVERD 647
|
490 500 510
....*....|....*....|....*....|....*
gi 1920237982 1755 TSEKSKQRLEAEAgrfRELA----EEAARLRALAE 1785
Cdd:COG3096 648 ELAARKQALESQI---ERLSqpggAEDPRLLALAE 679
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
592-770 |
2.13e-11 |
|
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: 66.70 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 592 LHGFVAAATKELMWLSDREEEEVGFDWSDRNTNMAAKKEGYSALMHELELKEKKIKEIQSTGDRLLREDHPARPTAESFQ 671
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 672 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKYTCDrsiTATRLEDLLQDAQDEKEQLSEY 751
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170
....*....|....*....
gi 1920237982 752 RGHLSGLAKRAKAIVQLKP 770
Cdd:cd00176 159 EPRLKSLNELAEELLEEGH 177
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1060-1945 |
2.17e-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: 70.77 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1060 EKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRaqaeaqqpvfdalrdelrgaqevgerlqq 1139
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD----------------------------- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1140 rhgERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdplgawlrDAKQRQEQIQAVPLANSQAVR 1219
Cdd:pfam02463 231 ---YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEE--------KEKKLQEEELKLLAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1220 EQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSgsesiIQEYVDLRTRYSE 1299
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL-----EKLQEKLEQLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1300 LSTLTSQYIRFISETLRRMEEEERLA-----EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEE 1374
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKseeekEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1375 VARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLR-IEEEIRVVRLQLEATERQRGGAEGELQALR 1453
Cdd:pfam02463 455 KQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESkARSGLKVLLALIKDGVGGRIISAHGRLGDL 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1454 ARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQ-AEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAE 1532
Cdd:pfam02463 535 GVAVENYKVAISTAVIVEVSATADEVEERQKLVrALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLE 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1533 RARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHvavvQLREEATRRAQQQAEAERARAEAERELERWQLKA 1612
Cdd:pfam02463 615 ADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEE----GLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1613 NEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1692
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1693 RAETEQGEQQRQLLEEELARLQREAAAATQKrrELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRE 1772
Cdd:pfam02463 771 LKEKELAEEREKTEKLKVEEEKEEKLKAQEE--ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1773 LAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRR 1852
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1853 LLEEQAAQHKADIEARLAQLRKASESELERQKglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDT 1932
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEE---RNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
890
....*....|...
gi 1920237982 1933 LRSKEQAEQEAAR 1945
Cdd:pfam02463 1006 KLIRAIIEETCQR 1018
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1662-2582 |
2.44e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 70.59 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1662 ELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAeME 1739
Cdd:pfam01576 111 QLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA-MI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1740 VLLASKARAEEESRSTSEKSKQRLEAEAGrfrELAEEAARLRALAEEAKRQRQLAEEDavrqraeaervLAEKLAAISEA 1819
Cdd:pfam01576 190 SDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEE-----------LQAALARLEEE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1820 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRrlleEQAAQHKADIEARLAQLRKASESELERQKGLVEdtLRQRRqvEE 1899
Cdd:pfam01576 256 TAQKNNALKKIRELEAQISELQEDLESERAAR----NKAEKQRRDLGEELEALKTELEDTLDTTAAQQE--LRSKR--EQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1900 EILALKGSFEKAAAGKAELELELGRIRGTAEDTLrsKEQAEQeAARQRQLAAEEERRRREAEERVQKSL----AAEEEAA 1975
Cdd:pfam01576 328 EVTELKKALEEETRSHEAQLQEMRQKHTQALEEL--TEQLEQ-AKRNKANLEKAKQALESENAELQAELrtlqQAKQDSE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1976 RQRKAALEEVERLKAKVEEARRLRERAEQESARqLQLAQEAAQKRLQAEEKahafavqqKEQELQQTLQQEQSVLERLRS 2055
Cdd:pfam01576 405 HKRKKLEGQLQELQARLSESERQRAELAEKLSK-LQSELESVSSLLNEAEG--------KNIKLSKDVSSLESQLQDTQE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2056 EAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQ 2135
Cdd:pfam01576 476 LLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2136 AADAEMEKHKQFAEQALRQKAQVEQELTALRLQLeetDHQKSILDEELQRLKAEVTEAArqrgqvEEELFSLRVQMEelg 2215
Cdd:pfam01576 556 ALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDL---DHQRQLVSNLEKKQKKFDQMLA------EEKAISARYAEE--- 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2216 klKARIEAENRalvlrDKDSAQRLLQEEAEKMKQVAEEAARlsvaaqeAARLRQLAEEDLAQQRALAEKMLKE----KMQ 2291
Cdd:pfam01576 624 --RDRAEAEAR-----EKETRALSLARALEEALEAKEELER-------TNKQLRAEMEDLVSSKDDVGKNVHElersKRA 689
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2292 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLEtERQRQL-----EMSAEAERLRLRVAEM 2366
Cdd:pfam01576 690 LEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGE-EKRRQLvkqvrELEAELEDERKQRAQA 768
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2367 SRAQARAEEDARRFRKQAEDIGERlyRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLK 2446
Cdd:pfam01576 769 VAAKKKLELDLKELEAQIDAANKG--REEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQ 846
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2447 SEEMQTVRQE-QLLQETQALQQ---SFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQL 2522
Cdd:pfam01576 847 EDLAASERARrQAQQERDELADeiaSGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTEL 926
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2523 AAS---------------------------MEEARRRQHEA-----EEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRE 2570
Cdd:pfam01576 927 AAErstsqksesarqqlerqnkelkaklqeMEGTVKSKFKSsiaalEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKE 1006
|
970
....*....|..
gi 1920237982 2571 RLQHLEEERRAA 2582
Cdd:pfam01576 1007 VLLQVEDERRHA 1018
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1489-2025 |
2.64e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 70.66 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1489 AELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAE-RARQVQVALETAQRSAEAELQSEHAS--------F 1559
Cdd:COG3899 712 ARRALARGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALyLAGRFEEAEALLERALAARALAALAAlrhgnppaS 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1560 AEKTAQLERTLKEEHVAVVQLREEATRRAQQ--QAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQkslTQAEAE 1637
Cdd:COG3899 792 ARAYANLGLLLLGDYEEAYEFGELALALAERlgDRRLEARALFNLGFILHWLGPLREALELLREALEAGLE---TGDAAL 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1638 KQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREA 1717
Cdd:COG3899 869 ALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAA 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1718 AAATQKRRELEAELAKVRAEMEVLLASKARAeeesrstsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1797
Cdd:COG3899 949 AAAAALAAALALAAAAAAAAAAALAAAAAAA-------------AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAAL 1015
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1798 AVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASE 1877
Cdd:COG3899 1016 AAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAA 1095
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1878 SELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRR 1957
Cdd:COG3899 1096 ALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAAL 1175
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237982 1958 REAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2025
Cdd:COG3899 1176 AALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1693-2009 |
2.72e-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: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1693 RAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAElAKVRAEMEVLLASKARAEEESRSTSEKSkqrlEAEAGRFRE 1772
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ-AAIYAEQERMAMERERELERIRQEERKR----ELERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1773 LAEEAARLRALaEEAKRQRQLAEEdAVRQRAEAERV--LAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEA-- 1848
Cdd:pfam17380 370 IAMEISRMREL-ERLQMERQQKNE-RVRQELEAARKvkILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAre 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1849 FQRRLLEEQAAQHKADIEARLAQLRKASESELERQKglvedtlRQRRQVEEEilaLKGSFEKAAAGKAELELELGRIRGT 1928
Cdd:pfam17380 448 MERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK-------RDRKRAEEQ---RRKILEKELEERKQAMIEEERKRKL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1929 AEDTLRSKEQAEQEAARQRQlaaeeerrrREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2008
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRRE---------AEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
|
.
gi 1920237982 2009 Q 2009
Cdd:pfam17380 589 A 589
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1400-2025 |
3.39e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 70.25 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1400 RQSSEAEIQAKARQVEA--AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE----RL 1473
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1474 RRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAeLQ 1553
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1554 SEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAerelerwqlkANEALRLRLQAEEVAQQKSLTQ 1633
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAED----------DLQALESELREQLEAGKLEFNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1634 AEAEKQKEEAEREARRRG-KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR 1712
Cdd:pfam12128 438 EEYRLKSRLGELKLRLNQaTATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1713 LQREAAAATQ----KRRELEAELAKVRAEMEVLLASKARAEEESRS------TSEKSKQRLEAEAGRFRELAEEAARLRA 1782
Cdd:pfam12128 518 RQSALDELELqlfpQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTdldpevWDGSVGGELNLYGVKLDLKRIDVPEWAA 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1783 LAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHK 1862
Cdd:pfam12128 598 SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERK 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1863 A-------DIEARLAQLRKASESELERQKG---------------LVEDTLRQRRQVEEEILALKGSFE----------- 1909
Cdd:pfam12128 678 DsanerlnSLEAQLKQLDKKHQAWLEEQKEqkreartekqaywqvVEGALDAQLALLKAAIAARRSGAKaelkaletwyk 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1910 --------------KAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAA 1975
Cdd:pfam12128 758 rdlaslgvdpdviaKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADT 837
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 1976 RQRKAALEevERLKAKVEEARRLRE-----RAEQESARQLQLAQEAAQKRLQAEE 2025
Cdd:pfam12128 838 KLRRAKLE--MERKASEKQQVRLSEnlrglRCEMSKLATLKEDANSEQAQGSIGE 890
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2703-2741 |
3.45e-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: 3.45e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1920237982 2703 LLEAQAASGFLLDPVRNRRLAVNEAVKEGIVGPELHHKL 2741
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1370-2468 |
3.78e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 69.82 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1370 RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEA--AERSRLRIEEEIRvVRLQLEATErqrggAEG 1447
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQlqAETELCAEAEEMR-ARLAARKQE-----LEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1448 ELQALRARAEEAEAQKRQAQEEAERLRRQVQDetqrkrqAEAELalrvqAEAEAAREKqralqaleeLRLQAEEAERRLR 1527
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQD-------LEEQL-----DEEEAARQK---------LQLEKVTTEAKIK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1528 QAEAErarqvqVALETAQRSaeaELQSEHASFAEKTAQLERTLKEEHVAVVQL-----REEATRRAQQQAEAERARAEAE 1602
Cdd:pfam01576 135 KLEED------ILLLEDQNS---KLSKERKLLEERISEFTSNLAEEEEKAKSLsklknKHEAMISDLEERLKKEEKGRQE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1603 RELERWQLKAnEALRLRlqaEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQR 1682
Cdd:pfam01576 206 LEKAKRKLEG-ESTDLQ---EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE--LQED 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1683 LAAEqelirlRAETEQGEQQRQLLEEELARLQRE---AAAATQKRRELEAelakvRAEMEVLLASKArAEEESRSTSEKS 1759
Cdd:pfam01576 280 LESE------RAARNKAEKQRRDLGEELEALKTEledTLDTTAAQQELRS-----KREQEVTELKKA-LEEETRSHEAQL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1760 KQRLEAEAGRFRELAEE---AARLRALAEEAK--------------RQRQLAEEDAVRQRAEAERVLAEKLAAISEATRL 1822
Cdd:pfam01576 348 QEMRQKHTQALEELTEQleqAKRNKANLEKAKqalesenaelqaelRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1823 KTEAEIALKEKEAENERLRRLAEDeafqrrlLEEQAAQHKADIEARLAQLRKASE--SELERQKGLVEDTLrqrRQVEEE 1900
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNE-------AEGKNIKLSKDVSSLESQLQDTQEllQEETRQKLNLSTRL---RQLEDE 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1901 ILALKGSFEKAAAGKAELELELGRIRGTAEDTlrsKEQAEQEAARQRQLaaeeerrrreaeERVQKSLAAEEEAARQRka 1980
Cdd:pfam01576 498 RNSLQEQLEEEEEAKRNVERQLSTLQAQLSDM---KKKLEEDAGTLEAL------------EEGKKRLQRELEALTQQ-- 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1981 aLEEVERLKAKVEEAR-RLRERAE-----QESARQLQLAQEAAQKR---LQAEEKA-HAFAVQQKEQELQQTLQQEQSVL 2050
Cdd:pfam01576 561 -LEEKAAAYDKLEKTKnRLQQELDdllvdLDHQRQLVSNLEKKQKKfdqMLAEEKAiSARYAEERDRAEAEAREKETRAL 639
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2051 ERLRSeaeaarraaeeaeaareraereAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAA 2130
Cdd:pfam01576 640 SLARA----------------------LEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEM 697
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2131 LRQKQaadaEMEKHKQFAEQA-LR-------QKAQVEQELTALRLQLEEtdhQKSILDEELQRLKAEVTEAARQRGQvee 2202
Cdd:pfam01576 698 KTQLE----ELEDELQATEDAkLRlevnmqaLKAQFERDLQARDEQGEE---KRRQLVKQVRELEAELEDERKQRAQ--- 767
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2203 eLFSLRVQME-ELGKLKARIEAENRAlvlrdKDSAQRLLQEEAEKMKQVAeeaarlsvaaqeaarlRQLAEEDLAQQRAL 2281
Cdd:pfam01576 768 -AVAAKKKLElDLKELEAQIDAANKG-----REEAVKQLKKLQAQMKDLQ----------------RELEEARASRDEIL 825
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2282 AEKMLKEKmqavqeatRLKA-EAELLQQQKELA-QEQARR-LQEDKEQMAQQLAQETQGfqKTLETERQRQLEmsaeaER 2358
Cdd:pfam01576 826 AQSKESEK--------KLKNlEAELLQLQEDLAaSERARRqAQQERDELADEIASGASG--KSALQDEKRRLE-----AR 890
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2359 LRLRVAEMSRAQARAEEDARRFRKQAEDIgERLyRTELATQEKvmLVQTLETQRQQSDRDAERLREAIAELEHE-KDKLK 2437
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQV-EQL-TTELAAERS--TSQKSESARQQLERQNKELKAKLQEMEGTvKSKFK 966
|
1130 1140 1150
....*....|....*....|....*....|.
gi 1920237982 2438 QEAQLLQLKSEEMqtvrQEQLLQETQALQQS 2468
Cdd:pfam01576 967 SSIAALEAKIAQL----EEQLEQESRERQAA 993
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2137-2493 |
4.03e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.68 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2137 ADAEMEKHKQFAEQA--LRQKA-QVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEE 2213
Cdd:PRK02224 344 AESLREDADDLEERAeeLREEAaELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2214 LGKLKARIEAENRALVLRDKDsAQRLLQE-EAEKMKQVAEEAARLSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKM 2290
Cdd:PRK02224 424 LREREAELEATLRTARERVEE-AEALLEAgKCPECGQPVEGSPHVETIEEDRERVEELEAEleDLEEEVEEVEERLERAE 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2291 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSraQ 2370
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRER-AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN--S 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2371 ARAEEDARrfRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERL---REAIAELEHEKDklkqEAQLLQLKS 2447
Cdd:PRK02224 580 KLAELKER--IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLaekRERKRELEAEFD----EARIEEARE 653
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1920237982 2448 EEMQTVR-QEQLLQETQALQQsflsEKDSLLQRERCIEQEKAKLEQL 2493
Cdd:PRK02224 654 DKERAEEyLEQVEEKLDELRE----ERDDLQAEIGAVENELEELEEL 696
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
40-131 |
4.55e-11 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 62.61 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 40 HISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirsSRLPrEKGRMRfhKLQNVQIALDYLRHRQV----KLVNIRNDDI 115
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSK-----LRVP-AISRLQ--KLHNVEVALKALKEAGVlrggDGGGITAKDI 96
|
90
....*....|....*.
gi 1920237982 116 ADGNPKLTLGLIWTII 131
Cdd:cd21223 97 VDGHREKTLALLWRII 112
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1333-1858 |
5.59e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 69.50 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1333 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKAR 1412
Cdd:COG3899 722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1413 QVEAAERSRLRIEEEIRVV-RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL--RRQVQDETQRKRQAEA 1489
Cdd:COG3899 802 LLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAA 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1490 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERT 1569
Cdd:COG3899 882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1570 LKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARR 1649
Cdd:COG3899 962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1650 RGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA 1729
Cdd:COG3899 1042 ALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALA 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1730 ELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVL 1809
Cdd:COG3899 1122 ALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAAL 1195
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1920237982 1810 AEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQA 1858
Cdd:COG3899 1196 LAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2132-2334 |
6.09e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.87 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2132 RQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQM 2211
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2212 EELGK---LKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2288
Cdd:COG4942 114 YRLGRqppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1920237982 2289 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQE 2334
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
971-1526 |
8.90e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 8.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 971 EACETRTVHRLRLPLDKEPARECAQRITEQQKAqaevDGLGKGV--ARLSAEAEKVLAlPEPSPAAPTLRSELELTLGKL 1048
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA----DEAKKKAeeAKKKADAAKKKA-EEAKKAAEAAKAEAEAAADEA 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1049 EQVRSLS-AIYLEKLKTISLVIRSTQEAEEVLRAhEEQLKEAQAVPATLPELEATKAALKK---LRAQAEAQQPVfdalr 1124
Cdd:PTZ00121 1360 EAAEEKAeAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKadeAKKKAEEKKKA----- 1433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1125 DELRGAQEvgERLQQRHGERDVEVERWRERVTLLLERwqavlaqtdvrQRELEQLGRQLRYYREsADPLGAWLRDAKQRQ 1204
Cdd:PTZ00121 1434 DEAKKKAE--EAKKADEAKKKAEEAKKAEEAKKKAEE-----------AKKADEAKKKAEEAKK-ADEAKKKAEEAKKKA 1499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1205 EQIQAVPLANSQAVREQLRQEKALLEDIERHGE--KVEEcqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSG 1282
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakKADE----AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1283 SESIIQEYVDLR----TRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERlaeveaalEKQRQLAEAHAQAKA 1358
Cdd:PTZ00121 1576 KNMALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK--------KKVEQLKKKEAEEKK 1647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1359 QAEReaqgLQRRMQEEVARREEVAVEAQEQKRSIQEelqhLRQSSEAEiqakarqvEAAERSRLRIEEEIRVVRLQLEAT 1438
Cdd:PTZ00121 1648 KAEE----LKKAEEENKIKAAEEAKKAEEDKKKAEE----AKKAEEDE--------KKAAEALKKEAEEAKKAEELKKKE 1711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1439 ERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAElalrvQAEAEAAREKQRALQALEELRLQ 1518
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK-----KEEEKKAEEIRKEKEAVIEEELD 1786
|
....*...
gi 1920237982 1519 AEEAERRL 1526
Cdd:PTZ00121 1787 EEDEKRRM 1794
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
151-251 |
9.87e-11 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 61.60 E-value: 9.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 151 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 230
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 1920237982 231 VdVPQPDEKSIITYVSSLYDA 251
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1319-1819 |
1.32e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 68.35 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1319 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER-----EAQGLQRRMQEEVARREEVAVEAQEQKRSIQ 1393
Cdd:COG3899 741 EEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRhgnppASARAYANLGLLLLGDYEEAYEFGELALALA 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1394 EELQHLRQSSEAEIqAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1473
Cdd:COG3899 821 ERLGDRRLEARALF-NLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAA 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1474 RRQVQDETQRKRQAEAELALRVQAEAEAAREkqRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQ 1553
Cdd:COG3899 900 AAAALAAAAAAAALAAAELARLAAAAAAAAA--LALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAA 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1554 SEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQ 1633
Cdd:COG3899 978 AAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAA 1057
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1634 AEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARL 1713
Cdd:COG3899 1058 AAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLL 1137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1714 QREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQL 1793
Cdd:COG3899 1138 LAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLAL 1217
|
490 500
....*....|....*....|....*.
gi 1920237982 1794 AEEDAVRQRAEAERVLAEKLAAISEA 1819
Cdd:COG3899 1218 EAAALLLLLLLAALALAAALLALRLL 1243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2229-2585 |
1.69e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2229 VLRDKDSAQRLLQEEA---EKMKQVAEEAARLSVAAQEA-ARLRQLAEEDLAQQRAL---AEKMlkEKMQAVQEATRlKA 2301
Cdd:TIGR02168 149 IIEAKPEERRAIFEEAagiSKYKERRKETERKLERTRENlDRLEDILNELERQLKSLerqAEKA--ERYKELKAELR-EL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2302 EAELLQQQKELAQEQARRLQEDKEQMAQQLAQET---QGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDAR 2378
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTaelQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2379 RFRKQAEDIGERLYRtelatqekvmlvqtLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQL 2458
Cdd:TIGR02168 306 ILRERLANLERQLEE--------------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2459 LQEtQALQQSFLSEKDSLLQRERCIEQEKAKLEQLfqdeVAKAQALreeqQRQQQQMQQEKQQLAASMEEARRRQHEAE- 2537
Cdd:TIGR02168 372 SRL-EELEEQLETLRSKVAQLELQIASLNNEIERL----EARLERL----EDRRERLQQEIEELLKKLEEAELKELQAEl 442
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1920237982 2538 EGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALAR 2585
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1655-2029 |
2.04e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1655 EQAVRQRELAEQELEKQRQL--AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELA 1732
Cdd:COG4717 105 EELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1733 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAV------------- 1799
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallgl 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1800 --RQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASE 1877
Cdd:COG4717 265 ggSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1878 SELERQKGLVE-DTLRQRRQVEEEILALKGSFEKAAAGKAElelelgRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERR 1956
Cdd:COG4717 345 RIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 1957 RREAEERVQKSLAAE-EEAARQRKAALEEVERLKAKVEEAR-RLRERAEQESARQLQLAQEAAQKRLQAEEKAHA 2029
Cdd:COG4717 419 EELLEALDEEELEEElEELEEELEELEEELEELREELAELEaELEQLEEDGELAELLQELEELKAELRELAEEWA 493
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1386-1575 |
2.08e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 65.98 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1386 QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQL--EATERQRGGAEGELQALRARAEEAEAQK 1463
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQkkQAEEAAKQAALKQKQAEEAAAKAAAAAK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1464 RQAQEEAERLRRQV-QDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALE 1542
Cdd:PRK09510 147 AKAEAEAKRAAAAAkKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
170 180 190
....*....|....*....|....*....|...
gi 1920237982 1543 TAQRSAEAELQSEHASFAEKTAQLERTLKEEHV 1575
Cdd:PRK09510 227 AAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1306-2023 |
2.10e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.45 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1306 QYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEA 1385
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1386 QEQKRSIQEELQHLRQ---SSEAEIQA-KARQVEAAERSRLRIEEEIRVVRLQLE----ATERQRGGAEGELQALRAR-- 1455
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHFRslgsAISKILRELDTEISYLKGRif 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1456 --AEEAEAQKRQAQEEAERLRRQVQDET-QRKRQAEAELAlRVQAEAEAAREKQRALQAleelrlQAEEAERRLRQAEAE 1532
Cdd:pfam15921 242 pvEDQLEALKSESQNKIELLLQQHQDRIeQLISEHEVEIT-GLTEKASSARSQANSIQS------QLEIIQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1533 RARQVQvALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAeaerelerwQLKA 1612
Cdd:pfam15921 315 YMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQ---------KLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1613 NEALRLRLQAEEVAQQKSLtqaeaekqkeeaerEARRRGKAEEQAVRQRELAEQELEKQRQLA---------EGTAQQRL 1683
Cdd:pfam15921 385 DLHKREKELSLEKEQNKRL--------------WDRDTGNSITIDHLRRELDDRNMEVQRLEAllkamksecQGQMERQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1684 AAEQ----ELIRLRAETEQGEQQRQLLEEELARLqreaaaaTQKRRELEAELAKVrAEMEVLLASKARAEEESRSTSEKS 1759
Cdd:pfam15921 451 AAIQgkneSLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTV-SDLTASLQEKERAIEATNAEITKL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1760 KQRLEAEAGRFRELAEEAARLRALAEEAKRQR-QLAEEDAV----RQ----------------------RAEAERVLAEK 1812
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVieilRQqienmtqlvgqhgrtagamqveKAQLEKEINDR 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1813 LAAISEATRLKTEAEIALKEKEAE---------------NERLRRLAEDEAFQRRLLEEQAAQHK------ADIEARLAQ 1871
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARvsdlelekvklvnagSERLRAVKDIKQERDQLLNEVKTSRNelnslsEDYEVLKRN 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1872 LRKASE------SELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAG-KAELELELGRIrgtaeDTLRSK----EQAE 1940
Cdd:pfam15921 683 FRNKSEemetttNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGmQKQITAKRGQI-----DALQSKiqflEEAM 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1941 QEAARQRQLAAEEERRRREAEERV---QKSLAAEEEAARQRKAALEE--------VERLKAKVEEARRLRERAEQESARq 2009
Cdd:pfam15921 758 TNANKEKHFLKEEKNKLSQELSTVateKNKMAGELEVLRSQERRLKEkvanmevaLDKASLQFAECQDIIQRQEQESVR- 836
|
810
....*....|....
gi 1920237982 2010 LQLAQEAAQKRLQA 2023
Cdd:pfam15921 837 LKLQHTLDVKELQG 850
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2229-2584 |
2.94e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2229 VLRDKDSAQRLLQEEAEKMKQ-----VAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM--LKEKMQAVQEA-TRLK 2300
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERykelkAELRELELALLVLRLEELREELEELQEELKEAEEELeeLTAELQELEEKlEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2301 AEAELLQQQKELAQE---QARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDA 2377
Cdd:TIGR02168 274 LEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2378 RRFRKQAEdigerlyrtelatqEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKqeAQLLQLKSE-EMQTVRQE 2456
Cdd:TIGR02168 354 ESLEAELE--------------ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIERLEARlERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2457 QLLQETQALQQSFLSEKDSLLQRErcIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHeA 2536
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAE--LEELEEELEEL-QEELERLEEALEELREELEEAEQALDAAERELAQLQARLD-S 493
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1920237982 2537 EEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLqHLEEERRAALA 2584
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI-SVDEGYEAAIE 540
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1655-2401 |
4.10e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1655 EQAVRQRELAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1734
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARER---LAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1735 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLA 1814
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLEREL---EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1815 AISEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRlleeqaaqhKADIEARLAQLRKAseseLERQKGLVEDTLR-- 1892
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELE--AEIASLERR---------KSNIPARLLALRDA----LAEALGLDEAELPfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1893 -QRRQVEEEILALKGSFEKAaagkaelelelgrIRGTAEDTLRSKEQAEQ--EAARQRQLAAEeerrrreaeerVQKSLA 1969
Cdd:COG4913 464 gELIEVRPEEERWRGAIERV-------------LGGFALTLLVPPEHYAAalRWVNRLHLRGR-----------LVYERV 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1970 AEEEAARQRKAALEE--VERLKAKVEEARrlrERAEQESARQLQLAQEAAQKRLQAEEKA--------HAFAVQQKEQEL 2039
Cdd:COG4913 520 RTGLPDPERPRLDPDslAGKLDFKPHPFR---AWLEAELGRRFDYVCVDSPEELRRHPRAitragqvkGNGTRHEKDDRR 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2040 QQTLQqeqSVLerlrseaeaarraaeeaeaareraereAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEaeqe 2119
Cdd:COG4913 597 RIRSR---YVL---------------------------GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDA---- 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2120 aarraqaeqaaLRQKQAADAEMEKHkQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQ 2199
Cdd:COG4913 643 -----------LQERREALQRLAEY-SWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2200 VEEELFSLRvqmEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2279
Cdd:COG4913 711 LKGEIGRLE---KELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2280 ALAEKMLKEKMQAVQEATRLKAEAELLQQ-QKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLeterqrQLEMSAEAER 2358
Cdd:COG4913 788 ELERAMRAFNREWPAETADLDADLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIEFVADL------LSKLRRAIRE 861
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 2359 LRLRVAEMSRA----------------QARAEEDARRFRKQAEDIGERLYRTELATQEK 2401
Cdd:COG4913 862 IKERIDPLNDSlkripfgpgrylrleaRPRPDPEVREFRQELRAVTSGASLFDEELSEA 920
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
991-1579 |
4.94e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.52 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 991 RECAQRITEQQKAQaevdglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELEltlgkleqvrslsaiylEKLKTISLVI 1069
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELE-----------------ARLESLSESV 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1070 RSTQEAEEVLRAHEEQLK-EAQAVPATLPELEATKAALKKLRAQAEaqqpvfdalrDELRGAQEVGERLQQrHGERDVEV 1148
Cdd:PRK04863 575 SEARERRMALRQQLEQLQaRIQRLAARAPAWLAAQDALARLREQSG----------EEFEDSQDVTEYMQQ-LLEREREL 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1149 ERWRERVTlllERWQAVLAQTD-VRQRELEQLGRQLRYyresADPLGAWL----------RDAKQRQ----EQIQAVPLA 1213
Cdd:PRK04863 644 TVERDELA---ARKQALDEEIErLSQPGGSEDPRLNAL----AERFGGVLlseiyddvslEDAPYFSalygPARHAIVVP 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1214 NSQAVREQLRQEKALLEDI-------ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAqlEPVASPAKKPK----VQSG 1282
Cdd:PRK04863 717 DLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKrieqLRAE 794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1283 SESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER 1362
Cdd:PRK04863 795 REELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEAD--PEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKE 872
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1363 EAQGLQR-----------RMQEEVARREEVAVEAQEQKRSIQ---------EELQHLRQSSEAEIQAKARQVEAAE---- 1418
Cdd:PRK04863 873 GLSALNRllprlnlladeTLADRVEEIREQLDEAEEAKRFVQqhgnalaqlEPIVSVLQSDPEQFEQLKQDYQQAQqtqr 952
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1419 --RSRLRIEEEIRVVRLQLEATERQR-GGAEGELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDETQRKRQAEAELALR 1494
Cdd:PRK04863 953 daKQQAFALTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYNQVLASLKSS 1028
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1495 VQAEAEAAREKQRALQAL---------EELRLQAEEAERRLRQAEAERArqvqvALETAQRSAEAELQsehaSFAEKTAQ 1565
Cdd:PRK04863 1029 YDAKRQMLQELKQELQDLgvpadsgaeERARARRDELHARLSANRSRRN-----QLEKQLTFCEAEMD----NLTKKLRK 1099
|
650
....*....|....
gi 1920237982 1566 LERTLKEEHVAVVQ 1579
Cdd:PRK04863 1100 LERDYHEMREQVVN 1113
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1509-2004 |
5.49e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1509 LQALEELRLQAEEAE---RRLRQAEAERARQVQVALE-TAQRSAEAELQSEHASFAEKTAQLERtLKEEHVAVVQLREEA 1584
Cdd:PRK02224 161 LGKLEEYRERASDARlgvERVLSDQRGSLDQLKAQIEeKEEKDLHERLNGLESELAELDEEIER-YEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1585 TRRAQQQAEAERARAEAERELERWQLKANEALRLRLQ-AEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQREL 1663
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREElAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1664 AEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLA 1743
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQ-AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1744 SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE----------------DAVRQRAEAER 1807
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvETIEEDRERVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1808 VLAEKLAAIsEATRLKTEAEIALKEKEAENE-RLRRLAEdeafQRRLLEEQAAQHKADIEA---RLAQLRKAS---ESEL 1880
Cdd:PRK02224 479 ELEAELEDL-EEEVEEVEERLERAEDLVEAEdRIERLEE----RREDLEELIAERRETIEEkreRAEELRERAaelEAEA 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1881 ERQKglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELElELGRIRgtaeDTLRSKEQAEQEAARQRQLAAEEERRRREA 1960
Cdd:PRK02224 554 EEKR---EAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERIR----TLLAAIADAEDEIERLREKREALAELNDER 625
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1920237982 1961 EERVQkslaaeeeAARQRKAALEEvERLKAKVEEARRLRERAEQ 2004
Cdd:PRK02224 626 RERLA--------EKRERKRELEA-EFDEARIEEAREDKERAEE 660
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1744-2015 |
5.64e-10 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 65.74 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1744 SKARAEEESRSTSEKSKQRLEAEAGRF-RELAEEAARlralAEEAKRQRQLAEEDAVrqrAEAERVLAEKLAAISEATRL 1822
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLeREKAAREAR----HKKAAEARAAKDKDAV---AAALARVKAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1823 KTEAEIALKEKEAEnERLRRLAEDEAFQRRLLEEQAAQHKADIEARL--AQLRKASESELERQKGLVEDTlrQRRQVEEE 1900
Cdd:PRK05035 509 KAGARPDNSAVIAA-REARKAQARARQAEKQAAAAADPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDP--KKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1901 ILALKGSFEKAAAGKAELELELgrirgTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 1980
Cdd:PRK05035 586 IARAKAKKAAQQAASAEPEEQV-----AEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKA 660
|
250 260 270
....*....|....*....|....*....|....*
gi 1920237982 1981 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2015
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1073-1524 |
7.57e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 7.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1073 QEAEEVLRAHEEQLK--EAQAVPATLPELEATKAALKKLRAQAEAQQPVFDAlrDELRGAQEVGERLQQRHGErdvEVER 1150
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA--DELKKAEELKKAEEKKKAE---EAKK 1571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1151 WRERVTLLLERWQavlaqtDVRQRELEQLGRQLRYYRESADPLGAWLRdaKQRQEQIQAvplansqavrEQLRQEKALLE 1230
Cdd:PTZ00121 1572 AEEDKNMALRKAE------EAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKA----------EELKKAEEEKK 1633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1231 DIERHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAKKPkvqsgSESIIQEYVDLRtRYSELSTLTSQYIRF 1310
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEEDEK-KAAEALKKEAEEAKK 1703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1311 ISETLRRMEEEERLAEQQRAEERERLAEVEaalekqrqlaeahaQAKAQAEREaqglqRRMQEEVARREEVAVEAQEQKR 1390
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAE--------------EAKKEAEED-----KKKAEEAKKDEEEKKKIAHLKK 1764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1391 SIQEELQHLRQSSEAEIQAKARqvEAAERSRLRIEEEIRVVRLQLEATerQRGGAEGELQALRARAEEAEAQKRQAqEEA 1470
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVIEEELD--EEDEKRRMEVDKKIKDIFDNFANI--IEGGKEGNLVINDSKEMEDSAIKEVA-DSK 1839
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 1471 ERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRaLQALEELRLQAEEAER 1524
Cdd:PTZ00121 1840 NMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDL-KEDDEEEIEEADEIEK 1892
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1666-2027 |
7.57e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 7.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1666 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQR--EAAAATQKRRELEAELAKVRAEMEvlla 1743
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1744 sKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLK 1823
Cdd:COG4717 150 -ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1824 TEAEIALKEKEAENERLRRL---------------AEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVE 1888
Cdd:COG4717 229 LEQLENELEAAALEERLKEArlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1889 DTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERrrreaeerVQKSL 1968
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL--------LAEAG 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1969 AAEEEAARQRKAALEEVERLKAKVEEA-RRLRERAEQESARQLQLAQEAAQKRLQAEEKA 2027
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELeEQLEELLGELEELLEALDEEELEEELEELEEE 440
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1077-1896 |
8.90e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.75 E-value: 8.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1077 EVLRAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAqqpvfdaLRDELRGAQEvGERLQQRHGERDVEVERWRERvt 1156
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA-------ASDHLNLVQT-ALRQQEKIERYQADLEELEER-- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1157 llLERWQAVLAQTDVRQRELEqlgRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVReQLRQEKALLE----DI 1232
Cdd:PRK04863 364 --LEEQNEVVEEADEQQEENE---ARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ-ALERAKQLCGlpdlTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1233 ERHGEKVEECQRFAKQYINAIKDYELQLVTYKA---QLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQY-- 1307
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQLqq 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1308 IRFISETLRRMEEEERLAEQQRAEERERL-------AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREE 1380
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAEFCKRLgknlddeDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1381 VAVEAQEQkRSIQEELQHLRQSSEAE----------IQAKARQVEAAERSRLRIEEEIRVVRLQLEATErQRGGAEGE-L 1449
Cdd:PRK04863 598 LAARAPAW-LAAQDALARLREQSGEEfedsqdvteyMQQLLERERELTVERDELAARKQALDEEIERLS-QPGGSEDPrL 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1450 QALRAR-----------------AEEAEA---QKRQA--QEEAERLRRQVQDET-------------QRKRQA-----EA 1489
Cdd:PRK04863 676 NALAERfggvllseiyddvsledAPYFSAlygPARHAivVPDLSDAAEQLAGLEdcpedlyliegdpDSFDDSvfsveEL 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1490 ELALRVQ-AEAE--------------AAREKQralqaLEELRLQAEEAERRLRQAEAERaRQVQVALETAQR-------- 1546
Cdd:PRK04863 756 EKAVVVKiADRQwrysrfpevplfgrAAREKR-----IEQLRAEREELAERYATLSFDV-QKLQRLHQAFSRfigshlav 829
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1547 SAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVA 1626
Cdd:PRK04863 830 AFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEA 909
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1627 QQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ--------------LAEGTAQQRLAAEQEL-IR 1691
Cdd:PRK04863 910 KRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafaltevvqrrahFSYEDAAEMLAKNSDLnEK 989
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1692 LRAETEQGEQQRQLLEEEL--------------ARLQREAAAATQKRRELEAELAK--VRAEMEVLLASKARAEE----- 1750
Cdd:PRK04863 990 LRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQMLQELKQELQDlgVPADSGAEERARARRDElharl 1069
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1751 ----ESRSTSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAKRQRQLAeEDAVRQRAEAERVLAEKLAAIS--EAT 1820
Cdd:PRK04863 1070 sanrSRRNQLEKQLTFCEAEmdnlTKKLRKLERDYHEMREQVVNAKAGWCAV-LRLVKDNGVERRLHRRELAYLSadELR 1148
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1821 RLKTEAEIALKEKEAENERLR---RLAEDEAFQ----------RRLLEEQAAQhkaDIeARLAQLRKASEsELERQKGLV 1887
Cdd:PRK04863 1149 SMSDKALGALRLAVADNEHLRdvlRLSEDPKRPerkvqfyiavYQHLRERIRQ---DI-IRTDDPVEAIE-QMEIELSRL 1223
|
....*....
gi 1920237982 1888 EDTLRQRRQ 1896
Cdd:PRK04863 1224 TEELTSREQ 1232
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2242-2663 |
9.25e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 9.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2242 EEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLK-AEAELLQQQKELAQ--EQAR 2318
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARkaEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2319 RLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRlRVAEMSRAQ-ARAEEDARRF---RKQAEDIGERLYRT 2394
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEER-KAEEARKAEdAKKAEAVKKAeeaKKDAEEAKKAEEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2395 ELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQllqlKSEEMQTVrqEQLLQETQALQQSFLSEKD 2474
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK----KAEEKKKA--DEAKKKAEEAKKADEAKKK 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2475 SLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASME-----------EARRRQHEAE---EGV 2540
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkadaakkkaEEKKKADEAKkkaEED 1403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2541 RRQQEELQRLAQQQQQQEKLL--AEENQRLRERLQHLEEERRAalarseEIAPSRAAAARALPNGQDAADGPAAAAEPEH 2618
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKkkAEEKKKADEAKKKAEEAKKA------DEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1920237982 2619 AFDGLRRKVPAQRLQEVGVLSAEELQQLAQGRTTVAELAQREDVR 2663
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1181-1851 |
1.16e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1181 RQLRYYRESADPLGAWLRDAKQRQEQIQAvpLANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDY---- 1256
Cdd:PRK03918 111 SSVREWVERLIPYHVFLNAIYIRQGEIDA--ILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFikrt 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1257 ---ELQLVTYKAQLEPVASPAKK-----PKVQSGSESIIQEYVDLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQ 1328
Cdd:PRK03918 189 eniEELIKEKEKELEEVLREINEisselPELREELEKLEKEVKELEELKEEIEELEKE-LESLEGSKRKLEEKIRELEER 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1329 RAEERERLAEVE---AALEKQRQLAEAHAQAK-----------------AQAEREAQGLQRRMQEEVARREEVAvEAQEQ 1388
Cdd:PRK03918 268 IEELKKEIEELEekvKELKELKEKAEEYIKLSefyeeyldelreiekrlSRLEEEINGIEERIKELEEKEERLE-ELKKK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1389 KRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQE 1468
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1469 EAERLRRQVQDETQRKRQAEAELALRVQAEAEAarEKQRALQALEELRLQAEEAERRLRQAEAERARQ--VQVALETAQ- 1545
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELTEEHRKELLEEYTA--ELKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEq 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1546 -RSAEAELQSEHASFAEKTAQLERTLKEEhvaVVQLREEATRRAQqqaeaeraraeaerelerwQLKANEALRLRLQAEE 1624
Cdd:PRK03918 505 lKELEEKLKKYNLEELEKKAEEYEKLKEK---LIKLKGEIKSLKK-------------------ELEKLEELKKKLAELE 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1625 VAQQKsltqaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLaEGTAQQRLAAEQELIRLRaeteQGEQQRQ 1704
Cdd:PRK03918 563 KKLDE----------------------LEEELAELLKELEELGFESVEEL-EERLKELEPFYNEYLELK----DAEKELE 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1705 LLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLasKARAEEESRSTSEKskqrleaeagrFRELAEEAARLRALA 1784
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREE-----------YLELSRELAGLRAEL 682
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1785 EEAKRQRQLAEEDAvrqraeaeRVLAEKLAAISEATRLKTEAEIALKEKEAENERLRR---LAEDEAFQR 1851
Cdd:PRK03918 683 EELEKRREEIKKTL--------EKLKEELEEREKAKKELEKLEKALERVEELREKVKKykaLLKERALSK 744
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
23-131 |
1.42e-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: 58.35 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 23 KKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERdvirssRLPREKGRMRFHKLQNV 93
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTID-ER------KLNKKKPKNIFEATENL 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1920237982 94 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 131
Cdd:cd21217 76 NLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1486-1853 |
1.52e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 64.37 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1486 QAEAELALRVQAEAEAAREKQRALQALEELrlqAEEAERRLRQAEAERARQvqvaletaqrsaeAELQSEHASFAEktaq 1565
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEK---AREVERRRKLEEAEKARQ-------------AEMDRQAAIYAE---- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1566 lertlkEEHVAVVQLREeatrraqqqaeaeraraeaereLERWQLKANEALRLRLQAEEVAQQksLTQAEAEKQKEEAER 1645
Cdd:pfam17380 339 ------QERMAMERERE----------------------LERIRQEERKRELERIRQEEIAME--ISRMRELERLQMERQ 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1646 EARRRGKAEEQAVRQRELAEQE-----LEKQRQLAEGTAQQRLAAEQELIRLraETEQGEQQRQLLEEELARLQReaaaa 1720
Cdd:pfam17380 389 QKNERVRQELEAARKVKILEEErqrkiQQQKVEMEQIRAEQEEARQREVRRL--EEERAREMERVRLEEQERQQQ----- 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1721 TQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKskqrlEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAvR 1800
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK-----ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER-R 535
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 1801 QRAEAER---VLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRL 1853
Cdd:pfam17380 536 REAEEERrkqQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
924-1573 |
1.62e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 924 DRLQAEREYgscSRHYQQLLQSLEQGEQEESrcqrcISELKDIRLQLEACEtrtvhrlrlpldkepaRECAQRITEQQKA 1003
Cdd:TIGR02169 201 ERLRREREK---AERYQALLKEKREYEGYEL-----LKEKEALERQKEAIE----------------RQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1004 QAEVDGLGKGVA----RLSAEAEKVLALPEPSPAAptLRSELELTLGKLEQVRSLSAIYLEKL--------KTISLVIRS 1071
Cdd:TIGR02169 257 TEEISELEKRLEeieqLLEELNKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKERELedaeerlaKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1072 TQEAEEVLRAHEEQLKEAQAVPAtlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGE-------- 1143
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTE---EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINElkreldrl 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1144 ------RDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQ--------- 1208
Cdd:TIGR02169 412 qeelqrLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEkelsklqre 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1209 -----AVPLANSQAVREQLRQEKALLEDI--------------ERHGEKVE-------------------ECQRFAKQY- 1249
Cdd:TIGR02169 492 laeaeAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlgsvgERYATAIEvaagnrlnnvvveddavakEAIELLKRRk 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1250 --------INAIK---------------DYELQLVTYKAQLEPVASPAKKPKV-----QSGSESIIQ-----------EY 1290
Cdd:TIGR02169 572 agratflpLNKMRderrdlsilsedgviGFAVDLVEFDPKYEPAFKYVFGDTLvvediEAARRLMGKyrmvtlegelfEK 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1291 VDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRR 1370
Cdd:TIGR02169 652 SGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1371 MQEEVARREEVAVEAQEQKRSIQEELQHLrQSSEAEIQAKARQVEAAERSRLRIE-----EEIRVVRLQLEATERQRGGA 1445
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSEL-KELEARIEELEEDLHKLEEALNDLEarlshSRIPEIQAELSKLEEEVSRI 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1446 EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK---RQAEAELALRVQAEAEAAREKQRALQALEE----LRLQ 1518
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIksiEKEIENLNGKKEELEEELEELEAALRDLESrlgdLKKE 890
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 1519 AEEAERRLRQAEaERARQVQVALETAqRSAEAELQSEHASFAEKTAQLERTLKEE 1573
Cdd:TIGR02169 891 RDELEAQLRELE-RKIEELEAQIEKK-RKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1325-1523 |
2.31e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.90 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1325 AEQQRAEE-RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARReevavEAQEQKrsiQEELQHLRQSS 1403
Cdd:PRK09510 72 KSAKRAEEqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQ-----AALKQK---QAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1404 EAEIQAKARQVEAAERSRlRIEEEIRvVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrrqVQDETQR 1483
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK----AAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1920237982 1484 KRQAEAELAL-RVQAEAEAAREKQRALQALEELRLQAEEAE 1523
Cdd:PRK09510 218 KAAAEAKAAAaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1671-1877 |
2.34e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1671 QRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEE 1750
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1751 ESRSTSEKSKQRLEA--------------EAGRFRELAEEAARLRALAEEAKRQ-----RQLAEEDAVRQRAEAERvlAE 1811
Cdd:COG4942 98 ELEAQKEELAELLRAlyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQaeelrADLAELAALRAELEAER--AE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 1812 KLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASE 1877
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1218-1808 |
2.54e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1218 VREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDlrtRY 1297
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE---EY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1298 SELSTLTSQYIrfisETLRRMEEEERLAEQQRAEERERLAEVEaalEKQRQLaeahaqakaqaeREAQGLQRRMQEEVAR 1377
Cdd:PRK03918 296 IKLSEFYEEYL----DELREIEKRLSRLEEEINGIEERIKELE---EKEERL------------EELKKKLKELEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1378 REEvAVEAQEQKRSIQEELQHLRQS-SEAEIQAKARQVEAAERSRLRIEEEIRVV---RLQLEATERQRGGAEGELQALR 1453
Cdd:PRK03918 357 LEE-RHELYEEAKAKKEELERLKKRlTGLTPEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1454 ARA---------EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlrvqaEAEAAREKQRALQALEELRLQAEEAER 1524
Cdd:PRK03918 436 GKCpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR-----ELEKVLKKESELIKLKELAEQLKELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1525 RLRQAEAERarqvqvaLETAQRSAEaELQSEHASFAEKTAQLERTLKEEHvavvQLREEATRRAQQQAEAERARAEAERE 1604
Cdd:PRK03918 511 KLKKYNLEE-------LEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLKE 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1605 LERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLA 1684
Cdd:PRK03918 579 LEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--ELEKKY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1685 AEQELIRLRAETEQgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLlaSKARAEEESrstSEKSKQRLE 1764
Cdd:PRK03918 657 SEEEYEELREEYLE-------LSRELAGLRAELEELEKRREEIKKTLEKLKEELEER--EKAKKELEK---LEKALERVE 724
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1765 AEAGRFRELAEEAARlRALAEEAKRQRQLAEE------DAVRQRAEAERV 1808
Cdd:PRK03918 725 ELREKVKKYKALLKE-RALSKVGEIASEIFEEltegkySGVRVKAEENKV 773
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
149-251 |
2.84e-09 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 57.77 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 149 TAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 227
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 1920237982 228 PEDVDVPQPDEKSIITYVSSLYDA 251
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1070-1266 |
2.89e-09 |
|
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: 60.15 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1070 RSTQEAEEVLRAHEEQLKEAQaVPATLPELEATKAALKKLRAQAEAQQPVFDALrdelrgaQEVGERLQQRHGERDVEVe 1149
Cdd:cd00176 7 RDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1150 rwRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLGAWLRDAKQRQEQIQavPLANSQAVREQLRQEKALL 1229
Cdd:cd00176 78 --QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELE 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1920237982 1230 EDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1266
Cdd:cd00176 153 EELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2131-2589 |
3.47e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 63.45 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2131 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILdeelqRLKAEVTEAARQRGQVEEELFSLRVQ 2210
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA-----PLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2211 MEELGKLKARIEA--ENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAA---RLRQLAEE---DLAQQRALA 2282
Cdd:TIGR00618 320 MRSRAKLLMKRAAhvKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqHIHTLQQQkttLTQKLQSLC 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2283 EKMLKEKMQAVQEATRLKAEAELLQQ------QKELAQEQARRLQEDKEQMAQQLAQETQGFQK-------------TLE 2343
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGQlahakkQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsaqslkereqqlqTKE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2344 TERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLR 2423
Cdd:TIGR00618 480 QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRA 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2424 EAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEqlLQETQALQQSFLSEKDSLLQRERCIE---------QEKAKLEQLF 2494
Cdd:TIGR00618 560 SLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNI--TVRLQDLTEKLSEAEDMLACEQHALLrklqpeqdlQDVRLHLQQC 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2495 QDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEAR---------------------------------RRQHEAEEGVR 2541
Cdd:TIGR00618 638 SQELALKLTALHALQLTLTQERVREHALSIRVLPKEllasrqlalqkmqsekeqltywkemlaqcqtllRELETHIEEYD 717
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1920237982 2542 RQQEELQRLAQQQQQQeklLAEENQRLRERLQHLEEERRAALARSEEI 2589
Cdd:TIGR00618 718 REFNEIENASSSLGSD---LAAREDALNQSLKELMHQARTVLKARTEA 762
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1694-2283 |
3.62e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1694 AETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTS--EKSKQRLEAEAG--- 1768
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELEslEGSKRKLEEKIRele 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1769 --------RFRELAEEAARLRALAEEAKRQRQLAEEdaVRQRAEAERVLAEKLAAISEATRlktEAEIALKEKEAENERL 1840
Cdd:PRK03918 266 erieelkkEIEELEEKVKELKELKEKAEEYIKLSEF--YEEYLDELREIEKRLSRLEEEIN---GIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1841 RRLAEDEAFQRRLLEEQAAQHKA--DIEARLAQLRKASES----ELERQKGLVEDTLRQRRQVEEEILAL---KGSFEKA 1911
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEISKItarIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1912 AAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLaaeeerrrrEAEERVQKSLAAEEEAARQRKAALEEVERLKAK 1991
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYT---------AELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1992 VEEARRLRERAEQESARQLQLAQEAAQKrlqAEEKAHAF-AVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAeeaeaa 2070
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEYeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELE------ 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2071 reraereaaqsrRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQ 2150
Cdd:PRK03918 563 ------------KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2151 ALRQKAQVEQELTALRLQLEETdhQKSILDEELQRLKAEVTEaarqrgqVEEELFSLRVQMEELGKLKARIEAEnralvL 2230
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEEL--EKKYSEEEYEELREEYLE-------LSRELAGLRAELEELEKRREEIKKT-----L 696
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 2231 RDkdsaqrlLQEEAEKMKQVAEEAARLSVAAQEAARLRQ--LAEEDLAQQRALAE 2283
Cdd:PRK03918 697 EK-------LKEELEEREKAKKELEKLEKALERVEELREkvKKYKALLKERALSK 744
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2228-2579 |
3.75e-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: 63.22 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2228 LVLRDKDSAQRLLQEEAEKM-----KQVAEEAARlsvaaqEAARLRQLAEEDLAQQRALAEkmlkekmqavqeatrlkaE 2302
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqerlRQEKEEKAR------EVERRRKLEEAEKARQAEMDR------------------Q 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2303 AELLQQQKELAQEQARRL----QEDKEQMAQQLAQETQGFQKTLETERQR-QLEMSAEAERLRLRVAEMSRAQARAEEDA 2377
Cdd:pfam17380 333 AAIYAEQERMAMERERELerirQEERKRELERIRQEEIAMEISRMRELERlQMERQQKNERVRQELEAARKVKILEEERQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2378 RRFRKQAEDIGERLYRTELATQEKVmlvQTLETQRQqsdRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQ 2457
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEARQREV---RRLEEERA---REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDR 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2458 LLQETQalqqsflsekdsllqRERCIEQEKAKLEQLFQDEVAKAQALREEqqrqqqqmqqekqqlaasMEEarRRQHEAE 2537
Cdd:pfam17380 487 KRAEEQ---------------RRKILEKELEERKQAMIEEERKRKLLEKE------------------MEE--RQKAIYE 531
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1920237982 2538 EGVRRQQEELQRlaqqqqqqEKLLAEENQRLRERLQHLEEER 2579
Cdd:pfam17380 532 EERRREAEEERR--------KQQEMEERRRIQEQMRKATEER 565
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1173-1551 |
3.78e-09 |
|
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: 63.43 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1173 QRELEQLGRQLRYYRESADplgawlrDAKQRQEQIQA-VPLANSQAvREQLRQekaLLEDIERHGEKVEECQRFAKQYIN 1251
Cdd:COG3096 849 ERELAQHRAQEQQLRQQLD-------QLKEQLQLLNKlLPQANLLA-DETLAD---RLEELREELDAAQEAQAFIQQHGK 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1252 AIkdyelqlvtykAQLEPVASPAKKPKVQSgsESIIQEYVDLRTRYSELStltsQYIRFISETLRRM------EEEERLA 1325
Cdd:COG3096 918 AL-----------AQLEPLVAVLQSDPEQF--EQLQADYLQAKEQQRRLK----QQIFALSEVVQRRphfsyeDAVGLLG 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1326 EQQRAEE--RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEevarreevaveAQEQKRSIQEELQHLrqss 1403
Cdd:COG3096 981 ENSDLNEklRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDA-----------KQQTLQELEQELEEL---- 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1404 eaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQ 1476
Cdd:COG3096 1046 --GVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcAVLRL 1123
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 1477 VQDETQRKRQAEAELalrvqaeaeaarekqrALQALEELRLQAEEAERRLRQAEAERArQVQVALETAQRSAEAE 1551
Cdd:COG3096 1124 ARDNDVERRLHRREL----------------AYLSADELRSMSDKALGALRLAVADNE-HLRDALRLSEDPRRPE 1181
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
144-246 |
4.34e-09 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 57.10 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 144 QSEDMTAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGV 222
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 1920237982 223 TRLLDPEDVDVPQPDEKSIITYVS 246
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1087-1508 |
4.75e-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: 62.83 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1087 KEAQAVPATLPELEA-----------------TKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERdVEVE 1149
Cdd:pfam17380 221 KEVQGMPHTLAPYEKmerrkesfnlaedvttmTPEYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEK-MEQE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1150 RWR---ERVTLLLERWQAVLAQTDVRQRELEqlgRQLRYYRESAdplgawlRDAKQRQEQIQAVPLANSQAVREQLRQEK 1226
Cdd:pfam17380 300 RLRqekEEKAREVERRRKLEEAEKARQAEMD---RQAAIYAEQE-------RMAMERERELERIRQEERKRELERIRQEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1227 ALLEDierhgEKVEECQRFakqyinaikdyelqlvtykaQLEPvaspakkpkvQSGSESIIQEYVDLRtrysELSTLTSQ 1306
Cdd:pfam17380 370 IAMEI-----SRMRELERL--------------------QMER----------QQKNERVRQELEAAR----KVKILEEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1307 YIRFISETLRRMEEEERLAEQQRAEERERLAEveaalEKQRQLAEAHAQakaQAEREAQGLQRRMQEEVARREEVAVEAQ 1386
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQREVRRLEE-----ERAREMERVRLE---EQERQQQVERLRQQEEERKRKKLELEKE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1387 EQKRSIQEELQhlRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqleatERQRGGAEGElqalRARAEEAEAQKRQA 1466
Cdd:pfam17380 483 KRDRKRAEEQR--RKILEKELEERKQAMIEEERKRKLLEKEME---------ERQKAIYEEE----RRREAEEERRKQQE 547
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1920237982 1467 QEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRA 1508
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4361-4399 |
4.76e-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: 4.76e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1920237982 4361 FLEVQYLTGGLIEPDTPGRVALDEALQRGTVDARTAQKL 4399
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1350-1573 |
4.77e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1350 AEAHAQAKAQAEREAQGLQRRMQEEVARREEvaveAQEQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEE 1426
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAA----LKKEEKALLKQLAALERriaALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1427 EIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ 1506
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 1507 RALQALEELRLQAEEAERRLRQAEAERARQVQV--ALETAQRSAEAELQSEHASFAEKTAQLERTLKEE 1573
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARleKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1663-1894 |
4.86e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 61.40 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1663 LAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAelakvraemevll 1742
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAK---KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQA------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1743 askARAEEESRSTSEKSKQRLEAEAGRfrelAEEAARLRALAEEAKRQrqlAEEDAVRQRAEAervlAEKLAaisEATRL 1822
Cdd:TIGR02794 111 ---AKQAEEKQKQAEEAKAKQAAEAKA----KAEAEAERKAKEEAAKQ---AEEEAKAKAAAE----AKKKA---EEAKK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 1823 KTEAEiALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIE----ARLAQLRKASESELERQKGLVEDTLRQR 1894
Cdd:TIGR02794 174 KAEAE-AKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEaaaaAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1467-1948 |
5.10e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1467 QEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQR 1546
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1547 SAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREeatrraqqqaeaeraraeaerelerwqlKANEALRLRLQAEEVA 1626
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEE----------------------------LEAELAELQEELEELL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1627 QQKSLTQAeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1706
Cdd:COG4717 184 EQLSLATE-----------------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1707 EEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRStseKSKQRLEAEAGRFRELAEEAARLRALAEE 1786
Cdd:COG4717 247 EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1787 AKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLE--EQAAQHKAD 1864
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1865 IEARLAQLRKASESELERQKGLVEDTLRQR-RQVEEEILALKGSFEKAAAGKAELELELGRIRGtaEDTLRSKEQAEQEA 1943
Cdd:COG4717 404 LEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEEL 481
|
....*
gi 1920237982 1944 ARQRQ 1948
Cdd:COG4717 482 KAELR 486
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4283-4320 |
6.97e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.03 E-value: 6.97e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1920237982 4283 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 4320
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
17-136 |
7.27e-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: 56.93 E-value: 7.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 17 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSSRLPREKGRMRfhKLQNVQIA 96
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIK---VPVDWNKVNKPPYPKLGANMK--KLENCNYA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1920237982 97 LDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 136
Cdd:cd21331 91 VELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1341-1565 |
7.89e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 61.36 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1341 AALEKQRQLAEAHAQAKAQAEREAQGLQRrmQEEVarREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAK---ARQVEAA 1417
Cdd:PRK09510 60 VVEQYNRQQQQQKSAKRAEEQRKKKEQQQ--AEEL--QQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKqaaLKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1418 ERsrlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDETQRKRQAEAELALRVQ 1496
Cdd:PRK09510 136 EA--------------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 1497 AEAEAAREKQRALQAleelrlqAEEAErrlRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ 1565
Cdd:PRK09510 197 AEAKKKAEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1315-1535 |
8.76e-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: 60.93 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1315 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQE 1394
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1395 ---ELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1471
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 1472 RLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERAR 1535
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1794-2327 |
8.80e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 8.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1794 AEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdEAFQRRLLEEQAAQHKADIEARLAQLR 1873
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1874 KASESELERQKGLVEDT--LRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAA 1951
Cdd:PRK03918 266 ERIEELKKEIEELEEKVkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1952 EEERrrreaeerVQKSLAAEEEAArqrkaalEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAfA 2031
Cdd:PRK03918 346 KLKE--------LEKRLEELEERH-------ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS-K 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2032 VQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEReaaqsRRQVEEAERLKQSAEEQAQAQAQAQAAAEK 2111
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELL-----EEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2112 LRKEAEQEAARraqaeqaaLRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKA--- 2188
Cdd:PRK03918 485 LEKVLKKESEL--------IKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkk 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2189 EVTEAARQRGQVEEELFSLRVQMEELG---------KLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEA-ARLS 2258
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGfesveeleeRLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAfEELA 636
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2259 VAAQEAARLR-QLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2327
Cdd:PRK03918 637 ETEKRLEELRkELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2138-2588 |
9.22e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.91 E-value: 9.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2138 DAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKaevtEAARQRGQVEEELFSLRVQMEELGKL 2217
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR----EAQEEQLKKQQLLKQLRARIEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2218 KARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEA-ARLSVAAQEAARLRQLA------EEDLAQQRALAEKMLKEKM 2290
Cdd:TIGR00618 276 EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIhTELQSKMRSRAKLLMKRaahvkqQSSIEEQRRLLQTLHSQEI 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2291 QAVQEATRLKAEAELLQQQKELAQeQARRLQEDKEQMAQQLaqetQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQ 2370
Cdd:TIGR00618 356 HIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKL----QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2371 ARAEEDARRFRKQAEDIGER----------LYRTELATQEKVMLVQTLETQRQQSDR-----DAERLREAIAELEHEKDK 2435
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITCTaqceklekihLQESAQSLKEREQQLQTKEQIHLQETRkkavvLARLLELQEEPCPLCGSC 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2436 LKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQM 2515
Cdd:TIGR00618 511 IHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 2516 QQEKQQLAASMEEARRR------QHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEE 2588
Cdd:TIGR00618 591 NITVRLQDLTEKLSEAEdmlaceQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRV 669
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1321-1535 |
1.16e-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: 60.24 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1321 EERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSiQEELQHLR 1400
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQK-QAEEAKAK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1401 QSSEAEIQAKA-RQVEAAERSRLRIEEEirvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE----AERLRR 1475
Cdd:TIGR02794 128 QAAEAKAKAEAeAERKAKEEAAKQAEEE----AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakakAEAAKA 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1476 QVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERAR 1535
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1352-1811 |
1.29e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 61.57 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1352 AHAQAKAQAEREAQGLQRRMQEEVARreeVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVV 1431
Cdd:COG3903 475 EYAAERLAEAGERAAARRRHADYYLA---LAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1432 RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQA 1511
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1512 LEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQ 1591
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1592 AEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1671
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1672 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE 1751
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1752 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAE 1811
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
144-251 |
1.31e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 55.48 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 144 QSEDMTAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGV 222
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1920237982 223 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 251
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1069-2006 |
1.35e-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: 61.51 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1069 IRSTQEAEEVLRAHEEQLKEAQAvpatlpeleatkaALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQ--RHGERdv 1146
Cdd:COG3096 284 SERALELRRELFGARRQLAEEQY-------------RLVEMARELEELSARESDLEQDYQAASDHLNLVQTalRQQEK-- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1147 eVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVReqlrqek 1226
Cdd:COG3096 349 -IERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ------- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1227 ALledierhgEKVEECQRFAKQYINAIKDYelqLVTYKAQLEpvaspakkpkvqsgseSIIQEYVDLRTRYSELSTLTSQ 1306
Cdd:COG3096 421 AL--------EKARALCGLPDLTPENAEDY---LAAFRAKEQ----------------QATEEVLELEQKLSVADAARRQ 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1307 YIRFIsETLRRMEEE-ERLAEQQRAEERER-------LAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARR 1378
Cdd:COG3096 474 FEKAY-ELVCKIAGEvERSQAWQTARELLRryrsqqaLAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1379 EEVAVEAQEQKRSIQEELQHLRQSSEAEIQakarqveaaersrlrieeeirvvrlqleaTERQRGGAEGELQALRARAEE 1458
Cdd:COG3096 553 EELEELLAELEAQLEELEEQAAEAVEQRSE-----------------------------LRQQLEQLRARIKELAARAPA 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1459 AeaqkRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAeeaeRRLRQAE-AERARQV 1537
Cdd:COG3096 604 W----LAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQI----ERLSQPGgAEDPRLL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1538 Q----------------VALETAQR-------SAEAELQSEHASFAEKTAQLERTLkeEHVAVVQLREEATRRAQQQAEA 1594
Cdd:COG3096 676 AlaerlggvllseiyddVTLEDAPYfsalygpARHAIVVPDLSAVKEQLAGLEDCP--EDLYLIEGDPDSFDDSVFDAEE 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1595 ERARAEAERELERWQL-------------KANEALRLRLQAEEVAQQKSltqaeaekqkeeaerearrrgkaeEQAVRQR 1661
Cdd:COG3096 754 LEDAVVVKLSDRQWRYsrfpevplfgraaREKRLEELRAERDELAEQYA------------------------KASFDVQ 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1662 ELaeQELEKQ-RQLAEGTAQQRLAAEQElirlrAETEQGEQQRQLLEEELARL----QREAAAATQKRRELEAeLAKVRA 1736
Cdd:COG3096 810 KL--QRLHQAfSQFVGGHLAVAFAPDPE-----AELAALRQRRSELERELAQHraqeQQLRQQLDQLKEQLQL-LNKLLP 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1737 EMEVL----LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA--LAEEAKRQRQL---AEEDAVRQRAEAER 1807
Cdd:COG3096 882 QANLLadetLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSdpEQFEQLQADYLqakEQQRRLKQQIFALS 961
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1808 VLAEKLAAISEAtrlktEAEIALKEKEAENERLR---RLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQK 1884
Cdd:COG3096 962 EVVQRRPHFSYE-----DAVGLLGENSDLNEKLRarlEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQ 1036
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1885 GLvedtlrQRRQVEEEILALKGSFEKAAAGKAELELELGRIRG--TAEDTLRSKEQAEQEAARQRqlaaeeerrrreaEE 1962
Cdd:COG3096 1037 EL------EQELEELGVQADAEAEERARIRRDELHEELSQNRSrrSQLEKQLTRCEAEMDSLQKR-------------LR 1097
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*.
gi 1920237982 1963 RVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRL--RERAEQES 2006
Cdd:COG3096 1098 KAERDYKQEREQVVQAKAGWCAVLRLARDNDVERRLhrRELAYLSA 1143
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2131-2587 |
1.49e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2131 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEET-----DHQKSILDEELQRLKAEVTEAARQRGQVEEELF 2205
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2206 SLRVQMEELG-----KLKARIEAENRALVLRDKDSAQrlLQEEAEKMK-QVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2279
Cdd:COG4913 327 ELEAQIRGNGgdrleQLEREIERLERELEERERRRAR--LEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2280 ALAEKMLKEKMQAVQEATRLKAEAELLQQQK---ELAQEQARR-----LQEDKEQM------------------------ 2327
Cdd:COG4913 405 EALAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRDalaeaLGLDEAELpfvgelievrpeeerwrgaiervl 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2328 ---AQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLyRTELATQEKVML 2404
Cdd:COG4913 485 ggfALTLLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWL-EAELGRRFDYVC 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2405 VQTLE-------------------TQRQQSDRDAERL--------REAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQ-- 2455
Cdd:COG4913 564 VDSPEelrrhpraitragqvkgngTRHEKDDRRRIRSryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDal 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2456 EQLLQETQALQQSFLSEKDsLLQRERCIEQEKAKLEQL--FQDEVAKAQALREEqqrqqqqmqqekqqLAASMEEARRRQ 2533
Cdd:COG4913 644 QERREALQRLAEYSWDEID-VASAEREIAELEAELERLdaSSDDLAALEEQLEE--------------LEAELEELEEEL 708
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 2534 HEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSE 2587
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
14-134 |
1.67e-08 |
|
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: 55.67 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 14 LKDERDRVQ--KKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDVIRSSRLPrekgrmrfHKLQ 91
Cdd:cd21222 7 FDEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPLHEYHLTPSTDD--------EKLH 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237982 92 NVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 134
Cdd:cd21222 79 NVKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1336-1748 |
1.89e-08 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 61.03 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1336 LAEVEAALEKQRQLAEAHAQAkaqaeREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE----------- 1404
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVA-----REDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1405 --------AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1476
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1477 VQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEH 1556
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1557 ASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEA 1636
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1637 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQRE 1716
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 1920237982 1717 AAAATQKRRELEAELAKVRAEMEVLLASKARA 1748
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1464-1984 |
1.93e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1464 RQAQEEAERLRRQVQD----ETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARqvqv 1539
Cdd:COG4913 238 ERAHEALEDAREQIELlepiRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER---- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1540 aLETAQRSAEAELQSEHASFAEKTAQLERTLKEEhvavvqlreeatrraqqqaeaeraraeaereLERWQLKANEALRLR 1619
Cdd:COG4913 314 -LEARLDALREELDELEAQIRGNGGDRLEQLERE-------------------------------IERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1620 LQAEEVAQQKSLTQAEAEKQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG 1699
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFA----------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1700 EQQRQLLEEELARLQREAAAATQ-KRRELE--AELAKVRAE-------MEVLLASKAR---------------------- 1747
Cdd:COG4913 432 ERRKSNIPARLLALRDALAEALGlDEAELPfvGELIEVRPEeerwrgaIERVLGGFALtllvppehyaaalrwvnrlhlr 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1748 ------------AEEESRSTSEKS-KQRLEAEAGRFR-----ELAEEAARLRALAEEA-----------------KRQRQ 1792
Cdd:COG4913 512 grlvyervrtglPDPERPRLDPDSlAGKLDFKPHPFRawleaELGRRFDYVCVDSPEElrrhpraitragqvkgnGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1793 LAEEDAVRQR----AEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEE-----QAAQHKA 1863
Cdd:COG4913 592 KDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeidvaSAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1864 DIEARLAQLRKASeSELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRirgtAEDTLRSKEQAEQEA 1943
Cdd:COG4913 672 ELEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE----LQDRLEAAEDLARLE 746
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1920237982 1944 ARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 1984
Cdd:COG4913 747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
22-133 |
3.48e-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: 54.43 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 22 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirSSRLPRekgRMRFHKLQNVQIALDYLR 101
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKH----ANKPPI---KMPFKKVENCNQVVKIGK 75
|
90 100 110
....*....|....*....|....*....|..
gi 1920237982 102 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 133
Cdd:cd21299 76 QLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
496-685 |
3.65e-08 |
|
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: 57.07 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 496 LRYLQDLLAWVEENQRRLDSAEWGVDLPSVEAQLGSHRGLHQSVEEFRTKIERARTDEGQLSPATRGAY---RDCLGRLD 572
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 573 LQYAKLLSSSKARLRSLE---SLHGFVAAATKELMWLSDREEEEVGFDWSDRNTNMAAKKEGYSALMHELELKEKKIKEI 649
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1920237982 650 QSTGDRLLREDHP-ARPTAESFQAALQTQWSWMLQLC 685
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1664-1851 |
4.76e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.66 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1664 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA--AATQKRRELEAELAKVRAEMEVL 1741
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQkqAEEAAAKAAAAAKAKAEAEAKRA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1742 LASKARAEEESrstseksKQRLEAEAgrfRELAEEAARLRALAEEAKrqrQLAEEDAVRQRAEAERVlAEKLAAISEATR 1821
Cdd:PRK09510 157 AAAAKKAAAEA-------KKKAEAEA---AKKAAAEAKKKAEAEAAA---KAAAEAKKKAEAEAKKK-AAAEAKKKAAAE 222
|
170 180 190
....*....|....*....|....*....|
gi 1920237982 1822 LKTEAEIALKEKEAENERLRRLAEDEAFQR 1851
Cdd:PRK09510 223 AKAAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1074-1429 |
4.76e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1074 EAEEVLRAHEEQLKEAQAVPATL-PELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWR 1152
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1153 ERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLrDAKQRQEQIQAVPLANSQAVREQLRQEKALLED- 1231
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL-DELRAELTLLNEEAANLRERLESLERRIAATERr 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1232 IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYVDLRTRYSELstltsqyirfi 1311
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELE---------ALLNERASLEEALALLRSELEEL----------- 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1312 SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ------------------LAEAHAQAKAQAEREAQGLQRRMQE 1373
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVridnlqerlseeysltleEAEALENKIEDDEEEARRRLKRLEN 979
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 1374 EVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAErsrlRIEEEIR 1429
Cdd:TIGR02168 980 KIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE----EIDREAR 1031
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1470-1929 |
5.59e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 59.65 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1470 AERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQAleelRLQAEEAERRLRQAEAERARQVQVALETAqrSAE 1549
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLA----RLDAEHDNLRAALRWALAHGDAELALRLA--AAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1550 AELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQK 1629
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1630 SLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1709
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1710 LARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKR 1789
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1790 QRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARL 1869
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1870 AQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTA 1929
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1386-1926 |
5.64e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 58.89 E-value: 5.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1386 QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEeirvVRLQLE--ATERQRGGAEGELQALRARaeeaEAQK 1463
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEE----LKLNLEraQTEEAQAKQDSELAKLRVE----EMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1464 RQAQEEAERLRRQVQDETQRKRQAEAELALrVQAE--------AEAAREKQRALQALEELRLQAEEAERRLRQAEAERAr 1535
Cdd:pfam05701 113 GIADEASVAAKAQLEVAKARHAAAVAELKS-VKEEleslrkeyASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1536 QVQVALETAQRS-AEAELQSEHASFA--EKTAQLERTLKEEHVAVVQLREEATRRAQQQAeaeraraeaerelerwQLKA 1612
Cdd:pfam05701 191 ATKESLESAHAAhLEAEEHRIGAALAreQDKLNWEKELKQAEEELQRLNQQLLSAKDLKS----------------KLET 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1613 NEALRLRLQAEEVAQQKSltqaeaekqkeEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEgtaqqRLAAEQEL 1689
Cdd:pfam05701 255 ASALLLDLKAELAAYMES-----------KLKEEADGEGNEKKTSTSIQAalaSAKKELEEVKANIE-----KAKDEVNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1690 IRLRAETEQGEQQRQllEEELARLQREAAAATQKRRELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAeagr 1769
Cdd:pfam05701 319 LRVAAASLRSELEKE--KAELASLRQREGMASIAVSSLEAELNRTKSEIALV---QAKEKEAREKMVELPKQLQQA---- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1770 frelAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEA--ENERLRRLAEDE 1847
Cdd:pfam05701 390 ----AQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlqESESSAESTNQE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1848 AFQR----------------RLLEEQAaqhKADIEARLAQLRKASESELERQKGLvEDTLRQRRQVEEEILALKGSFEKA 1911
Cdd:pfam05701 466 DSPRgvtlsleeyyelskraHEAEELA---NKRVAEAVSQIEEAKESELRSLEKL-EEVNREMEERKEALKIALEKAEKA 541
|
570
....*....|....*
gi 1920237982 1912 AAGKAELELELGRIR 1926
Cdd:pfam05701 542 KEGKLAAEQELRKWR 556
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2149-2589 |
5.76e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 59.47 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2149 EQALRQKAQVEQELTALRLQL-EETDHQKSILDEELQRLKAEVTEAARQRGQV---EEELFSLRVQMEELGKLKARIEAE 2224
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERAREEQEAA 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2225 NRAlvlrdkdsaQRLLQEEAEKMKQVAEEAARlsvaaqeaaRLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAE 2304
Cdd:pfam12128 484 NAE---------VERLQSELRQARKRRDQASE---------ALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAP 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2305 LLQQQ--KELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA-------QARAEE 2375
Cdd:pfam12128 546 DWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEAlqsarekQAAAEE 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2376 DARRFRKQAE--DIGERLYRTELaTQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTV 2453
Cdd:pfam12128 626 QLVQANGELEkaSREETFARTAL-KNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEE 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2454 RQEQLLQETQALQQSFL---SEKDSLLQR-----ERCIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQMQQEKQQLAAS 2525
Cdd:pfam12128 705 QKEQKREARTEKQAYWQvveGALDAQLALlkaaiAARRSGAKAELKAL-ETWYKRDLASLGVDPDVIAKLKREIRTLERK 783
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 2526 MEEARRRQHEAEEGVRRQQE----ELQRLAQQQQQQEKLLAEENQRL-------RERLQHLEEERRAALARSEEI 2589
Cdd:pfam12128 784 IERIAVRRQEVLRYFDWYQEtwlqRRPRLATQLSNIERAISELQQQLarliadtKLRRAKLEMERKASEKQQVRL 858
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2140-2588 |
6.63e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2140 EMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEE------ELFSLRVQMEE 2213
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiklseFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2214 LGKLKARIEAENRAL--VLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralAEKMLKEKmq 2291
Cdd:PRK03918 312 IEKRLSRLEEEINGIeeRIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--------LERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2292 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQ-----RQLEMSAEAERLRLRVAEM 2366
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2367 SRAQ---ARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKL-KQEAQL 2442
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2443 LQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRER-----CIEQEKAKLEQL--FQDEVAKAQALREEQQRQQQQM 2515
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELepFYNEYLELKDAEKELEREEKEL 621
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237982 2516 QQEKQQLAASMEEARRRQHEAEEgVRRQQEELQRlaqqqqqqeKLLAEENQRLRERLQHLEEERRAALARSEE 2588
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEE-LRKELEELEK---------KYSEEEYEELREEYLELSRELAGLRAELEE 684
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
153-248 |
7.08e-08 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 54.23 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 153 KLLL-WSQrMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNL-----------------------EN 208
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 209 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 248
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1627-1822 |
7.31e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.28 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1627 QQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1706
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1707 EEELARLQREAAAATQKRRELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1786
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 1920237982 1787 AKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRL 1822
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2181-2449 |
8.10e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2181 EELQRLKAEVTEAARQRGQVE------EELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEkmkQVAEEA 2254
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA---RLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2255 ARLSVAAQEAARLRQLAEEDLAQQralaekmlkekmqAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQE 2334
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGN-------------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2335 TQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQaedigerlyrtelatqekvmlVQTLETQRQQ 2414
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE---------------------IASLERRKSN 437
|
250 260 270
....*....|....*....|....*....|....*.
gi 1920237982 2415 SDRDAERLREAIAE-LEHEKDKLKQEAQLLQLKSEE 2449
Cdd:COG4913 438 IPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1374-1539 |
1.01e-07 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 58.61 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1374 EVARR----EEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegel 1449
Cdd:COG1193 490 EIARRlglpEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEK------- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1450 QALRARA-EEAEAQKRQAQEEAERLRRQVQDEtqrkrqaeaelalrvQAEAEAAREKQRALQALEElRLQAEEAERRLRQ 1528
Cdd:COG1193 563 EEILEKArEEAEEILREARKEAEELIRELREA---------------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKA 626
|
170
....*....|.
gi 1920237982 1529 AEAERARQVQV 1539
Cdd:COG1193 627 KPAKPPEELKV 637
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1405-1557 |
1.03e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 57.96 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1405 AEIQAKARQVEA-AERsrlriEEEIRVVRLQLEATERQrggAEGELQALRARAEEAEAQKRQAQEEAERlrrqvqdETQR 1483
Cdd:COG2268 195 AEIIRDARIAEAeAER-----ETEIAIAQANREAEEAE---LEQEREIETARIAEAEAELAKKKAEERR-------EAET 259
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237982 1484 KRqAEAELALRVQaEAEAAREKQRALQALE---ELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHA 1557
Cdd:COG2268 260 AR-AEAEAAYEIA-EANAEREVQRQLEIAErerEIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRA 334
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4014-4050 |
1.16e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.56 E-value: 1.16e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1920237982 4014 IRLLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEM 4050
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1454-1905 |
1.18e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1454 ARAEEAEAQKRQAQEEAERLRRQVQD-ETQRKRQAEAELAL----RVQAEAEAAREKQRALQALEELRLQAEEAERRLRQ 1528
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELeelrEELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1529 AEAERARQVQV-----ALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEaer 1603
Cdd:COG4717 151 LEERLEELRELeeeleELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE--- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1604 elerwQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAvrqrELAEQELEKQRQLAEGTAQQRL 1683
Cdd:COG4717 228 -----ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA----GVLFLVLGLLALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1684 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRstsEKSKQRL 1763
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL---EQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1764 EAEAGrfrelAEEAARLRALAEEAKRQRQLAEEdavrqRAEAERVLAEKLAAISEATRLKTEAEiaLKEKEAENERLRRL 1843
Cdd:COG4717 376 LAEAG-----VEDEEELRAALEQAEEYQELKEE-----LEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEE 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 1844 AEDEafqrrllEEQAAQHKADIEARLAQLrkASESELERQKGLVEDTLRQRRQVEEEILALK 1905
Cdd:COG4717 444 LEEE-------LEELREELAELEAELEQL--EEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
24-130 |
1.29e-07 |
|
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: 52.72 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 24 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLpreRDVirsSRLPREKGRMrfhkLQNVQIALDYLR 101
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKV---EDI---NGCPRSQSQM----IENVDVCLSFLA 72
|
90 100
....*....|....*....|....*....
gi 1920237982 102 HRQVKLVNIRNDDIADGNPKLTLGLIWTI 130
Cdd:cd21286 73 ARGVNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1313-1573 |
1.63e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 56.85 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1313 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSI 1392
Cdd:pfam13868 46 DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1393 QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1472
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1473 LR-RQVQDETQRK-RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEA 1550
Cdd:pfam13868 206 LRaKLYQEEQERKeRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRR 285
|
250 260
....*....|....*....|...
gi 1920237982 1551 ELQSEHASFAEKTAQLERTLKEE 1573
Cdd:pfam13868 286 MKRLEHRRELEKQIEEREEQRAA 308
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1040-1488 |
1.65e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1040 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKA-------ALKKLRAQ 1112
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAelaelpeRLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1113 AEAQQPVFDALRDELRGAQEVGERLQQrhgERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADP 1192
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1193 LGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKVeecqrfakQYINAIKDYELQLVTYKAQLEPVAS 1272
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV--------LFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1273 PAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRfiseTLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA 1352
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELL----ELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1353 HAQAKAQAEREAQGLQRRmQEEVARREEVAVEAQEQKRSIQEELQHLRQSS-EAEIQAKARQVEAAERSRLRIEEEIRVV 1431
Cdd:COG4717 380 GVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAEL 458
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237982 1432 RLQLEATERqrggaEGELQALRARAEEAEAQKRQAQEEAERLR------RQVQDETQRKRQAE 1488
Cdd:COG4717 459 EAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPP 516
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1021-1583 |
1.80e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1021 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLKEaqaVPATLPELE 1100
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1101 ATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLqqrhgerdvevERWRERvtllLERWQAVLAQTDVRQRELEQLG 1180
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL-----------SRLEEE----INGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1181 RQLRYYRESADPLGAWLR---DAKQRQEQIqavplansqavrEQLRQEKALL--EDIERHGEKVEECQRFAKQYINAIKD 1255
Cdd:PRK03918 345 KKLKELEKRLEELEERHElyeEAKAKKEEL------------ERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1256 YELQLVTYKAQLEPVASPAKKPKVQS---GSESIIQEYVDLRTRYSElstltsqYIRFISETLRRMEEEERlaeqqraEE 1332
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKCpvcGRELTEEHRKELLEEYTA-------ELKRIEKELKEIEEKER-------KL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1333 RERLAEVEAALEKQRQLAEAHAQAKaqaereaqglQRRMQEEvaRREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKAR 1412
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELAE----------QLKELEE--KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1413 QVEAAERsrlrIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1492
Cdd:PRK03918 547 ELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1493 lRVQAEAEAAREK-QRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERtLK 1571
Cdd:PRK03918 623 -KLEEELDKAFEElAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK-LK 700
|
570
....*....|..
gi 1920237982 1572 EEHVAVVQLREE 1583
Cdd:PRK03918 701 EELEEREKAKKE 712
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1321-1948 |
2.39e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 57.50 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1321 EERLAEQQRAeeRERLAEVEAALEK-QRQLA------------------EAHAQAKAQAEREAQGLQRRMQEEVARREEV 1381
Cdd:PRK10246 253 DELQQEASRR--QQALQQALAAEEKaQPQLAalslaqparqlrphweriQEQSAALAHTRQQIEEVNTRLQSTMALRARI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1382 AVEAQEQKRSIQEELQHLRQ-SSEAEIQAKARQVEAAERSRL----RIEEEIRVVRLQLEATERQRGGAEGELQALRARa 1456
Cdd:PRK10246 331 RHHAAKQSAELQAQQQSLNTwLAEHDRFRQWNNELAGWRAQFsqqtSDREQLRQWQQQLTHAEQKLNALPAITLTLTAD- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1457 EEAEAQKRQAQEEAER-----LRRQVQDETQRKRQAEAelalrvqAEAEAAREKQRALQALEELRLQAEEAERRLRQAEA 1531
Cdd:PRK10246 410 EVAAALAQHAEQRPLRqrlvaLHGQIVPQQKRLAQLQV-------AIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKT 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1532 ERARQVQVALETAQRsaeAELQS----------EHASFAEKTAqLERTlkeehvaVVQLREEATRRAQQQAeaeraraea 1601
Cdd:PRK10246 483 ICEQEARIKDLEAQR---AQLQAgqpcplcgstSHPAVEAYQA-LEPG-------VNQSRLDALEKEVKKL--------- 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1602 erelerwqlkANEALRLRLQAEEVAQQKSltqaeaekqkeeaerearrrgKAEEQAVRQRElAEQELEKQRQLAEGTAQQ 1681
Cdd:PRK10246 543 ----------GEEGAALRGQLDALTKQLQ---------------------RDESEAQSLRQ-EEQALTQQWQAVCASLNI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1682 RLAAEQELIRLRAETEQGEQQRQLLEEELArLQREAAAATQKRRELEAELAKVRAEMEVLLASKA------RAEEESRST 1755
Cdd:PRK10246 591 TLQPQDDIQPWLDAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWLAT 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1756 SEKSKQRLEAEAGRFRELAEEAARLRALAEeakrqrQLAEEDAVrqRAEAERVLAEKLAAISEATrLKTEAEIALKEKEA 1835
Cdd:PRK10246 670 RQQEAQSWQQRQNELTALQNRIQQLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQQD 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1836 ENERLR---------------RLAEDEAFQRRLLEEQAAQhkadieaRLAQLRKASESELERQKGLVEdtlrQRRQVEEE 1900
Cdd:PRK10246 741 VLEAQRlqkaqaqfdtalqasVFDDQQAFLAALLDEETLT-------QLEQLKQNLENQRQQAQTLVT----QTAQALAQ 809
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1920237982 1901 ILALKGSFEKAAAGKAELELELGRIRGT-AEDTLRSKE---QAEQEA-ARQRQ 1948
Cdd:PRK10246 810 HQQHRPDGLDLTVTVEQIQQELAQLAQQlRENTTRQGEirqQLKQDAdNRQQQ 862
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1685-1885 |
2.44e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1685 AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1764
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1765 A---------------EAGRFRELAEEAARLRALAEEAKR---QRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEA 1826
Cdd:COG3883 94 AlyrsggsvsyldvllGSESFSDFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 1827 EIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKG 1885
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1664-1916 |
2.81e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1664 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLA 1743
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1744 SKARAEE---------ESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEK 1812
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1813 LAAISEATRLKteAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLR 1892
Cdd:COG3883 174 EAQQAEQEALL--AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
250 260
....*....|....*....|....
gi 1920237982 1893 QRRQVEEEILALKGSFEKAAAGKA 1916
Cdd:COG3883 252 AGAAGAAAGSAGAAGAAAGAAGAG 275
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1306-1567 |
2.82e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.88 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1306 QYIRFISETLRRMEEEERLAEQ--QRAEER-ERLAEVEAA-LEKQRQLAEAHAQAKAQA---------EREAQGLQRRMQ 1372
Cdd:PRK05035 429 QYYRQAKAEIRAIEQEKKKAEEakARFEARqARLEREKAArEARHKKAAEARAAKDKDAvaaalarvkAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1373 EEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAA-ERSRLRIEEeirvvrlQLEATERQRGGAEGELQA 1451
Cdd:PRK05035 509 KAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAiARAKAKKAA-------QQAANAEAEEEVDPKKAA 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1452 LRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAelalrvqaeAEAAREKQRALQALEELRLQAEEAERRLRQAEA 1531
Cdd:PRK05035 582 VAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAA---------AIARAKAKKAEQQANAEPEEPVDPRKAAVAAAI 652
|
250 260 270
....*....|....*....|....*....|....*.
gi 1920237982 1532 ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLE 1567
Cdd:PRK05035 653 ARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAK 688
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1417-1537 |
2.89e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 55.82 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1417 AERSRLRIEEEIRVVRLQLEATERQRGgAEGELQALRARAEEAEAQKRQAQEEAERLR---------RQVQDETQRKR-Q 1486
Cdd:COG1566 81 LQAALAQAEAQLAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQalykkgavsQQELDEARAALdA 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1920237982 1487 AEAELAlRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV 1537
Cdd:COG1566 160 AQAQLE-AAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1671-1871 |
3.39e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 56.42 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1671 QRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRqllEEELARLQREAAAATQKRRELEAELAKVraemevllaskaraEE 1750
Cdd:COG2268 191 RRKIAEIIRDARIAEAE--AERETEIAIAQANR---EAEEAELEQEREIETARIAEAEAELAKK--------------KA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1751 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEA-----ERVLAEKLAAISEAtrlKTE 1825
Cdd:COG2268 252 EERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELeadvrKPAEAEKQAAEAEA---EAE 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1920237982 1826 AEIALKEKEAENERLRRLAE-DEAFQRRLLEEQAAQHKADIEARLAQ 1871
Cdd:COG2268 329 AEAIRAKGLAEAEGKRALAEaWNKLGDAAILLMLIEKLPEIAEAAAK 375
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2249-2702 |
4.45e-07 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 56.52 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2249 QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMA 2328
Cdd:COG4995 9 LLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2329 QQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTL 2408
Cdd:COG4995 89 LLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2409 ETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKA 2488
Cdd:COG4995 169 ALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2489 KLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRL 2568
Cdd:COG4995 249 ALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2569 RERLQHLEEERRAALARSEEIAPSRAAAARALPNGQDAADGPAAAAEPEHAFDGLRRKVPAQRLQEVGVLSAEELQQLAQ 2648
Cdd:COG4995 329 ALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQL 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 2649 GRTTVAELAQREDVRHYLQGRSSIAGLL-LKPADEKLTIYAALRRQLLSPGTALI 2702
Cdd:COG4995 409 LRLLLAALALLLALAAYAAARLALLALIeYIILPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1700-1884 |
4.45e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.58 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1700 EQQRQLLEEELAR-LQREAAAATQKRRELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEAGrfrelAEEAA 1778
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAK-----AAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1779 RLRALAEeakrqrQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRrllEEQA 1858
Cdd:PRK09510 146 KAKAEAE------AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK--AEAEAKKK---AAAE 214
|
170 180
....*....|....*....|....*.
gi 1920237982 1859 AQHKADIEARLAQLRKASESELERQK 1884
Cdd:PRK09510 215 AKKKAAAEAKAAAAKAAAEAKAAAEK 240
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1652-1869 |
5.04e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 55.24 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1652 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRreleAEL 1731
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKA----KEE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1732 AKVRAEMEvllaSKARAEEESRSTSEKSKQRLEAEAgrfreLAEEAARLRALAEEAKRQRQLAEEDA---VRQRAEAERV 1808
Cdd:TIGR02794 148 AAKQAEEE----AKAKAAAEAKKKAEEAKKKAEAEA-----KAKAEAEAKAKAEEAKAKAEAAKAKAaaeAAAKAEAEAA 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 1809 LAEKLAAISEATRLKTEAEIAL-KEKEAENERLRRLAEDEAFQRRLleeqAAQHKADIEARL 1869
Cdd:TIGR02794 219 AAAAAEAERKADEAELGDIFGLaSGSNAEKQGGARGAAAGSEVDKY----AAIIQQAIQQNL 276
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2137-2337 |
5.45e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2137 ADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEE--- 2213
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2214 --------LGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM 2285
Cdd:COG3883 94 alyrsggsVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 2286 LKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQG 2337
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1724-2430 |
5.53e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1724 RRELEAELAKVRAEMEVLLASKARAEEESRStsEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRA 1803
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQ--IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1804 EAERvlaeklaaiSEATRLKTEAEIALKEKEAENERLRRLaedeafqrrllEEQAAQHKADIEARLAQLRKASESELERQ 1883
Cdd:COG4913 298 EELR---------AELARLEAELERLEARLDALREELDEL-----------EAQIRGNGGDRLEQLEREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1884 KGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQlaaeeerrrreaeer 1963
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR--------------- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1964 vqkSLAAEEEAARQRKAAL-EEVERLKAKVEEARRLRE------------RAEQES-------------------ARQLQ 2011
Cdd:COG4913 423 ---ELEAEIASLERRKSNIpARLLALRDALAEALGLDEaelpfvgelievRPEEERwrgaiervlggfaltllvpPEHYA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2012 LAQEAAQkRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAAREraereaaqSRRQVEEAERL 2091
Cdd:COG4913 500 AALRWVN-RLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAELGRRF--------DYVCVDSPEEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2092 KQSAEEQAQAQaqaqaaaekLRKeaeqeaarraqaEQAALRQKQAADAEMEKHkQFAEQALRQKAQVEQELTALRLQLEE 2171
Cdd:COG4913 571 RRHPRAITRAG---------QVK------------GNGTRHEKDDRRRIRSRY-VLGFDNRAKLAALEAELAELEEELAE 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2172 TDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQmEELGKLKARIEAenralvLRDKDSAQRLLQEEAEKMKQVA 2251
Cdd:COG4913 629 AEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-REIAELEAELER------LDASSDDLAALEEQLEELEAEL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2252 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ-QKELAQEQARRLQEDKEQMAQQ 2330
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAlGDAVERELRENLEERIDALRAR 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2331 LAQETQGFQKTleterqrqleMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERL------YRTELATQEKVML 2404
Cdd:COG4913 782 LNRAEEELERA----------MRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYeerfkeLLNENSIEFVADL 851
|
730 740
....*....|....*....|....*.
gi 1920237982 2405 VQTLETQRQQSDRDAERLREAIAELE 2430
Cdd:COG4913 852 LSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2144-2447 |
6.11e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2144 HKQFAEQALRQKAQVEQ---ELTALRLQLEETDHQKSILDEELQRLKAEVTEAarqrgqvEEELFSLRVQME-------- 2212
Cdd:PRK04863 336 HLNLVQTALRQQEKIERyqaDLEELEERLEEQNEVVEEADEQQEENEARAEAA-------EEEVDELKSQLAdyqqaldv 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2213 ---------------------------ELGKLKARIEAenraLVLRDKDSAQRLLQEE-----AEKMKQVAEEAARL--- 2257
Cdd:PRK04863 409 qqtraiqyqqavqalerakqlcglpdlTADNAEDWLEE----FQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrk 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2258 ---SVAAQEAARLRQLAEEDLAQQRALAEKM---------LKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE 2325
Cdd:PRK04863 485 iagEVSRSEAWDVARELLRRLREQRHLAEQLqqlrmrlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELE 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2326 QMAQQLAQEtqgfqktLETERQRQLEMSAEAERLRLRVAE-MSRAQA--RAEEDARRFRKQAEDigerlyrtELATQEKV 2402
Cdd:PRK04863 565 ARLESLSES-------VSEARERRMALRQQLEQLQARIQRlAARAPAwlAAQDALARLREQSGE--------EFEDSQDV 629
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 2403 M--LVQTLETQRQQSdRDAERLREAIAELEHEKDKLKQ-----EAQLLQLKS 2447
Cdd:PRK04863 630 TeyMQQLLERERELT-VERDELAARKQALDEEIERLSQpggseDPRLNALAE 680
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1451-1849 |
6.82e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.11 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1451 ALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAeaelalrvqaeAEAAREKQRALQAL---------EELRLQAEE 1521
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQ-----------LDQLKEQLQLLNKLlpqanlladETLADRLEE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1522 AERRLRQAEAERA--RQVQVALETAQRSAEAeLQSEHASFAEktaqlertLKEEHVAVVQLREEATRRAQQQAEAERARA 1599
Cdd:COG3096 898 LREELDAAQEAQAfiQQHGKALAQLEPLVAV-LQSDPEQFEQ--------LQADYLQAKEQQRRLKQQIFALSEVVQRRP 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1600 EAERELERWQLKANEALRLRLQAeevaqqksltqaeaekqkeeaerearrrgkaeeqavrQRELAEQELEKQRQLAEGTA 1679
Cdd:COG3096 969 HFSYEDAVGLLGENSDLNEKLRA-------------------------------------RLEQAEEARREAREQLRQAQ 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1680 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREA-----AAATQKRRELEAELAKVRAEmevllaskaraeeesRS 1754
Cdd:COG3096 1012 AQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQAdaeaeERARIRRDELHEELSQNRSR---------------RS 1076
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1755 TSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAK----RQRQLAEEDAVRQRAEAERVL---AEKLAAISEatrlk 1823
Cdd:COG3096 1077 QLEKQLTRCEAEmdslQKRLRKAERDYKQEREQVVQAKagwcAVLRLARDNDVERRLHRRELAylsADELRSMSD----- 1151
|
410 420
....*....|....*....|....*....
gi 1920237982 1824 tEAEIALKEKEAENERLR---RLAEDEAF 1849
Cdd:COG3096 1152 -KALGALRLAVADNEHLRdalRLSEDPRR 1179
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1456-1573 |
6.94e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 55.26 E-value: 6.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1456 AEEAEAQKRQAQEEAErLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRAlQALEELRLQAEEAERRLRQA--EAER 1533
Cdd:COG2268 212 TEIAIAQANREAEEAE-LEQEREIETARIAEAEAELA-KKKAEERREAETARA-EAEAAYEIAEANAEREVQRQleIAER 288
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1920237982 1534 ARQVQVALETAQRsAEAELQSEHASFAEktAQLERTLKEE 1573
Cdd:COG2268 289 EREIELQEKEAER-EEAELEADVRKPAE--AEKQAAEAEA 325
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2132-2573 |
7.15e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.95 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2132 RQKQAADAEMEKHKQFAEQALRqkaqvEQELTALRLQLEE--TDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRV 2209
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLD-----EEEAARQKLQLEKvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2210 QMEE-------LGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMK----------QVAEEAARLS-VAAQEAARLRQLA 2271
Cdd:pfam01576 167 NLAEeeekaksLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlegestdlqeQIAELQAQIAeLRAQLAKKEEELQ 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2272 E-----EDLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL--AQETQGFQKTLET 2344
Cdd:pfam01576 247 AalarlEEETAQKNNALKKIRELEAQISE---LQEDLESERAARNKAEKQRRDLGEELEALKTELedTLDTTAAQQELRS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2345 ERQRQLEMSAEAERLRLRVAEMSRAQARaeedaRRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLRE 2424
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMR-----QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2425 AIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQL-------------------------------------LQETQALQQ 2467
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAeklsklqselesvssllneaegkniklskdvsslesqLQDTQELLQ 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2468 SFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQekqqLAASMEEARRRQHEAEEGVRRQQEEL 2547
Cdd:pfam01576 479 EETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSD----MKKKLEEDAGTLEALEEGKKRLQREL 554
|
490 500 510
....*....|....*....|....*....|
gi 1920237982 2548 ----QRLAQQQQQQEKLlaeenQRLRERLQ 2573
Cdd:pfam01576 555 ealtQQLEEKAAAYDKL-----EKTKNRLQ 579
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1076-1738 |
7.97e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.57 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1076 EEVLRAHEEQLKE-----AQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVER 1150
Cdd:pfam01576 337 EEETRSHEAQLQEmrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1151 WRERVT-------LLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAK-QRQEQIQAvPLANSQAVReQL 1222
Cdd:pfam01576 417 LQARLSeserqraELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQeLLQEETRQ-KLNLSTRLR-QL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1223 RQEKALLEdiERHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAK-----KPKVQSGSESIIQEYVDLRTRY 1297
Cdd:pfam01576 495 EDERNSLQ--EQLEEEEEAKRNVERQ----LSTLQAQLSDMKKKLEEDAGTLEaleegKKRLQRELEALTQQLEEKAAAY 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1298 SELS-------------TLTSQYIRFISETLRR-------MEEEERLAEQQRAEERERlAEVEAALEKQRQLAEAHA--- 1354
Cdd:pfam01576 569 DKLEktknrlqqelddlLVDLDHQRQLVSNLEKkqkkfdqMLAEEKAISARYAEERDR-AEAEAREKETRALSLARAlee 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1355 --QAKAQAEREAQGLQRRMQEEVARREEV------------AVEAQEQKRSIQEE-------------------LQHLRQ 1401
Cdd:pfam01576 648 alEAKEELERTNKQLRAEMEDLVSSKDDVgknvhelerskrALEQQVEEMKTQLEeledelqatedaklrlevnMQALKA 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1402 SSEAEIQAKArqvEAAERSRLRIEEEIRVVRLQLEATERQRGGA-------EGELQALRARAEEAEAQKRQAQEEAERLR 1474
Cdd:pfam01576 728 QFERDLQARD---EQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQLKKLQ 804
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1475 RQVQDetqrkRQAEAELALRVQAEAEA-AREKQRALQALEELRLQAEE----AERRLRQAEAERAR-QVQVALETAQRSA 1548
Cdd:pfam01576 805 AQMKD-----LQRELEEARASRDEILAqSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERDElADEIASGASGKSA 879
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1549 eaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAE-----AERARAEAERELERWQL-KANEALRLRLQA 1622
Cdd:pfam01576 880 ---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQlttelAAERSTSQKSESARQQLeRQNKELKAKLQE 956
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1623 EEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQA-----VRQRELAEQEL----EKQRQLAEGTAQQRLAAEQELIRLR 1693
Cdd:pfam01576 957 MEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQaanklVRRTEKKLKEVllqvEDERRHADQYKDQAEKGNSRMKQLK 1036
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1920237982 1694 AETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEM 1738
Cdd:pfam01576 1037 RQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2777-2813 |
8.70e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 8.70e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1920237982 2777 IRLLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEM 2813
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2230-2667 |
9.69e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.36 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2230 LRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ 2309
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2310 KELAQEQARRLQEDKEQMA--QQLAQETQGFQKTLETERQRqLEMSAEAERLRLRVAEMSRAQARAEEdarrFRKQAEDI 2387
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAV-LEETQERINRARKAAPLAAHIKAVTQ----IEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2388 GERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKS---EEMQTVRQEQLLQETQA 2464
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCqqhTLTQHIHTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2465 LQQSFLSEKDSLLQRErciEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQ 2544
Cdd:TIGR00618 393 QKLQSLCKELDILQRE---QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2545 EELQRLAQQQQQQEKlLAEENQRLRERLQHLEEERRAALARSEEIAPSRAAAARALPNGQDAADGPAAAAEPEHAFDGLR 2624
Cdd:TIGR00618 470 EREQQLQTKEQIHLQ-ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1920237982 2625 RKVPA-----QRLQEVGVLSAEELQQLAQGRTTVAELAQR-----EDVRHYLQ 2667
Cdd:TIGR00618 549 HQLTSerkqrASLKEQMQEIQQSFSILTQCDNRSKEDIPNlqnitVRLQDLTE 601
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2235-2451 |
9.87e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2235 SAQRLLQEEAEKMKQVAEEAARLSVAAQEAARlrqlAEEDLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQ 2314
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKK----EEKALLKQLAALERRIAALARRIRA---LEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2315 EQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRT 2394
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237982 2395 ELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQ 2451
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4117-4145 |
1.12e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 47.71 E-value: 1.12e-06
10 20
....*....|....*....|....*....
gi 1920237982 4117 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4145
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1848-2337 |
1.14e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1848 AFQRRLLEEQAAQHKADIEARLAQLRKASESELERQkglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRg 1927
Cdd:COG4717 41 AFIRAMLLERLEKEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1928 tAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2007
Cdd:COG4717 116 -EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2008 RQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVL-ERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVE 2086
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEaAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2087 EAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQA------LRQKAQVEQ 2160
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlelldrIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2161 ELTALRLQLEETDHQKSIlDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEEL-GKLKARIEAENRALVLRDKDSAQRL 2239
Cdd:COG4717 355 EAEELEEELQLEELEQEI-AALLAEAGVEDEEELRAALEQAEEYQELKEELEELeEQLEELLGELEELLEALDEEELEEE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2240 LQEEAEKMKQVAEEAARLSVAAQEA-ARLRQLAEEDLAQQRALAEKMLKEKMQ-AVQEATRLKAEAELLQQQKELAQEqa 2317
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELeAELEQLEEDGELAELLQELEELKAELReLAEEWAALKLALELLEEAREEYRE-- 511
|
490 500
....*....|....*....|
gi 1920237982 2318 RRLQEDKEQMAQQLAQETQG 2337
Cdd:COG4717 512 ERLPPVLERASEYFSRLTDG 531
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1453-1583 |
1.20e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 54.57 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1453 RARAEEAEAQ------KRQAQEEAerlRRQVQDETQRKRQAEAELALRVQAEAEAAREKQralQALEELRLQAEEAER-- 1524
Cdd:pfam15709 337 RLRAERAEMRrleverKRREQEEQ---RRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQEEEERkq 410
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 1525 -RLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ----LERTLKEEHVAVVQLREE 1583
Cdd:pfam15709 411 rLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQrqkeLEMQLAEEQKRLMEMAEE 474
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
4-141 |
1.47e-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: 50.81 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 4 SRAIQHEISslkdERDRVqkkTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVIR 74
Cdd:cd21323 14 SEGTQHSYS----EEEKV---AFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTID-ERAINK 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237982 75 SSRLPrekgrmrFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 141
Cdd:cd21323 86 KKLTP-------FTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1316-1579 |
1.50e-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: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1316 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVeaQEQKRSIQEE 1395
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM--DEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1396 LQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1475
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEK--EEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1476 QVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEA-ERARQVQVALETAQRSAEAELQS 1554
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELkERRLAEEAEREEEEFERMLRKQA 271
|
250 260
....*....|....*....|....*
gi 1920237982 1555 EHASFAEKTAQLERTLKEEHVAVVQ 1579
Cdd:pfam13868 272 EDEEIEQEEAEKRRMKRLEHRRELE 296
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
22-142 |
1.71e-06 |
|
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: 50.83 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 22 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRLPrekgrmrFHKLQN 92
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTID-ERAINKKKLTP-------FIIQEN 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1920237982 93 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 142
Cdd:cd21325 97 LNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1652-2025 |
1.72e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.10 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1652 KAEEQAVRQRElaEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1731
Cdd:pfam02029 14 RAREERRRQKE--EEEPSGQVTESVEPNEHNSYEED--SELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1732 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRElAEEAARLRALAEEAKRQ--RQLAEEDAVRQRAEAERVL 1809
Cdd:pfam02029 90 DPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKE-EETEIREKEYQENKWSTevRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1810 AEKLAAISEatrlKTEAEIALKEKEAENERLRRLAedeafQRRLLEEQAAQhkadiearlaqlrkASESELERQKGLVED 1889
Cdd:pfam02029 169 VPTENFAKE----EVKDEKIKKEKKVKYESKVFLD-----QKRGHPEVKSQ--------------NGEEEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1890 TLRQRRQVEEEilalkgsfEKAAAGKAELELELGRIRGTAEDtlrsKEQAEQEAARQRQLAAEEERRRREAEERVQKSLA 1969
Cdd:pfam02029 226 RQGGLSQSQER--------EEEAEVFLEAEQKLEELRRRRQE----KESEEFEKLRQKQQEAELELEELKKKREERRKLL 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 1970 AEEEaaRQRKAalEEVERLKAKVEEARRLRERAEQESArqlqlaqEAAQKRLQAEE 2025
Cdd:pfam02029 294 EEEE--QRRKQ--EEAERKLREEEEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1320-1504 |
1.84e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 53.66 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1320 EEERLAEQQRAEERERLAEveAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEvaveaqEQKRSIQEELQhl 1399
Cdd:PRK09510 107 EKERLAAQEQKKQAEEAAK--QAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAA------EAKKKAEAEAA-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1400 rQSSEAEIQAKARQVEAAersrlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqvqd 1479
Cdd:PRK09510 177 -KKAAAEAKKKAEAEAAA----------------KAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA--------- 230
|
170 180
....*....|....*....|....*
gi 1920237982 1480 ETQRKRQAEAELALRVQAEAEAARE 1504
Cdd:PRK09510 231 AAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1374-2001 |
2.01e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1374 EVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ----------LEATERQRG 1443
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEvkeleelkeeIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1444 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEaEAAREKQRALQALEELRLQAEEAE 1523
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE-EYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1524 RRLRQAEAERARQVQValetaqRSAEAELQSEHASFaEKTAQLERTLKEEHVAVVQLREEatrraqqqaeaeraraeaer 1603
Cdd:PRK03918 328 ERIKELEEKEERLEEL------KKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKR-------------------- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1604 elerwqLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREarrrgkaeEQAVRQRELAEQELEKqrqlAEGTAQ--Q 1681
Cdd:PRK03918 381 ------LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL--------KKEIKELKKAIEELKK----AKGKCPvcG 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1682 RLAAEQELIRLRAEteqgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVraEMEVLLASKARAE----EESRSTSE 1757
Cdd:PRK03918 443 RELTEEHRKELLEE----------YTAELKRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLkelaEQLKELEE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1758 KSK----QRLEAEAGRFRELAEEAARLRalaeeaKRQRQLAEEdaVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEK 1833
Cdd:PRK03918 511 KLKkynlEELEKKAEEYEKLKEKLIKLK------GEIKSLKKE--LEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1834 --EAENERLRRLAEDEAFQRRLLEEQAAQHkaDIEARLAQLRKAsESELERQKGLVEDTLRQRRQVEEEILALKGSF--- 1908
Cdd:PRK03918 583 gfESVEELEERLKELEPFYNEYLELKDAEK--ELEREEKELKKL-EEELDKAFEELAETEKRLEELRKELEELEKKYsee 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1909 --EKAAAGKAELELELGRIRGTAEDTLRSKEQAEqeaarqrqlaaeeerrrreaeervqKSLAAEEEAARQRKAALEEVE 1986
Cdd:PRK03918 660 eyEELREEYLELSRELAGLRAELEELEKRREEIK-------------------------KTLEKLKEELEEREKAKKELE 714
|
650
....*....|....*
gi 1920237982 1987 RLKAKVEEARRLRER 2001
Cdd:PRK03918 715 KLEKALERVEELREK 729
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2302-2588 |
2.06e-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: 54.36 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2302 EAELLQQQKELAQEQA----RRLQEDKEQMAQQ-LAQETQgfQKTLETERQRQLEMS-----AEAERLRLRVAEMSRAQA 2371
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKavseRQQQEKFEKMEQErLRQEKE--EKAREVERRRKLEEAekarqAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2372 RAEEDARRFRKQAEDI-GERLYRTELATQ-EKVMLVQTLETQRQQSDrdaERLREAIAELEHEKDKLKQEAQLLQLKSEE 2449
Cdd:pfam17380 345 ERERELERIRQEERKReLERIRQEEIAMEiSRMRELERLQMERQQKN---ERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2450 MQTVRQEQLLQETQALQQsflsekdslLQRERCIEQEKAKLEQLfqdevakaqalreeqqRqqqqMQQEKQQLAASMEEA 2529
Cdd:pfam17380 422 MEQIRAEQEEARQREVRR---------LEEERAREMERVRLEEQ----------------E----RQQQVERLRQQEEER 472
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 2530 RRRQHEAEEGVRRQQ--EELQRLAQQQQQQEKLLAE-ENQRLRERLQHLEEERRAALARSEE 2588
Cdd:pfam17380 473 KRKKLELEKEKRDRKraEEQRRKILEKELEERKQAMiEEERKRKLLEKEMEERQKAIYEEER 534
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3436-3472 |
2.08e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 2.08e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1920237982 3436 IRLLEAQIATGGIIDPVHSHRVPVDVAYQRGYFDEEM 3472
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2141-2365 |
2.21e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2141 MEKHKQFAEQALR----QKAQVEQELTALRLQLEE--TDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEEL 2214
Cdd:COG3206 166 LELRREEARKALEfleeQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2215 GKLKARIEAENRALVlrDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEkmqAVQ 2294
Cdd:COG3206 246 RAQLGSGPDALPELL--QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS---LEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237982 2295 EATRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAQETQGFQKTLET--ERQRQLEMSAEAERLRLRVAE 2365
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPE-LEAELRRLEREVEVARELYESllQRLEEARLAEALTVGNVRVID 392
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2229-2582 |
2.21e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2229 VLRDKDSAQRLLQEEAEKmKQVAEEAARLSVAAQEAARLRQLAE------EDLAQQRALAEKMLKEKMQAVQEATRLKAE 2302
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-KEEKDLHERLNGLESELAELDEEIEryeeqrEQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2303 AELLQQQKELAQ---EQARRLQEDKEQMAQQLAQETQGFQKTLETER-------QRQLEMSAEAERLRLRVAEMSRAQAR 2372
Cdd:PRK02224 260 IEDLRETIAETErerEELAEEVRDLRERLEELEEERDDLLAEAGLDDadaeaveARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2373 AEEDARRFRKQAEDIGERlyrtelaTQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQT 2452
Cdd:PRK02224 340 HNEEAESLREDADDLEER-------AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2453 VRQEqllqetqalqqsFLSEKDSLLQRERCIEqekAKLEQLfQDEVAKAQALREE--------------QQRQQQQMQQE 2518
Cdd:PRK02224 413 FLEE------------LREERDELREREAELE---ATLRTA-RERVEEAEALLEAgkcpecgqpvegspHVETIEEDRER 476
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2519 KQQLAASMEEARRRQHEAEEGVRRQQE------ELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAA 2582
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1651-1871 |
2.56e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 53.80 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1651 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqreaaaATQKRREL 1727
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1728 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEaeagrfrelaEEAARLRALAEEAKRQRQLAEEDAVRQRAEAER 1807
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQ----------LQAAQERARQQQEEFRRKLQELQRKKQQEEAER 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 1808 VLAEKLAAISEATRLKTEAEIALkeKEAENERLRRLAE-DEAFQRRLLEEQAAQHKADIEARLAQ 1871
Cdd:pfam15709 447 AEAEKQRQKELEMQLAEEQKRLM--EMAEEERLEYQRQkQEAEEKARLEAEERRQKEEEAARLAL 509
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1316-1577 |
2.57e-06 |
|
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: 53.12 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1316 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVAR--REEVAVEAQEQKRSIQ 1393
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRAdrREKQVIEKESRWREQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1394 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqleaterqRGGAEGELQALRARAEEAEaQKRQAQEEAERL 1473
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL------------QALREQNSLQLQERLEEAC-HKRQLKEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1474 RRQVQDETQRKRQAEAELALRVQAEAEAAREK----QRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1549
Cdd:pfam15558 168 KVQENNLSELLNHQARKVLVDCQAKAEELLRRlsleQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEE 247
|
250 260
....*....|....*....|....*...
gi 1920237982 1550 AELQSEHASFAEKTAQLERTLKEEHVAV 1577
Cdd:pfam15558 248 ERQEHKEALAELADRKIQQARQVAHKTV 275
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1449-1723 |
2.74e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1449 LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRALQA--------LEELRLQAE 1520
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQelaaleaeLAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1521 EAERRLRQAEAERARQVQVALETAQRSAEAELQSehasfAEKTAQLERTLKEEHVAVVQLREEATRRAQqqaeaerarae 1600
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRA----------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1601 aerelerwQLKANEALRLRLQAEEVAQQKSLtqaeaekqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAEgtaq 1680
Cdd:COG4942 158 --------DLAELAALRAELEAERAELEALL----------------------AELEEERAALEALKAERQKLLAR---- 203
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1920237982 1681 qrlaAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQK 1723
Cdd:COG4942 204 ----LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2153-2584 |
3.25e-06 |
|
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: 53.60 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2153 RQKAQVEQELTALRLQLEETDHQ---KSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALV 2229
Cdd:pfam07111 190 KQLAEAQKEAELLRKQLSKTQEEleaQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2230 LRDKDSAQRLLQEEAEKMKQVAEEAarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAE-AELLQQ 2308
Cdd:pfam07111 270 VRVQSLTHMLALQEEELTRKIQPSD---SLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQvAELQEQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2309 QKELAQEQA--RRLQEDKEQMAQQLAQETQGFQKTL----ETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRK 2382
Cdd:pfam07111 347 VTSQSQEQAilQRALQDKAAEVEVERMSAKGLQMELsraqEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2383 QAEDIGERLYRTELATQE----------KVMLVQTLETQRQQSDRDAERLREAIAELEH---EKDKLKQEAQL-LQLKSE 2448
Cdd:pfam07111 427 AVARIPSLSNRLSYAVRKvhtikglmarKVALAQLRQESCPPPPPAPPVDADLSLELEQlreERNRLDAELQLsAHLIQQ 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2449 EMQTVRQE-------------QLLQETQALQQSFLS---EKDSLLQRERCIEQEKAKLEQ-LFQDEVAKAQALREEQQRQ 2511
Cdd:pfam07111 507 EVGRAREQgeaerqqlsevaqQLEQELQRAQESLASvgqQLEVARQGQQESTEEAASLRQeLTQQQEIYGQALQEKVAEV 586
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237982 2512 QQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQ----EELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALA 2584
Cdd:pfam07111 587 ETRLREQLSDTKRRLNEARREQAKAVVSLRQIQhratQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNLMLA 663
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2238-2486 |
3.30e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 53.90 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2238 RLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ-EATRLKA---EAELLQQQKELA 2313
Cdd:PRK10929 123 RQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQaESAALKAlvdELELAQLSANNR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2314 QEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAE-AERLRLRVAEMSRAQARA----EEDARRFRKQAEDIG 2388
Cdd:PRK10929 203 QELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDLPKSIVAQfkinRELSQALNQQAQRMD 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2389 ERLYRTELATQEKVMLVQTLETQRQQ------SDRDAERLREAIAELEhEKDKLKQ----EAQLL--QLKSEEMQTvRQE 2456
Cdd:PRK10929 283 LIASQQRQAASQTLQVRQALNTLREQsqwlgvSNALGEALRAQVARLP-EMPKPQQldteMAQLRvqRLRYEDLLN-KQP 360
|
250 260 270
....*....|....*....|....*....|
gi 1920237982 2457 QLLQETQALQQSFLSEKDSLLQRERCIEQE 2486
Cdd:PRK10929 361 QLRQIRQADGQPLTAEQNRILDAQLRTQRE 390
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1346-1474 |
3.32e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 52.74 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1346 QRQLAEAHAQ-AKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKArQVEAAERSRLRI 1424
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ-ELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1425 EEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLR 1474
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2180-2385 |
3.34e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2180 DEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVlRDKDSAQRLLQEEAEKMKQVAEEAARLSV 2259
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2260 AAQEAARLRQLAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2331
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 2332 AQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAE 2385
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1383-2218 |
3.37e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.90 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1383 VEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAersrLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1462
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKA----CEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHN 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1463 KRQAQEEAERLRRQVQDETQRKRQaEAELALRVQAEAEAAREKqraLQALEELR-LQAEEAERRLRQAEAERARQVQVAL 1541
Cdd:TIGR00606 261 LSKIMKLDNEIKALKSRKKQMEKD-NSELELKMEKVFQGTDEQ---LNDLYHNHqRTVREKERELVDCQRELEKLNKERR 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1542 ETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRL--R 1619
Cdd:TIGR00606 337 LLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLcaD 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1620 LQAEEVAQQKSLTQAEAEKQKEEAEREArrrgKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG 1699
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTIEL----KKEILEKKQEEL--KFVIKELQQLEGSSDRILELDQELRKAERELSKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1700 EQQR--QLLEEELARLQREAAAATQKRRELEAELAKV------RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFR 1771
Cdd:TIGR00606 491 EKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFP 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1772 ELAEEAARLRALAEEAKRQRQ-LAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEI----ALKEKEAENERLRRLAED 1846
Cdd:TIGR00606 571 NKKQLEDWLHSKSKEINQTRDrLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcGSQDEESDLERLKEEIEK 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1847 EAFQRRLLEEQAAQHKADIEAR---------LAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKaaagkaE 1917
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQLtdenqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEK------R 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1918 LELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRR--EAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEA 1995
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNdiEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDV 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1996 RRLRERAEQESaRQLQLAQEAAQKRLQAEEKAHAF-AVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERA 2074
Cdd:TIGR00606 805 ERKIAQQAAKL-QGSDLDRTVQQVNQEKQEKQHELdTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2075 EREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKL----------RKEAEQEAARRAQAEQAALRQKQAADAEMEKH 2144
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDqqekeelissKETSNKKAQDKVNDIKEKVKNIHGYMKDIENK 963
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 2145 KQfaEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVtEAARQRGQVEEELFSLRVQMEELGKLK 2218
Cdd:TIGR00606 964 IQ--DGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDI-DTQKIQERWLQDNLTLRKRENELKEVE 1034
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2236-2563 |
3.46e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 52.61 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2236 AQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2315
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2316 QARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERlrlRVAEMSRAQARAEEDARRFRKQAEDIGERLYrte 2395
Cdd:pfam13868 113 EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE---RILEYLKEKAEREEEREAEREEIEEEKEREI--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2396 latqeKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEaqllqlksEEMQTVRQEQLLQETQALQQSFLSEKDS 2475
Cdd:pfam13868 187 -----ARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKERE--------EAEKKARQRQELQQAREEQIELKERRLA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2476 LLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQ 2555
Cdd:pfam13868 254 EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEE 333
|
....*...
gi 1920237982 2556 QQEKLLAE 2563
Cdd:pfam13868 334 ERQKKLKE 341
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1217-1949 |
3.58e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.57 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1217 AVREQLRQEKALLEDierhGEKVEECQRFAKQyinaikdyELQLVTYKAQLepvaspakkpKVQSGsesiIQEYVDLRTR 1296
Cdd:pfam05483 96 SIEAELKQKENKLQE----NRKIIEAQRKAIQ--------ELQFENEKVSL----------KLEEE----IQENKDLIKE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1297 yselSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAEREAQGLQRRMQEEva 1376
Cdd:pfam05483 150 ----NNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEK---MILAFEELRVQAENARLEMHFKLKED-- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1377 rreevaveaqeqkrsiQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1456
Cdd:pfam05483 221 ----------------HEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1457 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELR----LQAEEAERRLRQAEaE 1532
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKaahsFVVTEFEATTCSLE-E 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1533 RARQVQVALEtaqrSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATrraqqqaeaerarAEAERELERWQLKA 1612
Cdd:pfam05483 364 LLRTEQQRLE----KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKK-------------ILAEDEKLLDEKKQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1613 NEALRLRLQAEEvaQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQR-QLAEGTAQ--------QRL 1683
Cdd:pfam05483 427 FEKIAEELKGKE--QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTAHcdklllenKEL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1684 AAEQE--LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA---ELAKVRAEMEVLL---ASKARAEEESRST 1755
Cdd:pfam05483 505 TQEASdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESvreEFIQKGDEVKCKLdksEENARSIEYEVLK 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1756 SEKSKQRLEAEAGRFRELAEEAAR-LRALAEEAKRQRQlaEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKE 1834
Cdd:pfam05483 585 KEKQMKILENKCNNLKKQIENKNKnIEELHQENKALKK--KGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1835 AENERL--RRLAEdEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRrqvEEEILALKGSFEKAA 1912
Cdd:pfam05483 663 IEDKKIseEKLLE-EVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSELGLYKNKEQEQS 738
|
730 740 750
....*....|....*....|....*....|....*..
gi 1920237982 1913 AGKAELELELGRIRGtaeDTLRSKEQAEQEAARQRQL 1949
Cdd:pfam05483 739 SAKAALEIELSNIKA---ELLSLKKQLEIEKEEKEKL 772
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2141-2444 |
3.59e-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: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2141 MEKHKQFAEQALRQKAQVEQELTAlrlQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKAR 2220
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2221 IEAENRALvlrdKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAarlRQLAEE--DLAQQRALaekmLKEKMQavqeatr 2298
Cdd:TIGR04523 466 LETQLKVL----SRSINKIKQNLEQKQKELKSKEKELKKLNEEK---KELEEKvkDLTKKISS----LKEKIE------- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2299 lKAEAELLQQQKELAQeqarrLQEDKEQMAQQLAQETqgfqktLETERQRQLEmsaEAERLRLRVAEMSRAQARAEEDAR 2378
Cdd:TIGR04523 528 -KLESEKKEKESKISD-----LEDELNKDDFELKKEN------LEKEIDEKNK---EIEELKQTQKSLKKKQEEKQELID 592
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 2379 RFRKQAEDIGERLyrtelatQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQ 2444
Cdd:TIGR04523 593 QKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1319-1484 |
3.68e-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: 52.54 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1319 EEEERLAEQQRAEERERLAEVEAAleKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQH 1398
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1399 LRQSSEAEIQAKARQVEA-AERSRLRIEEEI----RVVRLQLEATERQRGGAEGELQALRARAEEAEAQK------RQAQ 1467
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAkAEAAKAKAAAEAaakaEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAG 258
|
170
....*....|....*..
gi 1920237982 1468 EEAERLRRQVQDETQRK 1484
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQN 275
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1862-2580 |
3.72e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.69 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1862 KADIEARLAQlRKASESELERQKGLVEDTLRQRrQVEEEILALKGSFEKAAAG-----KAELELELGRIRGTAEDTLRSK 1936
Cdd:pfam12128 199 KSMIVAILED-DGVVPPKSRLNRQQVEHWIRDI-QAIAGIMKIRPEFTKLQQEfntleSAELRLSHLHFGYKSDETLIAS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1937 EQAEQEA--ARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQ 2014
Cdd:pfam12128 277 RQEERQEtsAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSEL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2015 EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQS 2094
Cdd:pfam12128 357 ENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2095 AEEQAQaqaqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDh 2174
Cdd:pfam12128 437 EEEYRL----------KSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQAS- 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2175 qksildEELQRLKAEVTEAARQRGQVEEELFS--------LRVQM----EELGKLKARieaenrALVLR-------DKDS 2235
Cdd:pfam12128 506 ------EALRQASRRLEERQSALDELELQLFPqagtllhfLRKEApdweQSIGKVISP------ELLHRtdldpevWDGS 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2236 AQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2315
Cdd:pfam12128 574 VGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARL 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2316 QARRLQEDKEQMAQQLAQETQGFQKTLETERQrqlEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQA--EDIGERLYR 2393
Cdd:pfam12128 654 DLRRLFDEKQSEKDKKNKALAERKDSANERLN---SLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYwqVVEGALDAQ 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2394 TELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEqLLQETQALQQSFLSEK 2473
Cdd:pfam12128 731 LALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQE-VLRYFDWYQETWLQRR 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2474 DSLLQRERCIEQEKAKLEQlfqdevakaqalreEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQ 2553
Cdd:pfam12128 810 PRLATQLSNIERAISELQQ--------------QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATL 875
|
730 740
....*....|....*....|....*..
gi 1920237982 2554 QQQQEKllAEENQRLRERLQHLEEERR 2580
Cdd:pfam12128 876 KEDANS--EQAQGSIGERLAQLEDLKL 900
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1300-1555 |
4.31e-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: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1300 LSTLTSQYIRFISEtLRRMEEEERLA--EQQRAEERERLAEVEAALEKQRQlaeahAQAKAQAEREAQGLQRRMQEEVAR 1377
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1378 ReevaVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRieEEIRVVRLQLEATERQRGGAEGELQALRARAE 1457
Cdd:COG3206 228 L----AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLR--AQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1458 EAEAQKRQaqeEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAeaeRARQV 1537
Cdd:COG3206 302 ALRAQLQQ---EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL---LQRLE 375
|
250
....*....|....*...
gi 1920237982 1538 QVALETAQRSAEAELQSE 1555
Cdd:COG3206 376 EARLAEALTVGNVRVIDP 393
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1336-1430 |
4.36e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 53.42 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1336 LAEVEAALEKQRQLAEAHAQAKAQAEREAqglqRRMQEEVARREEVAVEAQEQKRSIQEELQHLR-QSSEAEIQAKARQV 1414
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALA----EAQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 1920237982 1415 EAAERSRLRI---EEEIRV 1430
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3695-3730 |
4.47e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.94 E-value: 4.47e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1920237982 3695 RQLLEAQAATGFLLDPVKGERLAVDEAVRKGLVGPE 3730
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1405-1584 |
4.50e-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: 52.16 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1405 AEIQAKARQVEAAERSRLRIEEEirvvrlQLEATERQRGGAEGELQALRARAEEAEAqKRQAQEEAERLRRQVQDETQRK 1484
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQ------QAEEAEKQRAAEQARQKELEQRAAAEKA-AKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1485 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTA 1564
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKA 205
|
170 180
....*....|....*....|
gi 1920237982 1565 QLERTLKEEHVAVVQLREEA 1584
Cdd:TIGR02794 206 AAEAAAKAEAEAAAAAAAEA 225
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2133-2318 |
4.60e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.11 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2133 QKQAADAEMEKHKQFAEQALRQKAQvEQELTALRLQLEETDHQKSILDEELQRLKAEVTeaarqrgQVEEELFSLRVQME 2212
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSIK-------QVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2213 ELGK---LKARI-----EAENRALVLrdkdsaQRLLQEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEEDLAQQRALA 2282
Cdd:pfam05667 381 ELEKqykVKKKTldllpDAEENIAKL------QALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLE 454
|
170 180 190
....*....|....*....|....*....|....*....
gi 1920237982 2283 E-KMLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2318
Cdd:pfam05667 455 EiKELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2133-2317 |
4.84e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2133 QKQAADAEMEKHKQFAEQA--LRQKAQVEQEltalRLQLEETDHQKSildeelQRLKAEVTEAARQRGQVEEELFSLRVQ 2210
Cdd:PRK09510 71 QKSAKRAEEQRKKKEQQQAeeLQQKQAAEQE----RLKQLEKERLAA------QEQKKQAEEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2211 MEELGKLKARIEAEN-RALVLRDKDSAQRLLQEEAEK-----MKQVAEEAARLSVAAQEAARLRQLAEE---DLAQQRAL 2281
Cdd:PRK09510 141 AAAAAKAKAEAEAKRaAAAAKKAAAEAKKKAEAEAAKkaaaeAKKKAEAEAAAKAAAEAKKKAEAEAKKkaaAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|....*.
gi 1920237982 2282 AEKmlKEKMQAVQEATRLKAEAELLQQQKELAQEQA 2317
Cdd:PRK09510 221 AEA--KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAK 254
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1657-2399 |
5.09e-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: 53.03 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1657 AVRQRELAEQELEKQRQLAeGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE-------LARLQrEAAAATQKrrelea 1729
Cdd:COG3096 277 ANERRELSERALELRRELF-GARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhLNLVQ-TALRQQEK------ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1730 eLAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAEAgRFRELAEEAARLRAlaEEAKRQRQLaeeDAVRQRAEAERvl 1809
Cdd:COG3096 349 -IERYQEDLEEL---TERLEEQEEVVEEAAEQLAEAEA-RLEAAEEEVDSLKS--QLADYQQAL---DVQQTRAIQYQ-- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1810 aEKLAAISEATRLKTEAEIALKEKEAENERLRRlAEDEAFQRRLleeQAAQHKADIEARLAQLRKAseseLERQKGLVED 1889
Cdd:COG3096 417 -QAVQALEKARALCGLPDLTPENAEDYLAAFRA-KEQQATEEVL---ELEQKLSVADAARRQFEKA----YELVCKIAGE 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1890 TLRQRR-QVEEEILALKGSFEKAAAGKAELELELGrirgtaedtlrskeQAEQEAARQRQLAAEEERRRREAEERVQKSL 1968
Cdd:COG3096 488 VERSQAwQTARELLRRYRSQQALAQRLQQLRAQLA--------------ELEQRLRQQQNAERLLEEFCQRIGQQLDAAE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1969 AAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEA-----AQKRLQ--AEEKAHAFAVQQkeqelqQ 2041
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawlaAQDALErlREQSGEALADSQ------E 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2042 TLQQEQSVLERLRseaeaarraaeeaeaareraerEAAQSRRQVEEAERlkqsaeeqaqaqaqaqaaaeklrkeaeqeaa 2121
Cdd:COG3096 628 VTAAMQQLLERER----------------------EATVERDELAARKQ------------------------------- 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2122 rraQAEQAALRQKQAADAEMEKHKQFAEQ----------------------AL--------------------------- 2152
Cdd:COG3096 655 ---ALESQIERLSQPGGAEDPRLLALAERlggvllseiyddvtledapyfsALygparhaivvpdlsavkeqlagledcp 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2153 ---------------------------------RQ-------------KAQVEQELTALRLQLEETD---HQKSILDEEL 2183
Cdd:COG3096 732 edlyliegdpdsfddsvfdaeeledavvvklsdRQwrysrfpevplfgRAAREKRLEELRAERDELAeqyAKASFDVQKL 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2184 QRL--------------------KAEVTEAARQRGQVEEELFSLRVQM----EELGKLKARIEAENRAL----VLRDKDS 2235
Cdd:COG3096 812 QRLhqafsqfvgghlavafapdpEAELAALRQRRSELERELAQHRAQEqqlrQQLDQLKEQLQLLNKLLpqanLLADETL 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2236 AQRL--LQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAekmlKEKMQAVQEATRLKAEA---------- 2303
Cdd:COG3096 892 ADRLeeLREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQ----ADYLQAKEQQRRLKQQIfalsevvqrr 967
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2304 -------------------ELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQkTLETERQRQLEMSAEAERlrlRVA 2364
Cdd:COG3096 968 phfsyedavgllgensdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLA-SLKSSRDAKQQTLQELEQ---ELE 1043
|
890 900 910
....*....|....*....|....*....|....*...
gi 1920237982 2365 EMS-RAQARAEEDA--RRFRKQAEDIGERLYRTELATQ 2399
Cdd:COG3096 1044 ELGvQADAEAEERAriRRDELHEELSQNRSRRSQLEKQ 1081
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2181-2589 |
5.32e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2181 EELQRLKAEVteAARQRGQVEEELFSLRVQMEELGKLKARIEaENRALVLRDKDSAQRLLQEEAEKMKQ---VAEEAARL 2257
Cdd:PRK02224 187 GSLDQLKAQI--EEKEEKDLHERLNGLESELAELDEEIERYE-EQREQARETRDEADEVLEEHEERREEletLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2258 SVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaqetQG 2337
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA----QA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2338 FQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLyrtelatqekvmlvQTLETQRQQSDR 2417
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI--------------EELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2418 DAERLREAIAELEHEKDKLKQEAQLLQ--LKSEEMQTVRQEQLLQE------TQALQQSflSEKDSLLQRERCIEQEKAK 2489
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEatLRTARERVEEAEALLEAgkcpecGQPVEGS--PHVETIEEDRERVEELEAE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2490 LEQL------FQDEVAKAQALREEQQR--QQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLL 2561
Cdd:PRK02224 484 LEDLeeeveeVEERLERAEDLVEAEDRieRLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
410 420 430
....*....|....*....|....*....|....
gi 1920237982 2562 AEENQRLRERLQHLEE------ERRAALARSEEI 2589
Cdd:PRK02224 564 EEEAEEAREEVAELNSklaelkERIESLERIRTL 597
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1313-1546 |
5.39e-06 |
|
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: 51.96 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1313 ETLRRMEEEERLAEQQRAEERERLA--EVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEvavEAQEQKR 1390
Cdd:pfam15558 51 ERRLLLQQSQEQWQAEKEQRKARLGreERRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQ---RKQCQEQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1391 SIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEA------EAQKR 1464
Cdd:pfam15558 128 RLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELlrrlslEQSLQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1465 QAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ----RALQALEELRL-QAEEAERRLRQAEAERARQVQV 1539
Cdd:pfam15558 208 RSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERqehkEALAELADRKIqQARQVAHKTVQDKAQRARELNL 287
|
....*..
gi 1920237982 1540 ALETAQR 1546
Cdd:pfam15558 288 EREKNHH 294
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3900-3937 |
5.71e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.94 E-value: 5.71e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1920237982 3900 QRFLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTA 3937
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
144-251 |
5.83e-06 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 48.26 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 144 QSEDMTAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGV 222
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 1920237982 223 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 251
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1751-2592 |
5.96e-06 |
|
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: 52.81 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1751 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIAL 1830
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1831 KEKEAENERlrrlAEDEAFQRRLLEEQAAQHkaDIEARLAQLRKASESELERQKGLVEDTLRQR--------RQVEEEIL 1902
Cdd:pfam15921 161 KEDMLEDSN----TQIEQLRKMMLSHEGVLQ--EIRSILVDFEEASGKKIYEHDSMSTMHFRSLgsaiskilRELDTEIS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1903 ALKGSF----EKAAAGKAELELELGRIRGTAEDTLrskEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQR 1978
Cdd:pfam15921 235 YLKGRIfpveDQLEALKSESQNKIELLLQQHQDRI---EQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1979 KAA----LEEVE----RLKAKVEEARRLRERAEQESARQLQLAQ----EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQE 2046
Cdd:pfam15921 312 NSMymrqLSDLEstvsQLRSELREAKRMYEDKIEELEKQLVLANseltEARTERDQFSQESGNLDDQLQKLLADLHKREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2047 QSVLERlrseaeaarraaeeaeaareraereaAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2126
Cdd:pfam15921 392 ELSLEK--------------------------EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2127 EQAALRQKQAADAEMEKHKQFAEQALRQKA---QVEQELTALRLQLEETDHQKSILDEELQR----LKAEVTEAARQRGQ 2199
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEmlrKVVEELTAKKMTLESSERTVSDLTASLQEkeraIEATNAEITKLRSR 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2200 VE---EELFSLRVQMEELGKLKAriEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQ-EAArlrQLAEEDL 2275
Cdd:pfam15921 526 VDlklQELQHLKNEGDHLRNVQT--ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKA---QLEKEIN 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2276 AQQRALAE-KMLKEKMQAvqEATRLKAEAELLQQQK-ELAQEQARRLQEDKEqmaqqLAQETQGFQKTLETERQRQLEMS 2353
Cdd:pfam15921 601 DRRLELQEfKILKDKKDA--KIRELEARVSDLELEKvKLVNAGSERLRAVKD-----IKQERDQLLNEVKTSRNELNSLS 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2354 AEAERLRlrvaemsraqaraeedaRRFRKQAEDIGERLYRTELATQE-KVMLVQTLETQRQQSDRDAERLREA------I 2426
Cdd:pfam15921 674 EDYEVLK-----------------RNFRNKSEEMETTTNKLKMQLKSaQSELEQTRNTLKSMEGSDGHAMKVAmgmqkqI 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2427 AELEHEKDKLKQEAQLLQlksEEMQTVRQEQ-LLQEtqalqqsflsEKDSLLQRERCIEQEKAKLEQlfQDEVAKAQALR 2505
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLE---EAMTNANKEKhFLKE----------EKNKLSQELSTVATEKNKMAG--ELEVLRSQERR 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2506 eeqqrqqqqMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLA----EENQRLRERLQhleeeRRA 2581
Cdd:pfam15921 802 ---------LKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQgpgyTSNSSMKPRLL-----QPA 867
|
890
....*....|.
gi 1920237982 2582 ALARSEEIAPS 2592
Cdd:pfam15921 868 SFTRTHSNVPS 878
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
17-137 |
6.03e-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: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 17 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSSRLPREKGRMRfhKLQNVQIA 96
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMTR---VPVDWGHVNKPPYPALGGNMK--KIENCNYA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237982 97 LDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 137
Cdd:cd21329 75 VELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1354-1576 |
6.18e-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: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1354 AQAKAQAEREAQGLQ---RRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKArqveaAERSRLRIEEEIRV 1430
Cdd:TIGR02794 46 GAVAQQANRIQQQKKpaaKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1431 vrlQLEATERQRggaegelqALRARAEEAEAqKRQAQEEAerlRRQVQDETQRKRQAEAelalrvQAEAEAAREKQRAL- 1509
Cdd:TIGR02794 121 ---AEEAKAKQA--------AEAKAKAEAEA-ERKAKEEA---AKQAEEEAKAKAAAEA------KKKAEEAKKKAEAEa 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 1510 --QALEELRLQAEEAERRLRQAE----------AERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVA 1576
Cdd:TIGR02794 180 kaKAEAEAKAKAEEAKAKAEAAKakaaaeaaakAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2131-2577 |
7.81e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2131 LRQKQAADAEMEKHKQFAEQALRQ-----KAQVEQELTA---LRLQLEETDHQKSI-LDEELQRLKAEVTEAARQRGQVE 2201
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQvymdlNNNIEKMILAfeeLRVQAENARLEMHFkLKEDHEKIQHLEEEYKKEINDKE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2202 EELFSLRVQM-EELGKLKARI----EAENRALVLRDKDSAQ-RLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDL 2275
Cdd:pfam05483 240 KQVSLLLIQItEKENKMKDLTflleESRDKANQLEEKTKLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2276 AQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ--------KELAQEQARRLQEDKEQMaQQLAQETQgfQKTLETERQ 2347
Cdd:pfam05483 320 QIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeattcslEELLRTEQQRLEKNEDQL-KIITMELQ--KKSSELEEM 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2348 RQLEMSAEAERLRLRVAeMSRAQARAEEdarrfRKQAEDIGERLYRTElatQEKVMLVQTLETQRQQSDRDAERLREAIA 2427
Cdd:pfam05483 397 TKFKNNKEVELEELKKI-LAEDEKLLDE-----KKQFEKIAEELKGKE---QELIFLLQAREKEIHDLEIQLTAIKTSEE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2428 ELEHEKDKLKQEAQLLQLKSEEMqTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQdevaKAQALREE 2507
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIEL-TAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK----QIENLEEK 542
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2508 QQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEE 2577
Cdd:pfam05483 543 EMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1651-1933 |
8.40e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1651 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAE 1730
Cdd:COG4372 23 GILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1731 LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQ----LAEEDAVRQRAEAE 1806
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEelaaLEQELQALSEAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1807 RVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGL 1886
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1920237982 1887 VEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTL 1933
Cdd:COG4372 263 LELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2159-2588 |
8.73e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.48 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2159 EQELTALRLQLEETDHQKSILDEElQRLKAEvtEAARQRGQVEeelfslRVQMEelGKLKariEAENRALVLRDKDSaqR 2238
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLE-EQLDEE--EAARQKLQLE------KVTTE--AKIK---KLEEDILLLEDQNS--K 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2239 LLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE-KMQAVQEATRLKAEAELLQqqkelAQEQA 2317
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEeKGRQELEKAKRKLEGESTD-----LQEQI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2318 RRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQA--RAEEDAR-RFRKQAEDIGERL--Y 2392
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEdlESERAARnKAEKQRRDLGEELeaL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2393 RTELA-TQEKVMLVQTLETQRQQsdrDAERLREAIaelehEKDKLKQEAQLLQLKSEEMQTVR--QEQLLQ--------- 2460
Cdd:pfam01576 305 KTELEdTLDTTAAQQELRSKREQ---EVTELKKAL-----EEETRSHEAQLQEMRQKHTQALEelTEQLEQakrnkanle 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2461 -ETQALQQSFL---SEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQalreEQQRQQQQMQQEKQQLAASMEEARRRQHEA 2536
Cdd:pfam01576 377 kAKQALESENAelqAELRTLQQAKQDSEHKRKKLEGQLQELQARLS----ESERQRAELAEKLSKLQSELESVSSLLNEA 452
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 2537 EEGVRRQQEELQRLAQQQQQQEKLLAEENQR---LRERLQHLEEERRAALARSEE 2588
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQEETRQklnLSTRLRQLEDERNSLQEQLEE 507
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2290-2435 |
9.02e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 52.33 E-value: 9.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2290 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQ-QLAQetQGFQKTLETERQRQLEMSAEAERLR 2360
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARgRLER--QKMHDKAKAEEQRTKLLELQAESAA 710
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 2361 LRVAEMSRAQARAEEDARRFRKQAEdigerLYRTEL-ATQEKVMLVQTLETQRQQSDRDAERlREAIAELEHEKDK 2435
Cdd:PTZ00491 711 VESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1278-1492 |
9.03e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1278 KVQSGSESIIQEYVDLRTRYSELSTL---TSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA-- 1352
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLal 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1353 --HAQAKAQAEREAQGLQRRMQeevARREEVaveaqEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIrv 1430
Cdd:COG4942 125 llSPEDFLDAVRRLQYLKYLAP---ARREQA-----EELRADLAELAALRAELEAERAELEALLAELEEERAALEALK-- 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 1431 vrlqleaTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1492
Cdd:COG4942 195 -------AERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1499-2030 |
9.29e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1499 AEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQV--ALETAQRSAEAELQS------EHASFAEKTAQLERTL 1570
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKlekevkELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1571 KEEHVAVVQLRE---EATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREA 1647
Cdd:PRK03918 248 ESLEGSKRKLEEkirELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1648 RRRGKAEEQAVRQRELAEQELEKQRQLAE--------GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR--LQREA 1717
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEEleerhelyEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKeeIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1718 AAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR-FRELAEEAARLRALAEEAKRQ-RQLAE 1795
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAeLKRIEKELKEIEEKERKLRKElRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1796 EDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERlRRLAEDEAFQRRLLEEqaAQHKADIEARLAQLRKA 1875
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLK-EKLIKLKGEIKSLKKE--LEKLEELKKKLAELEKK 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1876 SEsELERQKGLVEDTLRQR-----RQVEEEILALKGSFEK---AAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQR 1947
Cdd:PRK03918 565 LD-ELEEELAELLKELEELgfesvEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1948 QLAAEEERRrreaeervqKSLAAEEEAARQRKAALE---EVERLKAKVEEARRLRERAEQ--ESARQLQLAQEAAQKRLQ 2022
Cdd:PRK03918 644 ELRKELEEL---------EKKYSEEEYEELREEYLElsrELAGLRAELEELEKRREEIKKtlEKLKEELEEREKAKKELE 714
|
....*...
gi 1920237982 2023 AEEKAHAF 2030
Cdd:PRK03918 715 KLEKALER 722
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1201-1520 |
9.39e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.36 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1201 KQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQ 1280
Cdd:PRK10929 29 TQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLER-------AKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1281 SGSESIIQEYVDLRTRYSELSTLTSQ---YIRFISETLRRMEeeerlaeQQRAEERERLAEVEAALEKQRQLAEAHAQAK 1357
Cdd:PRK10929 102 MSTDALEQEILQVSSQLLEKSRQAQQeqdRAREISDSLSQLP-------QQQTEARRQLNEIERRLQTLGTPNTPLAQAQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1358 AQAereaqglqrrMQEEVARReevaveaqeqkRSIQEELQhLRQSSEAEIQAKAR-QVEAAERSRLRIEEEIRVVRLQLE 1436
Cdd:PRK10929 175 LTA----------LQAESAAL-----------KALVDELE-LAQLSANNRQELARlRSELAKKRSQQLDAYLQALRNQLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1437 aTERQRggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQ-------AEAEAAREKQRAL 1509
Cdd:PRK10929 233 -SQRQR------------EAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQrmdliasQQRQAASQTLQVR 299
|
330
....*....|.
gi 1920237982 1510 QALEELRLQAE 1520
Cdd:PRK10929 300 QALNTLREQSQ 310
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3902-3940 |
9.91e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.01 E-value: 9.91e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1920237982 3902 FLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTAFEL 3940
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1328-2032 |
1.14e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.11 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1328 QRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER-EAQGlqrrmqeevarrEEVAVEAQEQKRSIQEELQHLRQsseae 1406
Cdd:PRK10246 168 ERAELLEELTGTEIYGQISAMVFEQHKSARTELEKlQAQA------------SGVALLTPEQVQSLTASLQVLTD----- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1407 iqakarqveaaersrlriEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqvQDETQRKRQ 1486
Cdd:PRK10246 231 ------------------EEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKA-------QPQLAALSL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1487 AEAELALRVQAEaeaarEKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQrsaeaELQSEHASFAEKTAql 1566
Cdd:PRK10246 286 AQPARQLRPHWE-----RIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSA-----ELQAQQQSLNTWLA-- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1567 ertlkeEHVAVVQLREE-----ATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLtqaeaekqke 1641
Cdd:PRK10246 354 ------EHDRFRQWNNElagwrAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQ---------- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1642 eaerearrrgKAEEQAVRQR--ELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLqREAAA 1719
Cdd:PRK10246 418 ----------HAEQRPLRQRlvALHGQIVPQQKRLAQ-LQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADV-KTICE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1720 ATQKRRELEAELAKVRAEMEVLL--ASKARAEEESRS-TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1796
Cdd:PRK10246 486 QEARIKDLEAQRAQLQAGQPCPLcgSTSHPAVEAYQAlEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDES 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1797 DAvRQRAEAERVLAEKLAAISEA--TRLKTEAEIA--LKEKEAENERLRRLAEDEAFQRRLLE--EQAAQHKADIEARLA 1870
Cdd:PRK10246 566 EA-QSLRQEEQALTQQWQAVCASlnITLQPQDDIQpwLDAQEEHERQLRLLSQRHELQGQIAAhnQQIIQYQQQIEQRQQ 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1871 QLR----------------------KASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGT 1928
Cdd:PRK10246 645 QLLtalagyaltlpqedeeaswlatRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHE 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1929 AEDTLRSK-----EQAEQEAARQRQLAAEEERRRREAEERVQKSLAAE--EEAARQRKAALEevERLKAKVEEARRLRER 2001
Cdd:PRK10246 725 QCLSLHSQlqtlqQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAAllDEETLTQLEQLK--QNLENQRQQAQTLVTQ 802
|
730 740 750
....*....|....*....|....*....|.
gi 1920237982 2002 AEQESARQLQLAQEAAQKRLQAEEKAHAFAV 2032
Cdd:PRK10246 803 TAQALAQHQQHRPDGLDLTVTVEQIQQELAQ 833
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2248-2464 |
1.16e-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: 51.00 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2248 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2327
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2328 AQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKvmlvQT 2407
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AA 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237982 2408 LETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQA 2464
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
22-141 |
1.27e-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: 48.08 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 22 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRLPrekgrmrFHKLQN 92
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTID-ERTINKKKLTP-------FTIQEN 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1920237982 93 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 141
Cdd:cd21324 97 LNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1714-2035 |
1.36e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.66 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1714 QREAAAATQKRRELEAELAKVRAEMEvllaSKARAEEESRSTSEKSKQRlEAEAGRFRELAEEAARLralaeEAKRQRQL 1793
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKE----EKAREVERRRKLEEAEKAR-QAEMDRQAAIYAEQERM-----AMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1794 AEEDAVRQRAEAERVLAEKLAAisEATRLKtEAEIALKEKEAENERLRRLAEdEAFQRRLLEEQAAQHKADIEARLAQLR 1873
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAM--EISRMR-ELERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1874 KASESELERQ-KGLVEDTLRQRRQVEEEilalkgsfekaaagKAELELELGRIRGTAEDTLRSKEQAEQEaaRQRQLAAE 1952
Cdd:pfam17380 427 AEQEEARQREvRRLEEERAREMERVRLE--------------EQERQQQVERLRQQEEERKRKKLELEKE--KRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1953 EERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARrlRERAEQESARQLQLAQE---AAQKRLQAEEKAHA 2029
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER--RREAEEERRKQQEMEERrriQEQMRKATEERSRL 568
|
....*.
gi 1920237982 2030 FAVQQK 2035
Cdd:pfam17380 569 EAMERE 574
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2411-2600 |
1.44e-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: 50.92 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2411 QRQQSDRDAERLREAIAELEHEKDKLKQEAQLL--QLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKA 2488
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALlkQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2489 KLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASME------EARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLA 2562
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 1920237982 2563 EENQRLRERLQHLEEERRAALARSEEIAPSRAAAARAL 2600
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1793-2493 |
1.48e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.59 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1793 LAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKAdiEARLAQL 1872
Cdd:TIGR00606 165 LSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLES--SREIVKS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1873 RKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQlaae 1952
Cdd:TIGR00606 243 YENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKE---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1953 eerrrrEAEERVQKSLAAEEEAAR---QRKAALE-EVERLKAKVE---EARRLRERAEQESARQLQLAQEAAQKRLQAEE 2025
Cdd:TIGR00606 319 ------RELVDCQRELEKLNKERRllnQEKTELLvEQGRLQLQADrhqEHIRARDSLIQSLATRLELDGFERGPFSERQI 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2026 K-AHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQ 2104
Cdd:TIGR00606 393 KnFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2105 AQAAAEKLRKEAE---------------QEAARRAQAEQAALRQKQAADAEME----------------KHKQFAEQALR 2153
Cdd:TIGR00606 473 ILELDQELRKAERelskaeknsltetlkKEVKSLQNEKADLDRKLRKLDQEMEqlnhhtttrtqmemltKDKMDKDEQIR 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2154 Q-KAQVEQELTAL------RLQLEETDHQKS----ILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGklkariE 2222
Cdd:TIGR00606 553 KiKSRHSDELTSLlgyfpnKKQLEDWLHSKSkeinQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYE------D 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2223 AENRALVLRDKDSAQRLLQEEAEKM-KQVAEEAARLSVAAQeaaRLRQLAEED-----LAQQRALAEKMLKEKMQAVQEA 2296
Cdd:TIGR00606 627 KLFDVCGSQDEESDLERLKEEIEKSsKQRAMLAGATAVYSQ---FITQLTDENqsccpVCQRVFQTEAELQEFISDLQSK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2297 TRLkAEAELLQQQKELAQEQARRlqEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSR--AQARAE 2374
Cdd:TIGR00606 704 LRL-APDKLKSTESELKKKEKRR--DEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllGTIMPE 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2375 EDARRFRKQAEDIGERLYRtELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVR 2454
Cdd:TIGR00606 781 EESAKVCLTDVTIMERFQM-ELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI 859
|
730 740 750
....*....|....*....|....*....|....*....
gi 1920237982 2455 QeQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQL 2493
Cdd:TIGR00606 860 Q-HLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV 897
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2149-2588 |
1.53e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2149 EQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAenral 2228
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2229 vLRDKDSAQRLLQEEAEKMKQVAEEaarlsvaaqeaaRLRQLAEedlaqQRALAEKMLKEKMQAVQEATRLKAEAELLQQ 2308
Cdd:PRK03918 236 -LKEEIEELEKELESLEGSKRKLEE------------KIRELEE-----RIEELKKEIEELEEKVKELKELKEKAEEYIK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2309 QKELAQEQARRLQEDKEQMA--QQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMsRAQARAEEDARRFRKQAED 2386
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSrlEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2387 IGERLyrTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKqeAQLLQLKS---------EEMQTVRQEQ 2457
Cdd:PRK03918 377 LKKRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK--KAIEELKKakgkcpvcgRELTEEHRKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2458 LLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEvAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAE 2537
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLK 531
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1920237982 2538 EGVRRQQEELQRLAqQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEE 2588
Cdd:PRK03918 532 EKLIKLKGEIKSLK-KELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2299-2585 |
1.53e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.49 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2299 LKAEAELLQQQKELAQEQARRlqedkEQMAQQLAQETQGfQKTLETERQrqlemsAEAERLRLRVAEMsraqaRAEEDAR 2378
Cdd:COG3096 288 LELRRELFGARRQLAEEQYRL-----VEMARELEELSAR-ESDLEQDYQ------AASDHLNLVQTAL-----RQQEKIE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2379 RFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEA----QLLQLKsEEMQTVR 2454
Cdd:COG3096 351 RYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiqyqQAVQAL-EKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2455 Q---------EQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQ------DEVAKAQA-------LREEQQRQQ 2512
Cdd:COG3096 430 GlpdltpenaEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiaGEVERSQAwqtarelLRRYRSQQA 509
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237982 2513 QQMQQEKqqLAASMEEARRRQHEAEEgVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALAR 2585
Cdd:COG3096 510 LAQRLQQ--LRAQLAELEQRLRQQQN-AERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1294-1435 |
1.60e-05 |
|
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: 49.98 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1294 RTRYSELSTLTSQYIRFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRqlaeahaqakAQAEREAQglqR 1369
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKR----------YQDQLEAQ---R 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 1370 RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQL 1435
Cdd:pfam12037 123 RRNEELLRKQEESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAEARAKEERENEDLNLEQ 188
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1450-1714 |
1.79e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1450 QALRARAEEAEAQKRQAQEEAERLRRQVqDETQRKRQA--EAELALRVQAEAEAAREKQRALQA-LEELRLQAEEAERRL 1526
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEL-EEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESqLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1527 RQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAtrraqqqaeaeraraeaerele 1606
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI---------------------- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1607 rwqlkanEALRLRLQAEEVAQQKSLtqaeaekqkeeaerearrrgKAEEQAVRQRelaEQELEKQRQLAEGTAQQRLAAE 1686
Cdd:COG3206 301 -------AALRAQLQQEAQRILASL--------------------EAELEALQAR---EASLQAQLAQLEARLAELPELE 350
|
250 260
....*....|....*....|....*...
gi 1920237982 1687 QELIRLRAETeqgEQQRQLLEEELARLQ 1714
Cdd:COG3206 351 AELRRLEREV---EVARELYESLLQRLE 375
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1684-1779 |
1.81e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 51.11 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1684 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1763
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 1920237982 1764 EAEAGRFrELAEEAAR 1779
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
16-131 |
1.82e-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: 47.06 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 16 DERDRVQkktFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEvlsgDSLPRERDVIRSSRLPRE-KGRM 85
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLIN----DSVPDTIDERVLNKPPRKnKPLN 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1920237982 86 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 131
Cdd:cd21294 77 NFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1314-1530 |
1.83e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 50.64 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1314 TLRRMEEEERLAEQQRAEERERLAEVEAALEkqrqlaEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQ 1393
Cdd:pfam02029 134 EIREKEYQENKWSTEVRQAEEEGEEEEDKSE------EAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1394 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRV-VRLQLEATERQRGGAEG-ELQALRARAEEAEAQKRQAQEEAE 1471
Cdd:pfam02029 208 KSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLeAEQKLEELRRRRQEKESeEFEKLRQKQQEAELELEELKKKRE 287
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 1472 RLRRQVQDETQRKRQAEAELALRVQaeaeaaREKQRALQALEelRLQAEEAERRLRQAE 1530
Cdd:pfam02029 288 ERRKLLEEEEQRRKQEEAERKLREE------EEKRRMKEEIE--RRRAEAAEKRQKLPE 338
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1364-2000 |
1.93e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1364 AQGLQR---RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATER 1440
Cdd:pfam05483 73 SEGLSRlysKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1441 QRGGAEgELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAElaLRVQAEaeaarekqralQALEELRLQAE 1520
Cdd:pfam05483 153 TRHLCN-LLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEE--LRVQAE-----------NARLEMHFKLK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1521 EAERRLRQAEAERARQV-----QVALETAQrSAEAElqsehasfaEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAE 1595
Cdd:pfam05483 219 EDHEKIQHLEEEYKKEIndkekQVSLLLIQ-ITEKE---------NKMKDLTFLLEESRDKANQLEEKTKLQDENLKELI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1596 RARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQla 1675
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR-- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1676 egTAQQRLaaeqelirlraetEQGEQQRQLLEEELARLQREAAAATQ----KRRELEaELAKVRAEMEVLLASKARAEEE 1751
Cdd:pfam05483 367 --TEQQRL-------------EKNEDQLKIITMELQKKSSELEEMTKfknnKEVELE-ELKKILAEDEKLLDEKKQFEKI 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1752 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALaeEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLkteaeialk 1831
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLEIQLTAI--KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL--------- 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1832 ekeaENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGL--VEDTLRQRR--------QVEEEI 1901
Cdd:pfam05483 500 ----ENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELesVREEFIQKGdevkckldKSEENA 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1902 LALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKsLAAEEEAARQR--- 1978
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNK-LELELASAKQKfee 654
|
650 660 670
....*....|....*....|....*....|....*...
gi 1920237982 1979 ----------------KAALEEVERLKAKVEEARRLRE 2000
Cdd:pfam05483 655 iidnyqkeiedkkiseEKLLEEVEKAKAIADEAVKLQK 692
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1326-1480 |
1.97e-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: 49.15 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1326 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREaqglQRRMQEEVARREEVAVEAQEQKRSIqeelqhlrqSSEA 1405
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE----IKRLELEIEEVEARIKKYEEQLGNV---------RNNK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 1406 EIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1480
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1325-1753 |
2.19e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.68 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1325 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE 1404
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1405 AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1484
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1485 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTA 1564
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1565 QLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAE 1644
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1645 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKR 1724
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420
....*....|....*....|....*....
gi 1920237982 1725 RELEAELAKVRAEMEVLLASKARAEEESR 1753
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAA 512
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1511-1949 |
2.22e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 50.79 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1511 ALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQ---------LR 1581
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALrlaaalapfWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1582 EEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQR 1661
Cdd:COG3903 557 LRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAA 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1662 ELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVL 1741
Cdd:COG3903 637 AAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAA 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1742 LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATR 1821
Cdd:COG3903 717 AAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAA 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1822 LKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEI 1901
Cdd:COG3903 797 AAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAA 876
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1920237982 1902 LALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQL 1949
Cdd:COG3903 877 AAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAA 924
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2131-2336 |
2.29e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.99 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2131 LRQKQAADA-----EMEKHKQFAEQALRQKaqveqeltalrlQLEETDH---------QKSILDEELQRLKAEVTEAARQ 2196
Cdd:NF012221 1561 LADKERAEAdrqrlEQEKQQQLAAISGSQS------------QLESTDQnaletngqaQRDAILEESRAVTKELTTLAQG 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2197 RGQVEEElfslRVQMEELGKlKARIEAENRAL--VLRDKDSAQRLLQEEAEKMKQ--------VAEEAARLSVAAQEAAR 2266
Cdd:NF012221 1629 LDALDSQ----ATYAGESGD-QWRNPFAGGLLdrVQEQLDDAKKISGKQLADAKQrhvdnqqkVKDAVAKSEAGVAQGEQ 1703
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2267 LRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQ 2336
Cdd:NF012221 1704 NQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAK 1773
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2131-2578 |
2.41e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.59 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2131 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTalrlQLEETDHQKSILDEELQRLKAEVTEAARQRGQVE-----EELF 2205
Cdd:pfam10174 58 LKEQYRVTQEENQHLQLTIQALQDELRAQRDLN----QLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEherqaKELF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2206 SLRVQMEELgklKARIEAENRALVLRDkDSAQRLL---QEEAEKMKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALA 2282
Cdd:pfam10174 134 LLRKTLEEM---ELRIETQKQTLGARD-ESIKKLLemlQSKGLPKKSGEEDWERTRRIAEAEMQLGHL--EVLLDQKEKE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2283 EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLqedkEQMAQQLAQETQgfqkTLETErqrqLEMSAEAERLRLR 2362
Cdd:pfam10174 208 NIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSL----ERNIRDLEDEVQ----MLKTN----GLLHTEDREEEIK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2363 VAEMSRAQARaeedarrFRK-QAEDIGERLYRTE---LATQEKVmlvQTLETQRQQSDRDAERLREAIAELEHEKDKLKQ 2438
Cdd:pfam10174 276 QMEVYKSHSK-------FMKnKIDQLKQELSKKEselLALQTKL---ETLTNQNSDCKQHIEVLKESLTAKEQRAAILQT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2439 EAQLLQLKSEEMQTV-----RQEQLLQETQALQQSFLSE-KDSLLQRERCIEQEKAKLEQL---FQDEVAKAQALREEQQ 2509
Cdd:pfam10174 346 EVDALRLRLEEKESFlnkktKQLQDLTEEKSTLAGEIRDlKDMLDVKERKINVLQKKIENLqeqLRDKDKQLAGLKERVK 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 2510 RQQQQMQQEKQQLAaSMEEARRrqhEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEE 2578
Cdd:pfam10174 426 SLQTDSSNTDTALT-TLEEALS---EKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPE 490
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1350-1565 |
2.47e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1350 AEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLrqssEAEIQAKARQVEAAERsrlRIEEEIR 1429
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEA---EIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1430 VVRLQLEATERQrGGAEGELQAL--------------------RARAEEAEAQKrQAQEEAERLRRQVQDETQRKRQAEA 1489
Cdd:COG3883 87 ELGERARALYRS-GGSVSYLDVLlgsesfsdfldrlsalskiaDADADLLEELK-ADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 1490 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ 1565
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3771-3807 |
2.54e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.54e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1920237982 3771 LRLLDAQLATGGIVDPRLGFHLPLDVAYQRGYLDKDT 3807
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1609-2027 |
2.58e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.29 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1609 QLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1688
Cdd:COG5278 105 QQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1689 LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG 1768
Cdd:COG5278 185 LLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1769 RFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEA 1848
Cdd:COG5278 265 AALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1849 FQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGT 1928
Cdd:COG5278 345 ALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1929 AEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2008
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
410
....*....|....*....
gi 1920237982 2009 QLQLAQEAAQKRLQAEEKA 2027
Cdd:COG5278 505 LAALLLAAAEAALAAALAA 523
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1243-1574 |
2.69e-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: 50.40 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1243 QRFAKQYINAIKDYelqlvtYKAQLEPVASPAKKPKvQSGSESIIQEYVDLRTRY-SELSTLTSQyirfiSETLRRMEEE 1321
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1322 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQ----RRMQEEVArreEVAVEAQEQKRSIQEELQ 1397
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPtntyKTLELEIA---ESDVEVKKAELELVKEEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1398 HLRQSSEAEIQAKAR-QVEAAERSRLrieEEIRVVRLQLEATERQRGGAE-GELQALRARAEEAEAQKRQA--------- 1466
Cdd:NF033838 198 KEPRDEEKIKQAKAKvESKKAEATRL---EKIKTDREKAEEEAKRRADAKlKEAVEKNVATSEQDKPKRRAkrgvlgepa 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1467 -----QEEAERLRRQVQDET-------QRKRQAEAE-LALRVQAEAEAAREKQR---ALQALEELRLQAEEAERRLRQAE 1530
Cdd:NF033838 275 tpdkkENDAKSSDSSVGEETlpspslkPEKKVAEAEkKVEEAKKKAKDQKEEDRrnyPTNTYKTLELEIAESDVKVKEAE 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1920237982 1531 A----ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEH 1574
Cdd:NF033838 355 LelvkEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEA 402
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1817-2570 |
2.85e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 50.59 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1817 SEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQ 1896
Cdd:NF041483 22 AEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRSLASRPAYDGADIGYQAEQLLRNAQIQADQLRADAERELRDARA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1897 VEEEIlaLKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQ----------AEQEAARQRQLAAEEERRRREAEERVQK 1966
Cdd:NF041483 102 QTQRI--LQEHAEHQARLQAELHTEAVQRRQQLDQELAERRQtveshvnenvAWAEQLRARTESQARRLLDESRAEAEQA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1967 SLAAEEEAARqrkAALEEVERLKAKVEEARRLRE----RAEQESARQLQLAQEAAQKRLQAEEKAHAF-------AVQQK 2035
Cdd:NF041483 180 LAAARAEAER---LAEEARQRLGSEAESARAEAEailrRARKDAERLLNAASTQAQEATDHAEQLRSStaaesdqARRQA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2036 EQELQQTLQQEQSVLERLR-----SEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAE 2110
Cdd:NF041483 257 AELSRAAEQRMQEAEEALRearaeAEKVVAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQAL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2111 KLRKEAEQEAARRAQAEQAALRQKQAAdAEMEKHKQFAEQALRQKAQVEQELTalRLQLEETDHQKSILDEELQRLKAEV 2190
Cdd:NF041483 337 ADARAEAEKLVAEAAEKARTVAAEDTA-AQLAKAARTAEEVLTKASEDAKATT--RAAAEEAERIRREAEAEADRLRGEA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2191 TEAARQ-RGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAAR-----LSVAAQEA 2264
Cdd:NF041483 414 ADQAEQlKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARtaeelLTKAKADA 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2265 ARLRQLAEEDLAQQRALA-EKMLKEKMQAVQEATRLKAEAELLQQQkelAQEQARRLQEDKEQMAQQLAQETQGFQKTLE 2343
Cdd:NF041483 494 DELRSTATAESERVRTEAiERATTLRRQAEETLERTRAEAERLRAE---AEEQAEEVRAAAERAARELREETERAIAARQ 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2344 TERQRQLE-MSAEAERlRLRVAEMSRAQARAEedARRFRKQAEDIGERLyRTELAtqekvmlvQTLETQRQQSDRDAERL 2422
Cdd:NF041483 571 AEAAEELTrLHTEAEE-RLTAAEEALADARAE--AERIRREAAEETERL-RTEAA--------ERIRTLQAQAEQEAERL 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2423 R-EAIAELEHEkdKLKQEAQLLQLKSEEMQtvRQEQLLQETQALQQSFLSEKDSLLQRercIEQEKAKleqlfqdevaka 2501
Cdd:NF041483 639 RtEAAADASAA--RAEGENVAVRLRSEAAA--EAERLKSEAQESADRVRAEAAAAAER---VGTEAAE------------ 699
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2502 qalreeqqrqqqqmqqekqQLAASMEEARRRQHEAEEGVRRQQEEL-QRLAQQQQQQEKLLAEENQRLRE 2570
Cdd:NF041483 700 -------------------ALAAAQEEAARRRREAEETLGSARAEAdQERERAREQSEELLASARKRVEE 750
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2210-2590 |
3.02e-05 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 50.38 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2210 QMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2289
Cdd:COG5281 1 AAALAAAAALAAAAAAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2290 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA 2369
Cdd:COG5281 81 AAALAEDAAAAAAAAEAALAALAAAALALAAAALAEAALAAAAAAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2370 QARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEE 2449
Cdd:COG5281 161 AAAAAAAAAAAAAAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2450 MQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEA 2529
Cdd:COG5281 241 SAAAQALAALAAAAAAAALALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 2530 R-RRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIA 2590
Cdd:COG5281 321 AqALRAAAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWA 382
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2131-2433 |
3.18e-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: 49.68 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2131 LRQKQAADAEMEKHkqfAEQALRQKAQVEQELTALRLQLEETDHQksildeeLQRLKAEVTEAARQRGQVEEELFSLRVQ 2210
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2211 MEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEkmkqvaeeaarlsVAAQEAARLRQLAEEDLAQQRALAEKM-LKEK 2289
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2290 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAQETQGFQKTLEterqrqlEMSAEAERLRLRVAEMSRA 2369
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRLA-------GLEADLERRTQQFQEMQRA 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237982 2370 QARAEEDARRFRKQAEDIGERLYRTE---LATQEKV-MLVQTLETQRQQSDRDAERLREaiaELEHEK 2433
Cdd:pfam19220 320 RAELEERAEMLTKALAAKDAALERAEeriASLSDRIaELTKRFEVERAALEQANRRLKE---ELQRER 384
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2147-2378 |
3.30e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 49.69 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2147 FAEQALRQKAQ---VEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQrgqveeelfsLRVQMEELGKLKARIEA 2223
Cdd:PRK11637 38 FSAHASDNRDQlksIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRK----------LRETQNTLNQLNKQIDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2224 ENRalvlrdkdSAQRLLQEEAEKMKqvaeeaarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQA----VQEAtRL 2299
Cdd:PRK11637 108 LNA--------SIAKLEQQQAAQER---------LLAAQLDAAFRQGEHTGLQLILSGEESQRGERILAyfgyLNQA-RQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2300 KAEAELLQQQKELAQEqaRRLQEDKEQMAQQLAQETQGFQKTLETER-----------------QRQL-EMSAEAERLRL 2361
Cdd:PRK11637 170 ETIAELKQTREELAAQ--KAELEEKQSQQKTLLYEQQAQQQKLEQARnerkktltglesslqkdQQQLsELRANESRLRD 247
|
250
....*....|....*...
gi 1920237982 2362 RVAEMSR-AQARAEEDAR 2378
Cdd:PRK11637 248 SIARAEReAKARAEREAR 265
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1384-1521 |
3.44e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1384 EAQEQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGA---------EGELQA 1451
Cdd:COG1579 21 RLEHRLKELPAELAELEDelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1452 LRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEE 1521
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1652-1874 |
3.88e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.90 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1652 KAEEQAVRQRELAEQELEK-QRQLAEgtaqqrlaAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRE-LEA 1729
Cdd:COG1842 16 ALLDKAEDPEKMLDQAIRDmEEDLVE--------ARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREdLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1730 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVL 1809
Cdd:COG1842 88 EALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 1810 AEklaaiseatrlkteAEIALKEKEAENERLRRLAEDEAFQRRLLEeqaAQHKADIEARLAQLRK 1874
Cdd:COG1842 168 ER--------------MEEKIEEMEARAEAAAELAAGDSLDDELAE---LEADSEVEDELAALKA 215
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1361-1555 |
3.89e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 50.02 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1361 EREAQGLQRRMQEEVarreEVAVEAQEQKRSIQEELQhlrqsseaEIQAKARqveaAERSRL--RIE-EEIRVVRLQLEA 1437
Cdd:PTZ00491 643 ERTRDSLQKSVQLAI----EITTKSQEAAARHQAELL--------EQEARGR----LERQKMhdKAKaEEQRTKLLELQA 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1438 TerqrgGAEGELQAlRARAE-EAEAQKRQAQEEAErlrrqVQDETQRKRqaeaelALRVQAEAEAAREKQRALQALEELR 1516
Cdd:PTZ00491 707 E-----SAAVESSG-QSRAEaLAEAEARLIEAEAE-----VEQAELRAK------ALRIEAEAELEKLRKRQELELEYEQ 769
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1920237982 1517 LQAE---EAERRLRQAEAERARQVQVAL--ETAQRSAEA--ELQSE 1555
Cdd:PTZ00491 770 AQNEleiAKAKELADIEATKFERIVEALgrETLIAIARAgpELQAK 815
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
924-1494 |
4.03e-05 |
|
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: 50.12 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 924 DRLQAEREYGSCSRHYQQLLQSLEQGEQEESrcqrcISELKDIRL-QLEACETRTVHRLRlpldkepaRECAQRITEQQK 1002
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKRLwDRDTGNSITIDHLR--------RELDDRNMEVQR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1003 AQAEVDGL-----GKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEE 1077
Cdd:pfam15921 431 LEALLKAMksecqGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKER 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1078 VlraheeqlkeaqavpatlpeLEATKAALKKLRAQAEAQQPVFDALRDE---LRGAQEVGERLQQRHGERDVEVERWRER 1154
Cdd:pfam15921 511 A--------------------IEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQ 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1155 VTLLLE-------RWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLR--DAKQRQEQIQAVPLANSQAvrEQLRQE 1225
Cdd:pfam15921 571 IENMTQlvgqhgrTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRelEARVSDLELEKVKLVNAGS--ERLRAV 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1226 KALLEDIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQsgsesiiqeyvdLRTRYSELSTLTS 1305
Cdd:pfam15921 649 KDIKQERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ------------LKSAQSELEQTRN 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1306 qyirfiseTLRRMEEEERLAeqqraeererlaeVEAALEKQRQLAEAHAQAKAqaereaqglqrrMQEEVARREEVAVEA 1385
Cdd:pfam15921 714 --------TLKSMEGSDGHA-------------MKVAMGMQKQITAKRGQIDA------------LQSKIQFLEEAMTNA 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1386 QEQKRSIQEELQHLRQsseaeiqakarqveaaersrlrieeeirvvRLQLEATERQRggAEGELQALRA---RAEEAEAQ 1462
Cdd:pfam15921 761 NKEKHFLKEEKNKLSQ------------------------------ELSTVATEKNK--MAGELEVLRSqerRLKEKVAN 808
|
570 580 590
....*....|....*....|....*....|..
gi 1920237982 1463 KRQAQEEAERLRRQVQDETQRKRQAEAELALR 1494
Cdd:pfam15921 809 MEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1073-1572 |
4.05e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1073 QEAEEVLRAHEEQlkeaQAVPATLPELEATKAALKK-LRAQAEAQQpvfdaLRDELRGAQEVG-------ERLQQRHGER 1144
Cdd:PRK04863 496 DVARELLRRLREQ----RHLAEQLQQLRMRLSELEQrLRQQQRAER-----LLAEFCKRLGKNlddedelEQLQEELEAR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1145 ----DVEVERWRERVTLLlerwQAVLAQTDVRQRELEQLGRQLRYYRESADPL----GAWLRDAKQRQEQIQ--AVPLAN 1214
Cdd:PRK04863 567 leslSESVSEARERRMAL----RQQLEQLQARIQRLAARAPAWLAAQDALARLreqsGEEFEDSQDVTEYMQqlLERERE 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1215 SQAVREQLRQEK-ALLEDIER----HGEKVEECQRFAKQ-------------------YINA-------------IKDYE 1257
Cdd:PRK04863 643 LTVERDELAARKqALDEEIERlsqpGGSEDPRLNALAERfggvllseiyddvsledapYFSAlygparhaivvpdLSDAA 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1258 LQLVT--------YKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSelstltsqyiRFISETL-RRMEEEERLAEQQ 1328
Cdd:PRK04863 723 EQLAGledcpedlYLIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYS----------RFPEVPLfGRAAREKRIEQLR 792
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1329 RaeERERLAEveaalekqrqlaeahaqAKAQAEREAQGLQRRMQE---------EVARREEVAVEAQEQKRSIQEELQHL 1399
Cdd:PRK04863 793 A--EREELAE-----------------RYATLSFDVQKLQRLHQAfsrfigshlAVAFEADPEAELRQLNRRRVELERAL 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1400 RQSSEAEIQAKARQVEAAERSRL--------------RIEEEIRVVRLQLEATE------RQRGGA----EGELQALRAR 1455
Cdd:PRK04863 854 ADHESQEQQQRSQLEQAKEGLSAlnrllprlnlladeTLADRVEEIREQLDEAEeakrfvQQHGNAlaqlEPIVSVLQSD 933
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1456 AEEAEAQKR---QAQEEAERLRRQVQDET---QRKRQAEAELALRVQAEAEAAREKQRalQALEELRLQAEEAERRLRQA 1529
Cdd:PRK04863 934 PEQFEQLKQdyqQAQQTQRDAKQQAFALTevvQRRAHFSYEDAAEMLAKNSDLNEKLR--QRLEQAEQERTRAREQLRQA 1011
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1920237982 1530 EAERARQVQValetaqrsaEAELQSEHASFAEKTAQLERTLKE 1572
Cdd:PRK04863 1012 QAQLAQYNQV---------LASLKSSYDAKRQMLQELKQELQD 1045
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1377-1730 |
4.17e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1377 RREEVAVEAQEQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1456
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1457 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQ 1536
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1537 VQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEAL 1616
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1617 RLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1696
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 1920237982 1697 EQGEQQRQLLEEELARLQREAAAATQKRRELEAE 1730
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
17-137 |
4.21e-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: 46.14 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 17 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSSRLPREKGRMRfhKLQNVQIA 96
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIK---VPVDWNRVNKPPYPKLGENMK--KLENCNYA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237982 97 LDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 137
Cdd:cd21330 82 VELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
836-1486 |
4.23e-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: 49.97 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 836 NQEAQEAIARlEAQHQALVALWhQLHTEMKSLLAWQSLGRDMQlirsWSLATFRTLKPEE------------QRQALRsL 903
Cdd:TIGR00618 223 VLEKELKHLR-EALQQTQQSHA-YLTQKREAQEEQLKKQQLLK----QLRARIEELRAQEavleetqerinrARKAAP-L 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 904 ELHYQAFLRDSQDAGGFGPEDRLQaEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRL 983
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 984 PLDKEPARECAQRIT----EQQKAQAEVDGLGKGVARLSAEAEKVLALPEPSPAAptlRSELELTLGKLEQVRSLSAIYL 1059
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTtltqKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHA---KKQQELQQRYAELCAAAITCTA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1060 EKLKtisLVIRSTQEAEEVLRAHEEQLKEAQAVpaTLPELEATKAALKKLRAQAEAQQPVFDALR---------DELRGA 1130
Cdd:TIGR00618 452 QCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQETRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGPL 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1131 QEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLgawlrdakqRQEQIQAV 1210
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL---------QNITVRLQ 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1211 PLansqaVREQLRQEKALLEDIERHGEKVEECQRFAK--QYINAIKDYELQLVTYKAQLEpvASPAKKPKVQSGSESIIQ 1288
Cdd:TIGR00618 598 DL-----TEKLSEAEDMLACEQHALLRKLQPEQDLQDvrLHLQQCSQELALKLTALHALQ--LTLTQERVREHALSIRVL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1289 EYVDLRTRYSELSTLTSQY--IRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQG 1366
Cdd:TIGR00618 671 PKELLASRQLALQKMQSEKeqLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1367 LQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAE 1446
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEE 830
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1920237982 1447 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQ 1486
Cdd:TIGR00618 831 EQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3324-3362 |
4.49e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 43.09 E-value: 4.49e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1920237982 3324 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTATLL 3362
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
927-1365 |
4.51e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 927 QAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACE-----TRTVHRLRLPLDKEPAR--ECAQRITE 999
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERleELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1000 QQKAQAEVDGLGKGVARLSAEAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVL 1079
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1080 R------AHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRE 1153
Cdd:COG4717 233 EneleaaALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1154 RVTLLLERWQAVLAQTDVRQREleqlgrQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEkALLEDIE 1233
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDL------SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE-AGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1234 RHGEKVEECQRFaKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELstltSQYIRFISE 1313
Cdd:COG4717 386 ELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL----REELAELEA 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 1314 TLRRMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQ 1365
Cdd:COG4717 461 ELEQLEEDGELAEllQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3324-3359 |
4.76e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.76e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1920237982 3324 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 3359
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1311-1535 |
4.80e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.48 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1311 ISETLRRMEEEERLAEQQRAEERERLAEVEAAlEKQRQLAEAHAQAKAQAEREAQglqRRMQEEVARREEVavEAQEQKR 1390
Cdd:pfam02029 100 VAERKENNEEEENSSWEKEEKRDSRLGRYKEE-ETEIREKEYQENKWSTEVRQAE---EEGEEEEDKSEEA--EEVPTEN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1391 SIQEELQHLRQSSEAEIQAKARQVEaaERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKrQAQEEA 1470
Cdd:pfam02029 174 FAKEEVKDEKIKKEKKVKYESKVFL--DQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFL-EAEQKL 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 1471 ERLRRQVQD------ETQRKRQAEAELALrvqAEAEAAREKQRAL--------QALEELRLQAEEAERRLRQAEAERAR 1535
Cdd:pfam02029 251 EELRRRRQEkeseefEKLRQKQQEAELEL---EELKKKREERRKLleeeeqrrKQEEAERKLREEEEKRRMKEEIERRR 326
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1325-1722 |
4.93e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 49.27 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1325 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEElqhlrqsse 1404
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAE--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1405 aeiqaKARQVEAAERSRLRIEEEIRvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1484
Cdd:COG3064 75 -----AAKKLAEAEKAAAEAEKKAA------AEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1485 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTA 1564
Cdd:COG3064 144 AEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1565 QLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAE 1644
Cdd:COG3064 224 RAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAAL 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237982 1645 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQ 1722
Cdd:COG3064 304 AAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLA 381
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1491-1760 |
5.32e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1491 LALRVQAEAEAAREKQRALQALEElRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTL 1570
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1571 KEEHVAVVQLREeatrraqqqaeaeRARAEAERELERWQLKANEALRLRLQAEEVAQqksltqaeaekqKEEAEREARRR 1650
Cdd:COG4942 90 KEIAELRAELEA-------------QKEELAELLRALYRLGRQPPLALLLSPEDFLD------------AVRRLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1651 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAE 1730
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
250 260 270
....*....|....*....|....*....|
gi 1920237982 1731 LAKVRAEMEVLLASKARAEEESRSTSEKSK 1760
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1059-1527 |
5.38e-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: 49.35 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1059 LEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKAALkklraQAEAQQpVFDALRDELRGAQEVGERLQ 1138
Cdd:pfam05557 51 QELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQ-----LADARE-VISCLKNELSELRRQIQRAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1139 QRHGERDVEVERWRERVTLLLERWQAV---LAQTDVRQREL---EQLGRQLRYYRESADPLGAWLRDAKQRQEQIqavpl 1212
Cdd:pfam05557 125 LELQSTNSELEELQERLDLLKAKASEAeqlRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELARI----- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1213 ANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKK------------PKVQ 1280
Cdd:pfam05557 200 PELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSwvklaqdtglnlRSPE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1281 SGSESIIQEYVDLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQL---------- 1349
Cdd:pfam05557 280 DLSRRIEQLQQREIVLKEENSSLTSS-ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRVllltkerdgy 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1350 ------------AEAHAQAKAQAEREAQGLQRRMQ---EEVARREEVAVEA----QEQKRSIQEELQHLRQ--------S 1402
Cdd:pfam05557 359 railesydkeltMSNYSPQLLERIEEAEDMTQKMQahnEEMEAQLSVAEEElggyKQQAQTLERELQALRQqesladpsY 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1403 SEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ--DE 1480
Cdd:pfam05557 439 SKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIErlKR 518
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1920237982 1481 TQRKRQAEAELALRVQAEAEAAREKQralqaLEELRLQAEEAERRLR 1527
Cdd:pfam05557 519 LLKKLEDDLEQVLRLPETTSTMNFKE-----VLDLRKELESAELKNQ 560
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4110-4138 |
5.46e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 5.46e-05
10 20
....*....|....*....|....*....
gi 1920237982 4110 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4138
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1621-1797 |
5.59e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1621 QAEEVAQQKsltQAEAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1696
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1697 EQGEQQRQLLEEELArlQREAAAATQKRRELEA-----ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfr 1771
Cdd:PRK09510 161 KKAAAEAKKKAEAEA--AKKAAAEAKKKAEAEAaakaaAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEA---- 234
|
170 180
....*....|....*....|....*.
gi 1920237982 1772 ELAEEAARLRALAEEAKRQRQLAEED 1797
Cdd:PRK09510 235 KAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1801-2191 |
5.85e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.35 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1801 QRAEAERVLAEKLAAIsEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRLLEEQAAqhkadIEARLAQLRKASESEL 1880
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAA-----IYAEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1881 ERQKglVEDTLRQRRQVEEEilalkgsfekaaagkaELELELGRIRGTaeDTLRSKEQAEQEAARQRqlaaeeerrrrea 1960
Cdd:pfam17380 351 ERIR--QEERKRELERIRQE----------------EIAMEISRMREL--ERLQMERQQKNERVRQE------------- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1961 EERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR-ERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKeqel 2039
Cdd:pfam17380 398 LEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK---- 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2040 qqtlqqeqsvleRLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQE 2119
Cdd:pfam17380 474 ------------RKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEE 541
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 2120 aarraqaeqaalRQKQaadAEMEKHKQFAEQALRqkaqVEQELTALRLQLEETDHQKSILDEELQRLKAEVT 2191
Cdd:pfam17380 542 ------------RRKQ---QEMEERRRIQEQMRK----ATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
171-248 |
6.05e-05 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 44.60 E-value: 6.05e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237982 171 DNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 248
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1311-1516 |
6.10e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.51 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1311 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVAR-REEVAVEAQEQK 1389
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgREDLAREALERK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1390 RSIQEELQHLRQsseaeiqakarQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRARAEEAEAQKR----- 1464
Cdd:COG1842 94 AELEAQAEALEA-----------QLAQLEEQVEKLKEALRQLESKLEELKAKK-------DTLKARAKAAKAQEKvneal 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1465 ------QAQEEAERLRRQVqDETQRKRQAEAELALR--VQAEAEAAREKQRALQALEELR 1516
Cdd:COG1842 156 sgidsdDATSALERMEEKI-EEMEARAEAAAELAAGdsLDDELAELEADSEVEDELAALK 214
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1675-2171 |
6.11e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 49.47 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1675 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV----------RAEMEVLLAS 1744
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgllllgdyEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1745 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKT 1824
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1825 EAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILAL 1904
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1905 KGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 1984
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1985 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAA 2064
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2065 EEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKH 2144
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 1920237982 2145 KQFAEQALRQKAQVEQELTALRLQLEE 2171
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2131-2581 |
6.34e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.45 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2131 LRQKQAADAEMEKHKQFA--EQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQ-RGQVEEELFSL 2207
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTklQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTlDDQWKEKRDEL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2208 R----VQMEELGKLKARIEA-ENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAA---------RLRQLAEE 2273
Cdd:pfam12128 307 NgelsAADAAVAKDRSELEAlEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKhqdvtakynRRRSKIKE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2274 DLA------QQRALAEKMLKEKMQAVQEATRLKAEAEL---LQQQKELAQEQARRLQEDKEQMAQQLAQETQGfQKTLET 2344
Cdd:pfam12128 387 QNNrdiagiKDKLAKIREARDRQLAVAEDDLQALESELreqLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2345 ERQRQLEMSAEAERLRLRVAEMSRAQaraeEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQ-RQQSDRDAERLR 2423
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQ----SELRQARKRRDQASEALRQASRRLEERQSALDELELQlFPQAGTLLHFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2424 EAIAELEHEKDKLKQEAQL----LQLKSEEMQTVRQEQLLQETQALQQSflsEKDSLLQRERCIEQEKAKLEQLFQDEVA 2499
Cdd:pfam12128 542 KEAPDWEQSIGKVISPELLhrtdLDPEVWDGSVGGELNLYGVKLDLKRI---DVPEWAASEEELRERLDKAEEALQSARE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2500 KAQALreeqqrqqqqmQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLA----QQQQQQEKLLAEENQRLRERLQHL 2575
Cdd:pfam12128 619 KQAAA-----------EEQLVQANGELEKASREETFARTALKNARLDLRRLFdekqSEKDKKNKALAERKDSANERLNSL 687
|
....*.
gi 1920237982 2576 EEERRA 2581
Cdd:pfam12128 688 EAQLKQ 693
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1402-1615 |
6.76e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1402 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1479
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1480 -ETQRKRQAEAELAL------------RVQAEAEAAREKQRALQALEELRLQAEEAerrlrQAEAERARQVQVALETAQR 1546
Cdd:COG3883 93 rALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAK-----KAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 1547 SAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEA 1615
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1798-2009 |
6.90e-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: 48.61 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1798 AVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIeARLAQLRKASE 1877
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-AELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1878 SELERQKGLVEDTL----RQRRQVEEEILALKGSFEKAAAGKA-------ELELELGRIRGTAEDTLRSKEQAEQEAARQ 1946
Cdd:COG4942 97 AELEAQKEELAELLralyRLGRQPPLALLLSPEDFLDAVRRLQylkylapARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237982 1947 RQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQ 2009
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3105-3141 |
7.05e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 7.05e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1920237982 3105 LRLLDAQLSTGGIVDPSKSHRVPLDVACARGYLDKET 3141
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1282-1584 |
7.18e-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: 48.53 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1282 GSESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAaLEKQ--------RQLAEAH 1353
Cdd:pfam19220 63 AYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEA-LERQlaaeteqnRALEEEN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1354 AQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRsiqeeLQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRL 1433
Cdd:pfam19220 142 KALREEAQAAEKALQRAEGELATARERLALLEQENRR-----LQALSEEQAAELAELTRRLAELETQLDATRARLRALEG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1434 QL--EATERQRGGAEGELQALRARAEEAEaqkrqaqeeaerLRRQVQDETQRKRQAE---AELALRVQAEAEAAREKQRa 1508
Cdd:pfam19220 217 QLaaEQAERERAEAQLEEAVEAHRAERAS------------LRMKLEALTARAAATEqllAEARNQLRDRDEAIRAAER- 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237982 1509 lqALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSE--HASFAEKTAQLERTlkEEHVAVVQLREEA 1584
Cdd:pfam19220 284 --RLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEmlTKALAAKDAALERA--EERIASLSDRIAE 357
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2243-2378 |
7.35e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 48.72 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2243 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2322
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 2323 DKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDAR 2378
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAE 328
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1378-1538 |
7.83e-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: 48.98 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1378 REEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAE 1457
Cdd:pfam07111 490 RNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELT 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1458 EAEAQKRQAQEEA-----ERLRRQVQDETQ-----RKRQAEAELALRvQAEAEAAREKQRAlqalEELRLQAEEAerrlR 1527
Cdd:pfam07111 570 QQQEIYGQALQEKvaeveTRLREQLSDTKRrlneaRREQAKAVVSLR-QIQHRATQEKERN----QELRRLQDEA----R 640
|
170
....*....|..
gi 1920237982 1528 QAEAER-ARQVQ 1538
Cdd:pfam07111 641 KEEGQRlARRVQ 652
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1446-1580 |
8.41e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.83 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1446 EGELQALRARAEEAEAQkrqAQEEAERLRRQVQDetqRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERR 1525
Cdd:pfam09787 67 RGQIQQLRTELQELEAQ---QQEEAESSREQLQE---LEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1526 LRQAEAERARQ-VQVALETAQRSAEAELQSE-HA---SFAEKTAQLERTLKEEHVAVVQL 1580
Cdd:pfam09787 141 IKDREAEIEKLrNQLTSKSQSSSSQSELENRlHQlteTLIQKQTMLEALSTEKNSLVLQL 200
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2150-2377 |
8.46e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2150 QALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKL--KARIEAENRA 2227
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2228 LVLRDKDSAQRLLQE--EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2305
Cdd:COG3883 93 RALYRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 2306 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDA 2377
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1661-2373 |
8.98e-05 |
|
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: 48.96 E-value: 8.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1661 RELAEQELEKQRQLAEGTAQQRLAAE---QELIRLRAETEQGEQQRQLLEEELARLQ-REAAAATQK-RRELEAELA--- 1732
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMHfRSLGSAISKiLRELDTEISylk 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1733 ----KVRAEMEVLLA-SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAER 1807
Cdd:pfam15921 238 grifPVEDQLEALKSeSQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1808 VLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQL-----RKASESELER 1882
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhKREKELSLEK 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1883 QK-----------GLVEDTLRQR---RQVEEEIL-ALKGSFEKAAAGkaELELELGRIRGtaedtlrSKEQAEQEAARQR 1947
Cdd:pfam15921 398 EQnkrlwdrdtgnSITIDHLRRElddRNMEVQRLeALLKAMKSECQG--QMERQMAAIQG-------KNESLEKVSSLTA 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1948 QLAAEEERRRREAEERVQKSLAAE--EEAARQRKAALEEVER-LKAKVEEARRLRERAEQesarQLQLAQEaaqkrLQAE 2024
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLEssERTVSDLTASLQEKERaIEATNAEITKLRSRVDL----KLQELQH-----LKNE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2025 EKaHAFAVQQKEQELQQTLQQEQSVLERLRseaeaarraaeeaeaareraereaaqsrRQVEEAERLkqsaeeqaqaqaq 2104
Cdd:pfam15921 540 GD-HLRNVQTECEALKLQMAEKDKVIEILR----------------------------QQIENMTQL------------- 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2105 aqaaaeklrkeaeqeaarraqaeqaalrqkqaadaeMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQ 2184
Cdd:pfam15921 578 ------------------------------------VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIR 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2185 RLKAEVTEAARQRGQV----EEELFSLRVQMEELGKLKARIEAENRAL--VLRDKDSAQRLLQEEAEKMKQVAEE-AARL 2257
Cdd:pfam15921 622 ELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKRNFRNKSEEMETTTNKlKMQL 701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2258 SVAAQEAARLR---QLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAqe 2334
Cdd:pfam15921 702 KSAQSELEQTRntlKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELS-- 779
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1920237982 2335 tqgfqkTLETERQR---QLE-MSAEAERLRLRVAEMSRAQARA 2373
Cdd:pfam15921 780 ------TVATEKNKmagELEvLRSQERRLKEKVANMEVALDKA 816
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1973-2278 |
9.08e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1973 EAARQRKAALEEVERLKAKVEEARRLRER----AEQESARQLQLAQEAA----QKRLQAEEKAHAFAVQQKEQELQqtlq 2044
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERrrklEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEERKRE---- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2045 qeqsvLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERlKQSAEEQAQAQAQAQAAAEKLRKEAEQEAArra 2124
Cdd:pfam17380 362 -----LERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR-KVKILEEERQRKIQQQKVEMEQIRAEQEEA--- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2125 qaeqaalRQKQAADAEMEKHKQFaEQALRQKAQVEQELTALRLQLEETDHQKSILD---------EELQRLKAEVTEAAR 2195
Cdd:pfam17380 433 -------RQREVRRLEEERAREM-ERVRLEEQERQQQVERLRQQEEERKRKKLELEkekrdrkraEEQRRKILEKELEER 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2196 QRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEE--AEKMKQVAEEAARLSVAAQEAARLRQLAEE 2273
Cdd:pfam17380 505 KQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRriQEQMRKATEERSRLEAMEREREMMRQIVES 584
|
....*
gi 1920237982 2274 DLAQQ 2278
Cdd:pfam17380 585 EKARA 589
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
4-131 |
9.43e-05 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 45.35 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 4 SRAIQHeisSLKDErdrvQKKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVIR 74
Cdd:cd21292 14 SEGTTH---SYSEE----EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTID-ERAINK 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237982 75 SSRLPrekgrmrFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 131
Cdd:cd21292 86 KKLTV-------FTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1796-2274 |
9.44e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1796 EDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLleEQAAQHKADIEARLAQLRKA 1875
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL--EALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1876 seselerqkglvedtLRQRRQVEEEILALKgsfEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEER 1955
Cdd:COG4717 155 ---------------LEELRELEEELEELE---AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1956 RRREAEervqKSLAAEEEAARQRKAALEEVERLKakveearRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQK 2035
Cdd:COG4717 217 EAQEEL----EELEEELEQLENELEAAALEERLK-------EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2036 EQELQQTLQQEQSVLERLRseaeaarraaeeaEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKE 2115
Cdd:COG4717 286 LALLFLLLAREKASLGKEA-------------EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2116 AEQEAARRAQAEQAALRQKQAADaeMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQ-KSILDEELQRLKAEVTEAA 2194
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAAL--LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEEL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2195 RQR-GQVEEELFSLRVQMEELGKLKARIEAENRAlvLRDKDSAQRLLQEEAE---KMKQVAEEAARLSVAAQEAARLRQL 2270
Cdd:COG4717 431 EEElEELEEELEELEEELEELREELAELEAELEQ--LEEDGELAELLQELEElkaELRELAEEWAALKLALELLEEAREE 508
|
....
gi 1920237982 2271 AEED 2274
Cdd:COG4717 509 YREE 512
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1848-2373 |
9.86e-05 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 49.10 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1848 AFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEkAAAGKAELELELGRIRG 1927
Cdd:COG3321 867 PFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAA-LLALVALAAAAAALLAL 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1928 TAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2007
Cdd:COG3321 946 AAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALA 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2008 RQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEE 2087
Cdd:COG3321 1026 ALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAA 1105
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2088 AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRL 2167
Cdd:COG3321 1106 LLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAAL 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2168 QLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEElgklkARIEAENRALVLRDKDSAQRLLQEEAEKM 2247
Cdd:COG3321 1186 AAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAA-----ALALLALAAAAAAVAALAAAAAALLAALA 1260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2248 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2327
Cdd:COG3321 1261 ALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAA 1340
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1920237982 2328 AQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARA 2373
Cdd:COG3321 1341 LALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1485-1769 |
1.08e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.41 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1485 RQAEAELALRVQAEAEAAREKQR--ALQAleelRLQAEEAER--RLRQAEAERARQVQVALETAQRSAEAELQSEHASFA 1560
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARfeARQA----RLEREKAAReaRHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1561 EKTAQlertlKEEHVAVVQLREEATRRAQQQAEAERARAEAERelerwQLKANEALRLRLQAEEVAQQKSLTqaeAEKQK 1640
Cdd:PRK05035 508 IKAGA-----RPDNSAVIAAREARKAQARARQAEKQAAAAADP-----KKAAVAAAIARAKAKKAAQQAANA---EAEEE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1641 EEAEREARRRGKAEEQAvrqRELAEQELEKQRQLAEGTAQQRLAAEQELIrLRAETEQGEQQRQLLEEElarlqreaaAA 1720
Cdd:PRK05035 575 VDPKKAAVAAAIARAKA---KKAAQQAASAEPEEQVAEVDPKKAAVAAAI-ARAKAKKAEQQANAEPEE---------PV 641
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1920237982 1721 TQKRRELEAELAKVRAEmevlLASKARAEEESRSTSEKSKQRLEAEAGR 1769
Cdd:PRK05035 642 DPRKAAVAAAIARAKAR----KAAQQQANAEPEEAEDPKKAAVAAAIAR 686
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1655-2365 |
1.10e-04 |
|
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: 48.56 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1655 EQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR-----LQREAAAATQKRRELEA 1729
Cdd:pfam05483 98 EAELKQKENKLQENRKIIE-AQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnlLKETCARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1730 ELAKVR---AEMEVLLASKARAEEESRSTSEKSkqRLEAEAgrfrELAEEAARLRALAEEAKRQRQlaeedavrqraEAE 1806
Cdd:pfam05483 177 EREETRqvyMDLNNNIEKMILAFEELRVQAENA--RLEMHF----KLKEDHEKIQHLEEEYKKEIN-----------DKE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1807 RVLAEKLAAISEATRLKTEAEIALKEKEaenERLRRLAEDEAFQRRLLEeQAAQHKADIEARLAQLRKASESELERQKGL 1886
Cdd:pfam05483 240 KQVSLLLIQITEKENKMKDLTFLLEESR---DKANQLEEKTKLQDENLK-ELIEKKDHLTKELEDIKMSLQRSMSTQKAL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1887 VED---TLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEerrrreaeer 1963
Cdd:pfam05483 316 EEDlqiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME---------- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1964 VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ--ESARQLQLAQEAAQKRLQAEEK-AHAFAVQqkeqeLQ 2040
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQELIFLLQAREKeIHDLEIQ-----LT 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2041 QTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLkqsaeeqaqaqaqaqaaaeklrkeaeqea 2120
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDM----------------------------- 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2121 arraqaeQAALRQKQAadaEMEKHKQFAEQALRQKAQVEQELTALRLQLE--------ETDHQKSILD---EELQRLKAE 2189
Cdd:pfam05483 512 -------TLELKKHQE---DIINCKKQEERMLKQIENLEEKEMNLRDELEsvreefiqKGDEVKCKLDkseENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2190 VTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEeaarLSVAAQEAARLRQ 2269
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE----LASAKQKFEEIID 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2270 LAEEDLAQQRALAEKMLKEKMQA---VQEATRLKAEAELLQQQK--------ELAQEQARRLQEDKEQ---MAQQLAQET 2335
Cdd:pfam05483 658 NYQKEIEDKKISEEKLLEEVEKAkaiADEAVKLQKEIDKRCQHKiaemvalmEKHKHQYDKIIEERDSelgLYKNKEQEQ 737
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1920237982 2336 QGFQKTLETER----------QRQLEMS-AEAERLRLRVAE 2365
Cdd:pfam05483 738 SSAKAALEIELsnikaellslKKQLEIEkEEKEKLKMEAKE 778
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1457-1536 |
1.22e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 48.41 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1457 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAE------AEAAREKQRALQA-LEELRLQAEEAERRLRQA 1529
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELvaleglAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 1920237982 1530 EAERARQ 1536
Cdd:PRK11448 218 RKEITDQ 224
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1459-1584 |
1.29e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1459 AEAQKRQAQEEAERLRRQVQDETQRKRQAEaELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLR----QAEAERA 1534
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAAlkqkQAEEAAA 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1535 RQVQVA----------LETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEA 1584
Cdd:PRK09510 140 KAAAAAkakaeaeakrAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA 199
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1131-1536 |
1.35e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1131 QEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAV 1210
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETL 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1211 planSQAVREQLRQEKALLED---IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSE--- 1284
Cdd:TIGR00606 774 ----LGTIMPEEESAKVCLTDvtiMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIElnr 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1285 SIIQEYVD-LRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQR---------AEERERLAEVEAALEKQRQLAEAHA 1354
Cdd:TIGR00606 850 KLIQDQQEqIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTevqslireiKDAKEQDSPLETFLEKDQQEKEELI 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1355 QAKAQAEREAQGLQRRMQEEVarrEEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ 1434
Cdd:TIGR00606 930 SSKETSNKKAQDKVNDIKEKV---KNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQD 1006
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1435 LEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALrvqaeaeAAREKQRALQALEE 1514
Cdd:TIGR00606 1007 IDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDL-------IKRNHVLALGRQKG 1079
|
410 420
....*....|....*....|..
gi 1920237982 1515 LRLQAEEAERRLRQAEAERARQ 1536
Cdd:TIGR00606 1080 YEKEIKHFKKELREPQFRDAEE 1101
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1321-1550 |
1.37e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 47.67 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1321 EERLAEQQRAEERERLAEVEAAlEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELqhlr 1400
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHGA-EISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1401 qsSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1480
Cdd:PRK07735 86 --TEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1481 TQRKRQAEAELALrvqaeaEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEA 1550
Cdd:PRK07735 164 KAKAKAAAAAKAK------AAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGN 227
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2154-2397 |
1.38e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.53 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2154 QKAQVEQELTALRLQleetdhQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDK 2233
Cdd:TIGR02794 44 DPGAVAQQANRIQQQ------KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2234 DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARlrQLAEEDLAQQRALAEKMLKE-KMQAVQEA-----TRLKAEAELLQ 2307
Cdd:TIGR02794 118 QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEaKKKAEAEAkakaeAEAKAKAEEAK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2308 QQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQaedI 2387
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA---I 272
|
250
....*....|
gi 1920237982 2388 GERLYRTELA 2397
Cdd:TIGR02794 273 QQNLYDDPSF 282
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1972-2585 |
1.40e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1972 EEAARQRKAALEEVERLKAKVEEARRlreraeqeSARQLQLAQEAAQKRLQAEEKAhafavqqkeqelqqtlqqeqSVLE 2051
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDARE--------QIELLEPIRELAERYAAARERL--------------------AELE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2052 RLRSEAEAARRAAEEAEAARERAEREAAQSRRQvEEAERLKQsaeeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAAL 2131
Cdd:COG4913 276 YLRAALRLWFAQRRLELLEAELEELRAELARLE-AELERLEA-----------------RLDALREELDELEAQIRGNGG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2132 RQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETdhqKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQM 2211
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2212 EELGKLKARIEAENRALVLRDKDSAQRLLQeeaekMKQVAEEAARLS-VAAQEAARLRQLAEEDLAQQRAlAEKML---- 2286
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSNIPARLLA-----LRDALAEALGLDeAELPFVGELIEVRPEEERWRGA-IERVLggfa 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2287 ------KEKMQAVQEAT-RLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETE--RQRQLEMSAEAE 2357
Cdd:COG4913 489 ltllvpPEHYAAALRWVnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAElgRRFDYVCVDSPE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2358 RLRLRVAEMSRA-QARAeeDARRFRKQAEDIGERLYRTELATQEKvmlVQTLETQRQQSDRDAERLREAIAELEHEKDKL 2436
Cdd:COG4913 569 ELRRHPRAITRAgQVKG--NGTRHEKDDRRRIRSRYVLGFDNRAK---LAALEAELAELEEELAEAEERLEALEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2437 KQEAQLLQ-LKSEEMQTVRQEQLLQETQALQQsflsekdsllQRERcIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQM 2515
Cdd:COG4913 644 QERREALQrLAEYSWDEIDVASAEREIAELEA----------ELER-LDASSDDLAAL-EEQLEELEAELEELEEELDEL 711
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237982 2516 QQEKQQLAASMEEARRRQHEAEEGVRRqQEELQRLAQQQQQQEKLLAEENQRLRERL-QHLEEERRAALAR 2585
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLEA-AEDLARLELRALLEERFAAALGDAVERELrENLEERIDALRAR 781
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2241-2339 |
1.45e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 47.19 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2241 QEEAEKMKQVAEEAARLSVAAQEAARL----RQLAEEDLAQQRALAE--KMLKEKMQavQEATRLKAEAELLQQQKElaQ 2314
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLLeeqqRELEQKLEDQERSYEEhlRQLKEKME--EERENLLKEQERALESKL--K 266
|
90 100
....*....|....*....|....*
gi 1920237982 2315 EQARRLQEDKEQMAQQLAQETQGFQ 2339
Cdd:cd16269 267 EQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3068-3104 |
1.47e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.47e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1920237982 3068 KLLSAEKAVTGYKDPYSGQSVSLFQALKKGLIPREQG 3104
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
19-130 |
1.52e-04 |
|
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: 44.18 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 19 DRVQKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLpreRDVirsSRLPREKGRMrfhkLQNVQIA 96
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKI---EDI---NGCPKNRSQM----IENIDAC 77
|
90 100 110
....*....|....*....|....*....|....
gi 1920237982 97 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTI 130
Cdd:cd21285 78 LSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2147-2313 |
1.53e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.54 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2147 FAEQALrqkAQVEQELTALRLQLEETDHQKSILDEElqrlkAEVTEAARQRGQVEEELFSLRVQMEELgklkarieaenR 2226
Cdd:COG3524 181 FAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAAL-----------R 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2227 AlVLRDKDSAQRLLQEEAEKM-KQVAEEAARLSVAAQEAARLRQLAE-EDLAQQRALAEKMLKEKMQAVQEAtrlKAEAE 2304
Cdd:COG3524 242 S-YLSPNSPQVRQLRRRIAALeKQIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAALEQA---RIEAA 317
|
....*....
gi 1920237982 2305 llQQQKELA 2313
Cdd:COG3524 318 --RQQRYLA 324
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1394-1768 |
1.57e-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: 47.58 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1394 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEAT----ERQRGGAEGELQALRARAEEAEAQKRQAQEE 1469
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1470 AERL---RRQVQDETQRKRQAEAELALRVQAEAEAAREKQralQALEELRLQAEEAERRLRQAEAERaRQVQVALETAQ- 1545
Cdd:pfam07888 110 SEELseeKDALLAQRAAHEARIRELEEDIKTLTQRVLERE---TELERMKERAKKAGAQRKEEEAER-KQLQAKLQQTEe 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1546 --RSAEAELQSEHASFAEKTAQLERtLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKAnEALRLRLqaE 1623
Cdd:pfam07888 186 elRSLSKEFQELRNSLAQRDTQVLQ-LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV-EGLGEEL--S 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1624 EVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR 1703
Cdd:pfam07888 262 SMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237982 1704 QLLEEELArlqREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSE---KSKQRLEAEAG 1768
Cdd:pfam07888 342 EKLEVELG---REKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEyirQLEQRLETVAD 406
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1655-1850 |
1.60e-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: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1655 EQAVRQRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1731
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1732 AKVRAEMEVLLASKA--------------RAEEESRSTSEKSK-QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1796
Cdd:COG3206 250 GSGPDALPELLQSPViqqlraqlaeleaeLAELSARYTPNHPDvIALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 1797 DAVRQRAEAERVLAEKLAAIS-EATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 1850
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEaELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3940-3974 |
1.62e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.62e-04
10 20 30
....*....|....*....|....*....|....*
gi 1920237982 3940 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 3974
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1284-1495 |
1.64e-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: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1284 ESIIQEYVDLRTRYSelSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERL------AEVEAALEKQRQLAEAHAQAK 1357
Cdd:COG3206 155 NALAEAYLEQNLELR--REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlsEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1358 AQAeREAQGLQRRMQEEVARREEVAVEA-------------QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRI 1424
Cdd:COG3206 233 AEL-AEAEARLAALRAQLGSGPDALPELlqspviqqlraqlAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 1425 EEEIRVVRLQLEATERQRGGAEGELQALRARAE---EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRV 1495
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQRLEEARLAEALTV 385
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2148-2537 |
1.71e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2148 AEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVT--EAARQRGQVEEELFSLRVQMEELGKLKARIEAEN 2225
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2226 RALVlRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKekmQAVQEATRLKAEAEL 2305
Cdd:COG4717 156 EELR-ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE---EAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2306 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLET----------------------ERQRQLEMSAEAERLRLRV 2363
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSliltiagvlflvlgllallfllLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2364 AEMSRAQARAEEDARRFRKQAEDIGER---LYRTELATQEKVMLVQTLETQRQQSDRDAER---LREAIAELEHEKDKLK 2437
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEElleLLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2438 QEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQ 2517
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
410 420
....*....|....*....|
gi 1920237982 2518 EKQQLAASMEEARRRQHEAE 2537
Cdd:COG4717 472 AELLQELEELKAELRELAEE 491
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1686-1836 |
1.76e-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: 46.46 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1686 EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRS-TSEKSKQRLE 1764
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvRNNKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 1765 AE----AGRFRELAEEAARLRALAEEAKRQRQLAEEdavrQRAEAERVLAEKLAAISEATRlKTEAEIALKEKEAE 1836
Cdd:COG1579 96 KEieslKRRISDLEDEILELMERIEELEEELAELEA----ELAELEAELEEKKAELDEELA-ELEAELEELEAERE 166
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2148-2582 |
1.84e-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: 48.02 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2148 AEQALRQKAQVEQELTALRLQL-------EETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLK-A 2219
Cdd:COG3096 524 LEQRLRQQQNAERLLEEFCQRIgqqldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApA 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2220 RIEAENRALVLRD------KDSA------QRLLQEE----------AEKMKQVAEEAARLSVAA-QEAARLRQLAE---- 2272
Cdd:COG3096 604 WLAAQDALERLREqsgealADSQevtaamQQLLEREreatverdelAARKQALESQIERLSQPGgAEDPRLLALAErlgg 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2273 -------EDLAQQRA-LAEKMLKEKMQA--VQEATRLKAEAE----------LLQQQKELAQEQARRLQEDKEQMAQQLA 2332
Cdd:COG3096 684 vllseiyDDVTLEDApYFSALYGPARHAivVPDLSAVKEQLAgledcpedlyLIEGDPDSFDDSVFDAEELEDAVVVKLS 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2333 QETQGFQKTLE------TERQRQLE-MSAEAERLRLRVAEMS---RAQARAEEDARRFrkqaedIGERLYRTELATQEKV 2402
Cdd:COG3096 764 DRQWRYSRFPEvplfgrAAREKRLEeLRAERDELAEQYAKASfdvQKLQRLHQAFSQF------VGGHLAVAFAPDPEAE 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2403 MlvQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQsflsEKDSLLQRERC 2482
Cdd:COG3096 838 L--AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELRE----ELDAAQEAQAF 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2483 IEQEKAKLEQLfqdeVAKAQALReeqqrqqqQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLA 2562
Cdd:COG3096 912 IQQHGKALAQL----EPLVAVLQ--------SDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLL 979
|
490 500
....*....|....*....|....
gi 1920237982 2563 EENQ----RLRERLQHLEEERRAA 2582
Cdd:COG3096 980 GENSdlneKLRARLEQAEEARREA 1003
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1768-2014 |
2.00e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1768 GRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 1847
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1848 AFQRRLLEEQAAQHKADIE------ARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELE 1921
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIReleediKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1922 LGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAeervqKSLAAEEEAARQRKAALEE-VERLKAKVEEARRLRE 2000
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN-----EALLEELRSLQERLNASERkVEGLGEELSSMAAQRD 268
|
250
....*....|....*
gi 1920237982 2001 RAEQESAR-QLQLAQ 2014
Cdd:pfam07888 269 RTQAELHQaRLQAAQ 283
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2152-2592 |
2.10e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2152 LRQKAQVEQ-ELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIeaenralvl 2230
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI--------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2231 RDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2310
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2311 ELAQEQARRLQEDKEQMAQQLAQET--QGFQKTLETERQRQLEMSAEAERLRlrvAEMSRAQARAEEDARRFRKQAEDIG 2388
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMdyNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2389 ERL--YRTELAT--QEKVMLVQTLETQRQQSD----------------------------RDAERLREAIAELEHEKDKL 2436
Cdd:PRK01156 416 VKLqdISSKVSSlnQRIRALRENLDELSRNMEmlngqsvcpvcgttlgeeksnhiinhynEKKSRLEEKIREIEIEVKDI 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2437 KQEAQLLQ-----LKSEEM-QTVRQEQLLQETQALQQSFLSE----KDSLLQRERCIEQEKA-KLEQLFQDEVAKAQALR 2505
Cdd:PRK01156 496 DEKIVDLKkrkeyLESEEInKSINEYNKIESARADLEDIKIKinelKDKHDKYEEIKNRYKSlKLEDLDSKRTSWLNALA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2506 EEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEG-----------VRRQQEELQRLaqqqqQQEKLLAEENQRLRERLQH 2574
Cdd:PRK01156 576 VISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGfpddksyidksIREIENEANNL-----NNKYNEIQENKILIEKLRG 650
|
490
....*....|....*...
gi 1920237982 2575 LEEERRAALARSEEIAPS 2592
Cdd:PRK01156 651 KIDNYKKQIAEIDSIIPD 668
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4249-4282 |
2.29e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.29e-04
10 20 30
....*....|....*....|....*....|....
gi 1920237982 4249 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4282
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2146-2592 |
2.29e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.21 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2146 QFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAEN 2225
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2226 RALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2305
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2306 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAE 2385
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2386 DIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQAL 2465
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2466 QQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQE 2545
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1920237982 2546 ELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIAPS 2592
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2351-2585 |
2.49e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2351 EMSAEAERLRLRVAEMSRAQARAEeDARRFRKQAEDIgERLYRTELATQEKVMLVQTLETQRQ--QSDRDAERLREAIAE 2428
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALE-DAREQIELLEPI-RELAERYAAARERLAELEYLRAALRlwFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2429 LEHEKDKLKQEAQLLQLKSEEMQtvrqEQLLQETQALQQSFLSEKDSLlqrERCIEQEKAKLEQLFQdevaKAQALREEQ 2508
Cdd:COG4913 300 LRAELARLEAELERLEARLDALR----EELDELEAQIRGNGGDRLEQL---EREIERLERELEERER----RRARLEALL 368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237982 2509 QRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQqqqekllaeenQRLRERLQHLEEERRAALAR 2585
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL-----------RDLRRELRELEAEIASLERR 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1284-1628 |
2.66e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1284 ESIIQEYVDLRTRYSELST---LTSQYIRFISETLRRMEEEERLAE-QQRAEE-RERLAEVEAALEKQRQLAEAHAQAKA 1358
Cdd:COG4717 98 EELEEELEELEAELEELREeleKLEKLLQLLPLYQELEALEAELAElPERLEElEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1359 QAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQ---- 1434
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE----ELEELEEELEQLENELEAAALEERLKEARllll 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1435 --------------LEATERQRGGA----EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQ 1496
Cdd:COG4717 254 iaaallallglggsLLSLILTIAGVlflvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1497 AEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV----------------------QVALETAQRSAEAELQS 1554
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagvedeeelraaleqaeeYQELKEELEELEEQLEE 413
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 1555 -----EHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKAnEALRLRLQAEEVAQQ 1628
Cdd:COG4717 414 llgelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQ-ELEELKAELRELAEE 491
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1447-1669 |
2.68e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1447 GELQALRARAEEAEAQ-KRQAQEEAERLRRQVQDETQRKRQAEAElalRVQAEAEAAREKQRALQALEELRlQAEEAERR 1525
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQrKKKEQQQAEELQQKQAAEQERLKQLEKE---RLAAQEQKKQAEEAAKQAALKQK-QAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1526 LRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAtrraqqqaeaeraraeaerel 1605
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA--------------------- 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 1606 erwQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELE 1669
Cdd:PRK09510 200 ---KKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2353-2601 |
2.76e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2353 SAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHE 2432
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2433 KDKLKQEAQLLQLKSEEMQTVRQEQLLqetqaLQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQ 2512
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALL-----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2513 QqmqqEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIAPS 2592
Cdd:COG4942 174 A----ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
....*....
gi 1920237982 2593 RAAAARALP 2601
Cdd:COG4942 250 ALKGKLPWP 258
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1652-1864 |
3.01e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1652 KAEEQAVRQRELAEQ-----ELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQRQLLEEElarlqreaaaatqkRRE 1726
Cdd:NF012221 1555 DAAQNALADKERAEAdrqrlEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQRDAILEE--------------SRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1727 LEAELAKVRAEMEVLLAS-------------------KARAEEESRSTSEKSKQRLEAEAGRF----RELAEEAARLRAL 1783
Cdd:NF012221 1618 VTKELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLDDAKKISGKQLADAKQRHvdnqQKVKDAVAKSEAG 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1784 AEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRlLEEQAAQHKA 1863
Cdd:NF012221 1698 VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ-ADAKGAKQDE 1776
|
.
gi 1920237982 1864 D 1864
Cdd:NF012221 1777 S 1777
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1346-1525 |
3.09e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1346 QRQLAEAHAQAK---AQAEREAQglqrrmqeevARREEVAVEAqeqkrsiQEELQHLRQSSEAEIQAKARQVEAAERsRL 1422
Cdd:PRK12704 30 EAKIKEAEEEAKrilEEAKKEAE----------AIKKEALLEA-------KEEIHKLRNEFEKELRERRNELQKLEK-RL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1423 RIEEEIrvVRLQLEATERQRGGAEGELQALRARAEEAEAQkrqaQEEAERLRRQVQDETQR---KRQAEAELALRVQAEA 1499
Cdd:PRK12704 92 LQKEEN--LDRKLELLEKREEELEKKEKELEQKQQELEKK----EEELEELIEEQLQELERisgLTAEEAKEILLEKVEE 165
|
170 180
....*....|....*....|....*..
gi 1920237982 1500 EAAREKQRALQALEElrlQA-EEAERR 1525
Cdd:PRK12704 166 EARHEAAVLIKEIEE---EAkEEADKK 189
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1652-1845 |
3.16e-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: 46.45 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1652 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1731
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1732 AKVRAEMEVLLASKARAEEESRsTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAE 1811
Cdd:pfam13868 229 KKARQRQELQQAREEQIELKER-RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRA 307
|
170 180 190
....*....|....*....|....*....|....
gi 1920237982 1812 KLAAISEATRLKTEAEIALKEKEAENERLRRLAE 1845
Cdd:pfam13868 308 AEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
923-1584 |
3.18e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 923 EDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRITEQQK 1002
Cdd:pfam02463 293 KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1003 AQAEVDGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAH 1082
Cdd:pfam02463 373 EELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1083 EEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQE-------VGERLQQRHGERDVEVERWRERV 1155
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKEskarsglKVLLALIKDGVGGRIISAHGRLG 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1156 TLLLERWQAVLAQTDVRQRELEQLG-----RQLRYYRESADPLGAWLRDAKQRQEQIQAVPLA---NSQAVREQLRQEKA 1227
Cdd:pfam02463 533 DLGVAVENYKVAISTAVIVEVSATAdeveeRQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleIDPILNLAQLDKAT 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1228 LLEDIERHGEKV----EECQRFAKQYINAiKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTL 1303
Cdd:pfam02463 613 LEADEDDKRAKVvegiLKDTELTKLKESA-KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1304 TSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGL-QRRMQEEVARREEVA 1382
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSrLKKEEKEEEKSELSL 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1383 VEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrLQLEATERQRGGAEGELQALRARAEEAEAQ 1462
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLE---EEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1463 KRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALE 1542
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1920237982 1543 TAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEA 1584
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKE 970
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2131-2305 |
3.32e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2131 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEE---LFSL 2207
Cdd:PRK09510 80 QRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEakrAAAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2208 RVQMEELGKLKARIEAENRALVLRDK----DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAE 2283
Cdd:PRK09510 160 AKKAAAEAKKKAEAEAAKKAAAEAKKkaeaEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAE 239
|
170 180
....*....|....*....|..
gi 1920237982 2284 KmlKEKMQAVQEATRLKAEAEL 2305
Cdd:PRK09510 240 K--AAAAKAAEKAAAAKAAAEV 259
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1743-1940 |
3.41e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1743 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQrqlaEEDAVRQRAEAERVLAEKLAAISEATRL 1822
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1823 KTEAEIALKEKEAENerlrrlAEDEAfQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEIL 1902
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|....*...
gi 1920237982 1903 ALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAE 1940
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2138-2334 |
3.81e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2138 DAEMEKHKQFAEQALR---QKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQR------GQVEEELFSLR 2208
Cdd:PRK11281 55 EAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2209 VQMEELGklKARIEAENRALVLRDK--------DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAeedLAQQRA 2280
Cdd:PRK11281 135 DQLQNAQ--NDLAEYNSQLVSLQTQperaqaalYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQAL---LNAQND 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2281 LAEKMLK--EKMQAVQEATR--LKAEAELLQQQKELAQE--QARRLQEDKEQMAQQLAQE 2334
Cdd:PRK11281 210 LQRKSLEgnTQLQDLLQKQRdyLTARIQRLEHQLQLLQEaiNSKRLTLSEKTVQEAQSQD 269
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2991-3028 |
3.82e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 3.82e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1920237982 2991 RRALRGSGVIAGVWLEEAGQKLSIYEALRKDLLQPEAA 3028
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1655-1902 |
3.87e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.21 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1655 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLEEELARLQR-------EAAAATQKRREL 1727
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLEQENRRLQAlseeqaaELAELTRRLAEL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1728 EAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEAGRFR-ELAEEAARLRALAEEAKRQRQLAEE--DAVRQRAE 1804
Cdd:pfam19220 201 ETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMKLEALTARAAATEQLLAEarNQLRDRDE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1805 AERVLAEKLaaiSEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQK 1884
Cdd:pfam19220 277 AIRAAERRL---KEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSD 353
|
250
....*....|....*...
gi 1920237982 1885 GLveDTLRQRRQVEEEIL 1902
Cdd:pfam19220 354 RI--AELTKRFEVERAAL 369
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1652-1823 |
3.94e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.93 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1652 KAEEQAVRQR-ELAEQElekqrqlaegtAQQRLaaEQELIRLRAETEqgEQQRQLLeeelarlqreaaaatqkrrELEAE 1730
Cdd:PTZ00491 662 KSQEAAARHQaELLEQE-----------ARGRL--ERQKMHDKAKAE--EQRTKLL-------------------ELQAE 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1731 LAKVRAemevllASKARAEEESRSTSEKSKQRLEAEAGRFRelaEEAARLRALAE-EAKRQRQLAEEDAVRQRAEAERVL 1809
Cdd:PTZ00491 708 SAAVES------SGQSRAEALAEAEARLIEAEAEVEQAELR---AKALRIEAEAElEKLRKRQELELEYEQAQNELEIAK 778
|
170
....*....|....
gi 1920237982 1810 AEKLAAIsEATRLK 1823
Cdd:PTZ00491 779 AKELADI-EATKFE 791
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1651-1832 |
4.08e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1651 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQREAAAATQKRRELEA 1729
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1730 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEAGRF-RELAEEAARLRALAEEAKRQRQLAEEDavrqrAEAERV 1808
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLE-----HSGELV 511
|
170 180
....*....|....*....|....
gi 1920237982 1809 LAEKLAAISEATRLKTEAEIALKE 1832
Cdd:COG2433 512 PVKVVEKFTKEAIRRLEEEYGLKE 535
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1384-1519 |
4.09e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.81 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1384 EAQEQKRSIQEELQHLRQSS--EAEIQAKARQVEAAERSRLRIEEEI-RVVRLQleateRQRGGAEGELQALRARAEEAE 1460
Cdd:COG1566 87 QAEAQLAAAEAQLARLEAELgaEAEIAAAEAQLAAAQAQLDLAQRELeRYQALY-----KKGAVSQQELDEARAALDAAQ 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 1461 AQKRQAQEEAERLRRQVQDETQrKRQAEAELAlrvQAEAEAAREKQRalqaLEELRLQA 1519
Cdd:COG1566 162 AQLEAAQAQLAQAQAGLREEEE-LAAAQAQVA---QAEAALAQAELN----LARTTIRA 212
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1659-2375 |
4.33e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.72 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1659 RQRELAEQEleKQRQLAEGTAQQRLAAEQ-ELIRLRAeTEQGEQQRQLLEeelaRLQREAAAATQKRR---ELEAELAKV 1734
Cdd:PRK10246 251 RLDELQQEA--SRRQQALQQALAAEEKAQpQLAALSL-AQPARQLRPHWE----RIQEQSAALAHTRQqieEVNTRLQST 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1735 RAEMEVLLASKARAEEESRSTSEKSKQRLeAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAVRQRAEAERvlaEKLA 1814
Cdd:PRK10246 324 MALRARIRHHAAKQSAELQAQQQSLNTWL-AEHDRFRQWNNELAGWRAQFSQQTSDRE--QLRQWQQQLTHAE---QKLN 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1815 AISEATRLKTEAEIAlkekeaenERLRRLAEDEAFQRRLLEEQaAQHkADIEARLAQLrKASESELERQKGLVEDTLRQR 1894
Cdd:PRK10246 398 ALPAITLTLTADEVA--------AALAQHAEQRPLRQRLVALH-GQI-VPQQKRLAQL-QVAIQNVTQEQTQRNAALNEM 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1895 RQVEEEilalkgsfekaaagKAElelELGRIRGTAEDTLRSKEQAEQEAarQRQLAAEEERRRREAEERVQKSLAAEEEA 1974
Cdd:PRK10246 467 RQRYKE--------------KTQ---QLADVKTICEQEARIKDLEAQRA--QLQAGQPCPLCGSTSHPAVEAYQALEPGV 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1975 ARQRKAALE-EVERLKakvEEARRLRERAEQeSARQLQLAQEAAQkRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERL 2053
Cdd:PRK10246 528 NQSRLDALEkEVKKLG---EEGAALRGQLDA-LTKQLQRDESEAQ-SLRQEEQALTQQWQAVCASLNITLQPQDDIQPWL 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2054 rseaeaarraaeeaeaareraereaaqsrrqvEEAERLKQsaeeqaqaqaqaqaaaeklrkeaeqeaarraqaEQAALRQ 2133
Cdd:PRK10246 603 --------------------------------DAQEEHER---------------------------------QLRLLSQ 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2134 KQAADAEMEKH----KQFAEQALRQKAQVEQELTALRLQLEETDHQKSIL---DEELQRLKAEVTEAARQRGQVE--EEL 2204
Cdd:PRK10246 618 RHELQGQIAAHnqqiIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLatrQQEAQSWQQRQNELTALQNRIQqlTPL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2205 FSLRVQMEELGKLKARIEAEN------RALVLRDKDSA--QRLLQEEAEKMKQVAEEAARL--SVAAQEAARLRQLAEED 2274
Cdd:PRK10246 698 LETLPQSDDLPHSEETVALDNwrqvheQCLSLHSQLQTlqQQDVLEAQRLQKAQAQFDTALqaSVFDDQQAFLAALLDEE 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2275 LAQQralAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQK--TLETERQRQLEM 2352
Cdd:PRK10246 778 TLTQ---LEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLREntTRQGEIRQQLKQ 854
|
730 740
....*....|....*....|....
gi 1920237982 2353 SAEA-ERLRLRVAEMSRAQARAEE 2375
Cdd:PRK10246 855 DADNrQQQQALMQQIAQATQQVED 878
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3399-3435 |
4.34e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.34e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1920237982 3399 KLLSAEKAVTGYRDPYSGSTISLFQAMKKGLVLREHG 3435
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1292-1572 |
4.39e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.43 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1292 DLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQrAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRM 1371
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEEL-SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1372 QEEVARREEVAVEAQEQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGE 1448
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEelrSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1449 LQALRARAEEAEAQKRQAQ------EEAERLRRQVQDETQRKRQAEAELALRVQAEAEAARE-KQRALQALEELRLQAE- 1520
Cdd:pfam07888 236 LEELRSLQERLNASERKVEglgeelSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREgRARWAQERETLQQSAEa 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1920237982 1521 EAERRLRQAEAERARQVQVALETAQR-SAEAELQSEHASFAEKTAQLERTLKE 1572
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERMEReKLEVELGREKDCNRVQLSESRRELQE 368
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2231-2401 |
4.40e-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: 45.99 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2231 RDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATR-LKAEAELLQQQ 2309
Cdd:TIGR02794 65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAkAKAEAEAERKA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2310 KELAQEQARrlqEDKEQMAQQLAQetqgfQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGE 2389
Cdd:TIGR02794 145 KEEAAKQAE---EEAKAKAAAEAK-----KKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAE 216
|
170
....*....|..
gi 1920237982 2390 RLYRTELATQEK 2401
Cdd:TIGR02794 217 AAAAAAAEAERK 228
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1344-1475 |
4.44e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 43.88 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1344 EKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHL--RQSSEAEIQAKARQVEAAERSR 1421
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeeERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 1422 LRIEEEIRVVRLQLEATERQRGGAEGELQalraraeeaEAQKRQAQEEAERLRR 1475
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER 135
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1406-1573 |
4.54e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1406 EIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQvQDETQRKR 1485
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1486 QAEAelalrVQAEAEAAREKQRAL-QALEELRLQAEEAERRLRQAEAERARQVQ--VALETAQRSAEAELQSEHASFAEK 1562
Cdd:COG1579 90 EYEA-----LQKEIESLKRRISDLeDEILELMERIEELEEELAELEAELAELEAelEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|.
gi 1920237982 1563 TAQLERTLKEE 1573
Cdd:COG1579 165 REELAAKIPPE 175
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1652-1881 |
4.67e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1652 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEEL--------ARLQR 1715
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARpdnsaviaAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1716 EAAAATQKRRELEAE-----LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrelaeeAARLRALAeeAKRQ 1790
Cdd:PRK05035 527 KAQARARQAEKQAAAaadpkKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVA---------AAIARAKA--KKAA 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1791 RQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAedeafqrrlleeqAAQHKAdiEARLA 1870
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVA-------------AAIARA--KARKA 660
|
250
....*....|.
gi 1920237982 1871 QLRKASESELE 1881
Cdd:PRK05035 661 AQQQANAEPEE 671
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1576-2031 |
4.87e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 46.55 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1576 AVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEE 1655
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1656 QAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVR 1735
Cdd:COG3903 557 LRGLLRE-GRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAA 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1736 AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAA 1815
Cdd:COG3903 636 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAA 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1816 ISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRR 1895
Cdd:COG3903 716 AAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAA 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1896 QVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAA 1975
Cdd:COG3903 796 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAA 875
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 1976 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFA 2031
Cdd:COG3903 876 AAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2418-2548 |
4.89e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2418 DAERLREAIAELEHEKDKLKQEAQLLqlkseemqtvrqEQLLQETQALQQSFLSEKDSLLQRErciEQEKAKLEQLFQDE 2497
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEA------------EALLKEAEKLKEELEEKKEKLQEEE---DKLLEEAEKEAQQA 578
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2498 V--AKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGV-------RRQQEELQ 2548
Cdd:PRK00409 579 IkeAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKekkkkkqKEKQEELK 638
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1402-1536 |
5.13e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.44 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1402 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQVQDET 1481
Cdd:PRK12678 69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARR-GAARKAGE 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 1482 QRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQ 1536
Cdd:PRK12678 148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDD 202
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1319-1584 |
5.14e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 46.57 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1319 EEEERLAEQQRAEERER----------LAEVEAALEKQR---QLAEAHAQAKAQAEREAQGLQRR----MQEEVARREEV 1381
Cdd:PRK10811 507 EEAMALPSEEEFAERKRpeqpalatfaMPDVPPAPTPAEpaaPVVAAAPKAAAATPPAQPGLLSRffgaLKALFSGGEET 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1382 AVEAQEQKRSIQEElqhlRQSSEaeiQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEA 1461
Cdd:PRK10811 587 KPQEQPAPKAEAKP----ERQQD---RRKPRQNNRRDRNERRDTRDNRTRREGRENREENRRNRRQAQQQTAETRESQQA 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1462 QKRQAQEEAERLRRQVQDETQRKRQAEAELAlrvQAEAEAarekqralQALEELRLQAEEAERRLRQAEAERAR------ 1535
Cdd:PRK10811 660 EVTEKARTQDEQQQAPRRERQRRRNDEKRQA---QQEAKA--------LNVEEQSVQETEQEERVQQVQPRRKQrqlnqk 728
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 1536 ---QVQVALETAQRSAEAELQSEHASfAEKTAQLERTLKEEHVAVVQLREEA 1584
Cdd:PRK10811 729 vriEQSVAEEAVAPVVEETVAAEPVV-QEVPAPRTELVKVPLPVVAQTAPEQ 779
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1393-1751 |
5.43e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1393 QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1472
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1473 LRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAEL 1552
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1553 QSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLT 1632
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1633 QAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR 1712
Cdd:COG4372 252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
330 340 350
....*....|....*....|....*....|....*....
gi 1920237982 1713 LQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE 1751
Cdd:COG4372 332 LAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3360-3395 |
5.66e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.66e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1920237982 3360 TLLLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPE 3395
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2258-2536 |
5.79e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 46.37 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2258 SVAAQEAARLRQLAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmAQQLAqETQG 2337
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK---QQQLA-AISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2338 FQKTLETERQRQLEMSAEAERlrlrvaemsraqARAEEDARRFRKQAEDIGERLyrtelatqekvmlvQTLETQRQQSDR 2417
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR------------DAILEESRAVTKELTTLAQGL--------------DALDSQATYAGE 1641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2418 DAERLREAIAE--LEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSllqrerciEQEKAKLEQLFQ 2495
Cdd:NF012221 1642 SGDQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG--------EQNQANAEQDID 1713
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1920237982 2496 DEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRR-QHEA 2536
Cdd:NF012221 1714 DAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3031-3064 |
6.12e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 6.12e-04
10 20 30
....*....|....*....|....*....|....
gi 1920237982 3031 LLEAQAGTGHIIDPTTSARLTVDEAVRAGLVGPE 3064
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1642-1805 |
6.13e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.63 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1642 EAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREaaaat 1721
Cdd:COG2268 229 EQEREIETARIAEAEAELAKKKAEERREAETARAE---AEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAE----- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1722 QKRRELEAELaKVRAEmevllASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEedAVRQ 1801
Cdd:COG2268 301 REEAELEADV-RKPAE-----AEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE--IAEA 372
|
....
gi 1920237982 1802 RAEA 1805
Cdd:COG2268 373 AAKP 376
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1680-1948 |
6.59e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1680 QQRLAAEQELIRlraeteQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKS 1759
Cdd:PRK11637 53 QQDIAAKEKSVR------QQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1760 KQRLEAEagrFRELAEEAARLRALAEEAKRqrqlaeedavrqraeAERVLAeKLAAISEAtRLKTEAEialkekeaener 1839
Cdd:PRK11637 127 AAQLDAA---FRQGEHTGLQLILSGEESQR---------------GERILA-YFGYLNQA-RQETIAE------------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1840 LRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVedtlrqrrqveeeilALKGSFEKAAAGKAELE 1919
Cdd:PRK11637 175 LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLT---------------GLESSLQKDQQQLSELR 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 1920237982 1920 LELGRIRGT-AEDTLRSKEQAEQEA-------ARQRQ 1948
Cdd:PRK11637 240 ANESRLRDSiARAEREAKARAEREAreaarvrDKQKQ 276
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
21-134 |
6.61e-04 |
|
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: 42.41 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 21 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerdvIRSSRLPREKGRmrfHKLQNVQIALDYL 100
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVP-----LHSFHLTPTSFE---QKVHNVQFAFELM 87
|
90 100 110
....*....|....*....|....*....|....
gi 1920237982 101 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 134
Cdd:cd21306 88 QDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1651-1773 |
7.55e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1651 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQRQLLEEELARLQR-----EAAAATQKR 1724
Cdd:pfam17045 127 GKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRKQCLEASQSEIQRlrsklERAQDSLCA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 1725 RELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEAGRFREL 1773
Cdd:pfam17045 207 QELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1308-1572 |
7.79e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.91 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1308 IRFISETLRRMEEEERLAEQQRAEERERLAEV-EAALEKQRQLAEAHAQAKAQAEREaqglqrrmqeevarREEVAVEAQ 1386
Cdd:pfam00038 20 VRFLEQQNKLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLE--------------LDNLRLAAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1387 EQKRSIQEELQhLRQSSEAEIQAKARQVEAAERSRLRIEEEIrvvrlqleaterqrggaegelQALRaraEEAEAQKRQA 1466
Cdd:pfam00038 86 DFRQKYEDELN-LRTSAENDLVGLRKDLDEATLARVDLEAKI---------------------ESLK---EELAFLKKNH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1467 QEEAERLRRQVQDETQ-------RKRQAEAELA-LRVQAEAEAAREKQRA----LQALEELRLQAEEAERRLRQAEAERA 1534
Cdd:pfam00038 141 EEEVRELQAQVSDTQVnvemdaaRKLDLTSALAeIRAQYEEIAAKNREEAeewyQSKLEELQQAAARNGDALRSAKEEIT 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 1535 ---RQVQ-------------VALETAQRSAEAELQSEHASFAEKTAQLERTLKE 1572
Cdd:pfam00038 221 elrRTIQsleielqslkkqkASLERQLAETEERYELQLADYQELISELEAELQE 274
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1066-1721 |
7.90e-04 |
|
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: 45.87 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1066 SLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPE-LEATKAALKKLRAQAEAQqpvfdalRDELR-GAQEVGERLQQRHGE 1143
Cdd:pfam05483 158 NLLKETCARSAEKTKKYEYEREETRQVYMDLNNnIEKMILAFEELRVQAENA-------RLEMHfKLKEDHEKIQHLEEE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1144 RDVEVERWRERVTLLLerwqavlAQTDVRQRELEQLGRQLRYYRESADPLgawlrdakQRQEQIQAVPLANSQAVREQLR 1223
Cdd:pfam05483 231 YKKEINDKEKQVSLLL-------IQITEKENKMKDLTFLLEESRDKANQL--------EEKTKLQDENLKELIEKKDHLT 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1224 QEkalLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYK-AQLEPVASPAK---------KPKVQSGSESIIQEYVDL 1293
Cdd:pfam05483 296 KE---LEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeAQMEELNKAKAahsfvvtefEATTCSLEELLRTEQQRL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1294 RTRYSELSTLTSQYIRFISEtLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLaEAHAQAKAQAEREAQGLQRRMQE 1373
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSE-LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF-EKIAEELKGKEQELIFLLQAREK 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1374 EVARREEVAVEAQEQKRSIQEELQHLRQSSEAEiqaKARQVEAAERSRLRIEEEIRVVR------LQLEATERQRGGAEG 1447
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKE---KLKNIELTAHCDKLLLENKELTQeasdmtLELKKHQEDIINCKK 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1448 ELQALRARAEEAEAQKRQAQEEAERLRR---QVQDETQRKRQAEAELALRVQAEAEAAREKQRALQ-ALEELRLQAEEAE 1523
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREefiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEnKCNNLKKQIENKN 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1524 RRLRQAEAE-RARQVQVALETAQRSA--------EAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRaqqqaea 1594
Cdd:pfam05483 608 KNIEELHQEnKALKKKGSAENKQLNAyeikvnklELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKA------- 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1595 eraraeaerelerwQLKANEALRLRLQAEEVAQQKsltqaeaekqkEEAEREARRRGKAEEQAVRQRELAEQELEKQRQL 1674
Cdd:pfam05483 681 --------------KAIADEAVKLQKEIDKRCQHK-----------IAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQ 735
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1920237982 1675 AEGTAqqRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAT 1721
Cdd:pfam05483 736 EQSSA--KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1976-2465 |
7.95e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1976 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRS 2055
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2056 EAeaarraaeeaeaareraereaaqsrRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAArraqaeqaalRQKQ 2135
Cdd:COG4717 144 LP-------------------------ERLEELEERLEELRELEEELEELEAELAELQEELEELLE----------QLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2136 AADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKA-EVTEAARQRGQVEEELFSLRVQMEEL 2214
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeERLKEARLLLLIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2215 GKLKARI------EAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2288
Cdd:COG4717 269 LSLILTIagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2289 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKtleTERQRQLEMSAEAERLRLRVAEMSR 2368
Cdd:COG4717 349 LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQEL---KEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2369 AQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAER--LREAIAELEHEKDKLKQEAQLLQLK 2446
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELeeLKAELRELAEEWAALKLALELLEEA 505
|
490
....*....|....*....
gi 1920237982 2447 SEEMQTVRQEQLLQETQAL 2465
Cdd:COG4717 506 REEYREERLPPVLERASEY 524
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2154-2493 |
8.29e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2154 QKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVT-------EAARQRGQVEEELFSLRVQMEELGKLKARIEAENR 2226
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEklnnkynDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2227 AL-----VLRDKDSAQRLLQEEAEKMK----QVAEEAARLSVAAQEAARLRQLAEE---DLAQQRALAEKMLKEKMQAVQ 2294
Cdd:TIGR04523 198 KLelllsNLKKKIQKNKSLESQISELKkqnnQLKDNIEKKQQEINEKTTEISNTQTqlnQLKDEQNKIKKQLSEKQKELE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2295 EATR-----------LKAEAELLQQQKE---------LAQEQARRLQEDKEQMAQ------QLAQETQGFQKTLETERQR 2348
Cdd:TIGR04523 278 QNNKkikelekqlnqLKSEISDLNNQKEqdwnkelksELKNQEKKLEEIQNQISQnnkiisQLNEQISQLKKELTNSESE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2349 QLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAE 2428
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 2429 LEHEKDKLKQEAQLLQLKSEEMQTVRqEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQL 2493
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTR-ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2173-2334 |
8.52e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2173 DHQKSILDEELQRLKAEVTEAARQRGQVEEELfsLRVQMEELGKLKARieaenralvlRDKDSAQRLLQEEAEKMKQVAE 2252
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQ--ERLKQLEKERLAAQ----------EQKKQAEEAAKQAALKQKQAEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2253 EAARLSVAAQEAARLRQLAEEDLAQQrALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELAQEQArrlQEDKEQMAQ 2329
Cdd:PRK09510 137 AAAKAAAAAKAKAEAEAKRAAAAAKK-AAAEAKKKAEAEAAKKAaaeAKKKAEAEAAAKAAAEAKKKA---EAEAKKKAA 212
|
....*
gi 1920237982 2330 QLAQE 2334
Cdd:PRK09510 213 AEAKK 217
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1652-2033 |
8.58e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.42 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1652 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1731
Cdd:COG3064 20 QAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1732 AKVRAEMEVLLASKARAEEESRSTSEKSK--QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVL 1809
Cdd:COG3064 100 AAKEAEAAAAAEKAAAAAEKEKAEEAKRKaeEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1810 AEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVED 1889
Cdd:COG3064 180 AALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1890 TLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLA 1969
Cdd:COG3064 260 LGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEA 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 1970 AEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQ 2033
Cdd:COG3064 340 ALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGL 403
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1316-1504 |
8.83e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.67 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1316 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEE 1395
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARA-AAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1396 LQHLRQSSEAEIQAKARQVEAAERSRLRieeeiRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1475
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAE-----AERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRR 231
|
170 180
....*....|....*....|....*....
gi 1920237982 1476 QVQDETQRKRQAEAELALRVQAEAEAARE 1504
Cdd:PRK12678 232 RRDRRDARGDDNREDRGDRDGDDGEGRGG 260
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
1994-2445 |
9.05e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 45.73 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1994 EARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARER 2073
Cdd:COG4995 3 ALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2074 AEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALR 2153
Cdd:COG4995 83 AALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2154 QKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDK 2233
Cdd:COG4995 163 AALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2234 DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELA 2313
Cdd:COG4995 243 LAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2314 QEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYR 2393
Cdd:COG4995 323 LLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLA 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 2394 TELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQL 2445
Cdd:COG4995 403 LAAAQLLRLLLAALALLLALAAYAAARLALLALIEYIILPDRLYAFVQLYQL 454
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2135-2458 |
9.15e-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: 44.91 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2135 QAADAEMEKHKQFAEQALRQKAQVEQELtalRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEEL 2214
Cdd:pfam13868 16 LAAKCNKERDAQIAEKKRIKAEEKEEER---RLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2215 GKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ 2294
Cdd:pfam13868 93 YEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDE-FNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2295 EATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLAQETQGF---QKTLETERQRQLEMSAEAERLRLRVAEMSRA 2369
Cdd:pfam13868 172 EAEREEIEEEKEREIARLRaqQEKAQDEKAERDELRAKLYQEEQERkerQKEREEAEKKARQRQELQQAREEQIELKERR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2370 QARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQtLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEE 2449
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKR-LEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRER 330
|
....*....
gi 1920237982 2450 MQTVRQEQL 2458
Cdd:pfam13868 331 IEEERQKKL 339
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1317-1433 |
9.39e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1317 RMEEEERLAEQQRAEERERLAEVEA---ALEKQ-RQLAEAHAQAKAQAEREAQGLQRRMQEEVAR-----REEVAVEAQE 1387
Cdd:PRK00409 524 SLEELERELEQKAEEAEALLKEAEKlkeELEEKkEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiikelRQLQKGGYAS 603
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237982 1388 QKRS-IQEELQHLRQSSEAEIQAKARQVEAAErsRLRIEEEIRVVRL 1433
Cdd:PRK00409 604 VKAHeLIEARKRLNKANEKKEKKKKKQKEKQE--ELKVGDEVKYLSL 648
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2134-2422 |
9.72e-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: 45.71 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2134 KQAADAEMEKHKQFaEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAaRQRGQVEEELfslRVQMEE 2213
Cdd:COG3096 402 QQALDVQQTRAIQY-QQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLEL-EQKLSVADAA---RRQFEK 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2214 LGKLKARIEAEnralVLRDK--DSAQRLLQEEAEKMKQvaeeAARLSVAAQEAARLRQLAEEdlaQQRA--LAEKMLKEK 2289
Cdd:COG3096 477 AYELVCKIAGE----VERSQawQTARELLRRYRSQQAL----AQRLQQLRAQLAELEQRLRQ---QQNAerLLEEFCQRI 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2290 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaQETQGFQKTLETERQRQLEMSAEAERLRlrvaEMSRA 2369
Cdd:COG3096 546 GQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL-EQLRARIKELAARAPAWLAAQDALERLR----EQSGE 620
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1920237982 2370 QARAEEDARRFRKQAedigerLYRTELATQEKvmlvQTLETQRQQSDRDAERL 2422
Cdd:COG3096 621 ALADSQEVTAAMQQL------LEREREATVER----DELAARKQALESQIERL 663
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1655-1936 |
1.01e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1655 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1734
Cdd:COG4372 69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1735 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLA 1814
Cdd:COG4372 149 EEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1815 AISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQR 1894
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1920237982 1895 RQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSK 1936
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1325-1486 |
1.02e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.28 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1325 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE 1404
Cdd:PRK12678 65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1405 AEIQAKARQVEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEaERLRRQVQDETQRK 1484
Cdd:PRK12678 145 AGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRR 215
|
..
gi 1920237982 1485 RQ 1486
Cdd:PRK12678 216 EE 217
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4359-4396 |
1.10e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.10e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1920237982 4359 QRFLEVQYLTGGLIEPDTPGRVALDEALQRGTVDARTA 4396
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1308-1551 |
1.13e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1308 IRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQE 1387
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1388 QKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALR-------AraeEAE 1460
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKaeleaakA---ELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1461 AQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVA 1540
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
250
....*....|.
gi 1920237982 1541 LETAQRSAEAE 1551
Cdd:COG3883 255 AGAAAGSAGAA 265
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2345-2590 |
1.14e-03 |
|
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: 45.43 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2345 ERQRQLEMSAEA-ERLRLRVAEMSRAQARAEEDARRFRKQAEdigerlYRTELATQEKVMLVQTLETQRQQsdrdAERLR 2423
Cdd:TIGR02168 176 ETERKLERTRENlDRLEDILNELERQLKSLERQAEKAERYKE------LKAELRELELALLVLRLEELREE----LEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2424 EAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEqlLQETQALQQSFLSEKDSLLQR-ERCIEQEKAKLEQLFQDEVAKAQ 2502
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSE--LEEEIEELQKELYALANEISRlEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2503 ALREeqqrqqqqmqqekqqLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAA 2582
Cdd:TIGR02168 324 QLEE---------------LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
....*...
gi 1920237982 2583 LARSEEIA 2590
Cdd:TIGR02168 389 AQLELQIA 396
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
593-685 |
1.20e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.16 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 593 HGFVAAATKELMWLSDREEEEVGFDWSDRNTNMAAKKEGYSALMHELELKEKKIKEIQSTGDRLLREDHPARPTAESFQA 672
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1920237982 673 ALQTQWSWMLQLC 685
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1456-1840 |
1.23e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1456 AEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAR---EKQRALQALEELRLQAEEAERRLRQAEAE 1532
Cdd:PRK10929 104 TDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRqlnEIERRLQTLGTPNTPLAQAQLTALQAESA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1533 RARQVQVALETAQRSAE-----AELQSEhaSFAEKTAQLERTLkeehvavvqlreeatrraqqqaeaeraraeaereler 1607
Cdd:PRK10929 184 ALKALVDELELAQLSANnrqelARLRSE--LAKKRSQQLDAYL------------------------------------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1608 wqlkanEALRLRLQAEevaqqksltqaeaekqkeeaerearrrgkaeeqavRQRElAEQELEKQRQLAEGTAQQRLAAEQ 1687
Cdd:PRK10929 225 ------QALRNQLNSQ-----------------------------------RQRE-AERALESTELLAEQSGDLPKSIVA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1688 ELIRLRAETEQGEQQRQLLeEELARLQREAAAATQKRREleaELAKVRAEMEVLLASKARAE----EESRSTSEKSKQRL 1763
Cdd:PRK10929 263 QFKINRELSQALNQQAQRM-DLIASQQRQAASQTLQVRQ---ALNTLREQSQWLGVSNALGEalraQVARLPEMPKPQQL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1764 EAEAGRFRelaeeAARLR--ALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAA---------------ISEATRLK--- 1823
Cdd:PRK10929 339 DTEMAQLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTqrellnsllsggdtlILELTKLKvan 413
|
410
....*....|....*...
gi 1920237982 1824 TEAEIALKE-KEAENERL 1840
Cdd:PRK10929 414 SQLEDALKEvNEATHRYL 431
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1326-1453 |
1.24e-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: 44.11 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1326 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAqAEREaqglqRRMQEEVARREEVavEAQEQKRSIQEELQHLRQSSEA 1405
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKAEA-AEQE-----RKLLEEQQRELEQ--KLEDQERSYEEHLRQLKEKMEE 248
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1920237982 1406 EIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegELQALR 1453
Cdd:cd16269 249 ERENLLKEQERALESKLKEQEALLEEGFKEQAELLQE-----EIRSLK 291
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1449-1548 |
1.27e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.47 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1449 LQALRARAEEAE---AQKRQAQEEAERLRRQVQDEtQRKRQAEAElALRVQAEAEAAREKQRALQALEelrlqaEEAERR 1525
Cdd:COG0711 26 LKALDERQEKIAdglAEAERAKEEAEAALAEYEEK-LAEARAEAA-EIIAEARKEAEAIAEEAKAEAE------AEAERI 97
|
90 100
....*....|....*....|...
gi 1920237982 1526 LRQAEAERARQVQVALETAQRSA 1548
Cdd:COG0711 98 IAQAEAEIEQERAKALAELRAEV 120
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1651-2033 |
1.27e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 45.00 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1651 GKAEEQAVRQRELAEQELEK-----QRQLAEGTAQQRLAAEQELIRLRAE--TEQGEQQRQLLEEELARLQREAAAATQK 1723
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKilseiQKSLDKRKHTQNVALNKKLSDIKTEylYELNVLKEKSEAELTSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1724 RRELEAELAKVRAEMEVLLA-----SKARAEEESRSTSEKSKQRLEAEAGRFrELAEEAARLRALAEEAKRQRqlaEEDA 1798
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEeaekkAKDQKEEDRRNYPTNTYKTLELEIAES-DVEVKKAELELVKEEAKEPR---DEEK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1799 VRQrAEAErVLAEKlaaiSEATRLKteaEIALKEKEAENERLRRLaedEAFQRRLLEEQAAQHKADIEARLAqlRKASES 1878
Cdd:NF033838 206 IKQ-AKAK-VESKK----AEATRLE---KIKTDREKAEEEAKRRA---DAKLKEAVEKNVATSEQDKPKRRA--KRGVLG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1879 ELERQKGLVEDTLRQRRQVEEEIL---ALKGSFEKAAAGKAELELElGRIRGTAEDTLR-----SKEQAEQEAARqrqla 1950
Cdd:NF033838 272 EPATPDKKENDAKSSDSSVGEETLpspSLKPEKKVAEAEKKVEEAK-KKAKDQKEEDRRnyptnTYKTLELEIAE----- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1951 aeEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKA---KVEEARRLRERAEQESARQLQLAQEAAQKrlQAEEKA 2027
Cdd:NF033838 346 --SDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAeatRLEKIKTDRKKAEEEAKRKAAEEDKVKEK--PAEQPQ 421
|
....*.
gi 1920237982 2028 HAFAVQ 2033
Cdd:NF033838 422 PAPAPQ 427
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1384-1737 |
1.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1384 EAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQK 1463
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1464 RQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERA---RQVQVA 1540
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEslqEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1541 LETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRL 1620
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1621 QAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGE 1700
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
330 340 350
....*....|....*....|....*....|....*..
gi 1920237982 1701 QQRQLLEEELARLQREAAAATQKRRELEAELAKVRAE 1737
Cdd:COG4372 330 LALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAG 366
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2131-2588 |
1.35e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.12 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2131 LRQKQAADAEMEKHKQFAEQALRQKAQV----EQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2206
Cdd:pfam05557 78 NRLKKKYLEALNKKLNEKESQLADAREVisclKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2207 LRVQMEELGKLKARIEAENRALVLRDKDSaqrllqEEAEKMKqvaEEAARLSVAAQEAARLRqlaeEDLAQQRALAEKML 2286
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSQEQDS------EIVKNSK---SELARIPELEKELERLR----EHNKHLNENIENKL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2287 KEKMQAVQEATRLkaeaellqQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKT-------------LETERQRQLEMS 2353
Cdd:pfam05557 225 LLKEEVEDLKRKL--------EREEKYREEAATLELEKEKLEQELQSWVKLAQDTglnlrspedlsrrIEQLQQREIVLK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2354 AEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTE-----------LATQEKVMLVQTLE------TQRQQSD 2416
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKalvrrlqrrvlLLTKERDGYRAILEsydkelTMSNYSP 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2417 RDAERLREA----------IAELEHEKDKLKQEA----QLLQLKSEEMQTVRQeqllQETQALQQSFLSEKDSLLQRERC 2482
Cdd:pfam05557 377 QLLERIEEAedmtqkmqahNEEMEAQLSVAEEELggykQQAQTLERELQALRQ----QESLADPSYSKEEVDSLRRKLET 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2483 IEQEKAKLEQlfQDEVAKAQALREEQQRQQQQMQQEKQQLaasmeearrRQHEAEEGVRRQQEELQRLAqqqqqqeklla 2562
Cdd:pfam05557 453 LELERQRLRE--QKNELEMELERRCLQGDYDPKKTKVLHL---------SMNPAAEAYQQRKNQLEKLQ----------- 510
|
490 500
....*....|....*....|....*.
gi 1920237982 2563 EENQRLRERLQHLEEERRAALARSEE 2588
Cdd:pfam05557 511 AEIERLKRLLKKLEDDLEQVLRLPET 536
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1397-1685 |
1.37e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1397 QHLRQSsEAEIQAKARQVEAAERSRLRIEEeirvvrlqleateRQrggaegelqalrARAEeaeaqkRQAQEEAERLRRQ 1476
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA-------------RQ------------ARLE------REKAAREARHKKA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1477 VQDETQRKRQAEAELALRVQAEAEAAREK----------QRALQALEELR-LQAEEAERRLRQAEAERARQVQVALETAQ 1545
Cdd:PRK05035 477 AEARAAKDKDAVAAALARVKAKKAAATQPivikagarpdNSAVIAAREARkAQARARQAEKQAAAAADPKKAAVAAAIAR 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1546 RSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERElerwqlkANEALRLRLQAEEV 1625
Cdd:PRK05035 557 AKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKA-------AVAAAIARAKAKKA 629
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1626 AQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1685
Cdd:PRK05035 630 EQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2740-2776 |
1.41e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.41e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1920237982 2740 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVREHG 2776
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
24-248 |
1.47e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 44.93 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 24 KTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLSGDSLPRERDVIRSSRLPREKGRM-RFHKLQNVQIALDYLRH 102
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQ---LILLQALSKKLMPMTVTHKLVKKQPASGIEEnRFKAFENENYAVDLGIT 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 103 RQVKLVNIRNDDIADGNpKLTLGLIW-------TIILHFQISDiqvsgqsEDMTAKEKLLLWSQRMV------EGCQGLR 169
Cdd:COG5069 457 EGFSLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKD-------GCGLSDSDLCAWLGSLGlkgdkeEGIRSFG 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 170 CDNFTTSWRDGRLFNAIIHrhkPTLIDMNKVyRQTNLENLDQA-------FSVAERDLGVTRLLDPEDVDVPQPdEKSII 242
Cdd:COG5069 529 DPAGSVSGVFYLDVLKGIH---SELVDYDLV-TRGFTEFDDIAdarslaiSSKILRSLGAIIKFLPEDINGVRP-RLDVL 603
|
....*.
gi 1920237982 243 TYVSSL 248
Cdd:COG5069 604 TFIESL 609
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1321-1566 |
1.48e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.50 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1321 EERLAEQQRaEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQ----------EEVARREEVAVEAQEQKR 1390
Cdd:pfam07888 33 QNRLEECLQ-ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAelkeelrqsrEKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1391 SIQEE---LQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQ 1467
Cdd:pfam07888 112 ELSEEkdaLLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1468 EEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVAleTAQRS 1547
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA--AQRDR 269
|
250
....*....|....*....
gi 1920237982 1548 AEAELQSEHASFAEKTAQL 1566
Cdd:pfam07888 270 TQAELHQARLQAAQLTLQL 288
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1753-1901 |
1.51e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1753 RSTSEKSKQRLEAEAGRFRELAEEAArlralaEEAKRQRQL-AEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALK 1831
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 1832 EKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKasesELERQKGLVEDTLRQR--RQVEEEI 1901
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEA 167
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1333-1584 |
1.56e-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: 44.14 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1333 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKAR 1412
Cdd:pfam13868 12 NSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1413 QVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1492
Cdd:pfam13868 92 EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1493 LRVQAEAEAAREKQRAlqaleELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELqsehasfAEKTAQLERTLKE 1572
Cdd:pfam13868 172 EAEREEIEEEKEREIA-----RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREE-------AEKKARQRQELQQ 239
|
250
....*....|..
gi 1920237982 1573 EHVAVVQLREEA 1584
Cdd:pfam13868 240 AREEQIELKERR 251
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2184-2378 |
1.76e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.56 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2184 QRLKAEVTEAARQRGQVEEElfslrvqmeelgklkarieaenralvlrdkdsaQRLLQEEAEKMKQVAEEAARLSVAAQE 2263
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQ---------------------------------RRLQQEQLERAEKMREELELEQQRRFE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2264 AARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQQQKELAQEQARRLQEDKE---QMAQQLAQETQG 2337
Cdd:pfam15709 388 EIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQELQRKKQQEEAERAEAEKQrqkELEMQLAEEQKR 467
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1920237982 2338 FQKTLETERQRQLEMSAEAERLRLRVAEMSRaqARAEEDAR 2378
Cdd:pfam15709 468 LMEMAEEERLEYQRQKQEAEEKARLEAEERR--QKEEEAAR 506
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
2294-2372 |
1.89e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 43.93 E-value: 1.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 2294 QEATRLKAEAELLQQQKELAQEQArrlQEDKEQMAQQLAQETqgfqKTLETERQRQLEMSAEAERLRLRVAEMSRAQAR 2372
Cdd:PRK10920 60 QQAQNQTATNDALANQLTALQKAQ---ESQKQELEGILKQQA----KALDQANRQQAALAKQLDELQQKVATISGSDAK 131
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1434-1897 |
1.92e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1434 QLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALE 1513
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1514 ELRLQAEEAERRLRQAEAERARQVQValETAQRSAE--AELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQ 1591
Cdd:COG3064 97 KAKAAKEAEAAAAAEKAAAAAEKEKA--EEAKRKAEeeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1592 AEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1671
Cdd:COG3064 175 AAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1672 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE 1751
Cdd:COG3064 255 AAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1752 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALK 1831
Cdd:COG3064 335 ASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEA 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 1832 EKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQV 1897
Cdd:COG3064 415 ASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADL 480
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1319-1583 |
2.10e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.09 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1319 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREA-----------QGL-----------QRRMQEEVA 1376
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELkpsgqggldeeEAFldrtakreerrQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1377 RREEVAVEAQEQKRSIQEELQHlRQSSEAEIQAKARQVEaAERSRLRIEEEIRVVRL---QLEATERQRGGAEGELQALR 1453
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKEN-NEEEENSSWEKEEKRD-SRLGRYKEEETEIREKEyqeNKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1454 ARAEEAEAQKRQAQEEAERLRRQVQDE---------------TQRKRQA--EAELALRVQAEAEAAREKQRALQALE-EL 1515
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKIKKEKKvkyeskvfldqkrghPEVKSQNgeEEVTKLKVTTKRRQGGLSQSQEREEEaEV 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1516 RLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAE--KTAQLERTLKEEHVAVVQLREE 1583
Cdd:pfam02029 243 FLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREErrKLLEEEEQRRKQEEAERKLREE 312
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1325-1578 |
2.13e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1325 AEQQRAEERERlaeVEAALEkqrqlaEAHAQAKAQAEREAQGL---------------------QRRMQEEVARREEVAV 1383
Cdd:PHA03247 1586 AKQQRAEATDR---VTAALR------EALAAHERRAQSEAESLanlktllrvaaipataaktldQARSVAEIVDQIELLL 1656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1384 EAQEQKRSIQEE----LQHLRQSSEAEIQAKARQVEAAERSRLRieeeirvVRLQLEATERQRggaegeLQALRARAEEA 1459
Cdd:PHA03247 1657 EQTEKAAELDVAavdwLEHARRVFEAHPLTAARGGGPDPLARLH-------ARLDALGETRRR------TEALRRSLEAA 1723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1460 EAQKRQAQEEAERLRRQvqdetqrkrqaeaelALRVQAEAEAAREKQRALQALEE--LRLQAEEAERRLrqaeAERARQV 1537
Cdd:PHA03247 1724 EAEWDEVWGRFGRVRGG---------------AWKSPEALRAAREQLRALQTATNtvLGLRADAHYERL----PAKYQGA 1784
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1920237982 1538 qVALETAQRSAEAElqsEHASFAEKTAQLERTLKEEHVAVV 1578
Cdd:PHA03247 1785 -LGAKSAERAGAVE---ELGAAVARHDGLLARLREEVVARV 1821
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1393-1583 |
2.18e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 42.73 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1393 QEELQHLRQSSEAEIQakarqveaaersrlRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1472
Cdd:pfam15665 13 EAEIQALKEAHEEEIQ--------------QILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1473 LRRQVQDetqRKRQAEAELALRVQAEA----EAAREKQRALQALEELRLQAE-EAERRLRQAEAERARQVQVALETaqrs 1547
Cdd:pfam15665 79 YKRRVEE---RELKAEAEHRQRVVELSreveEAKRAFEEKLESFEQLQAQFEqEKRKALEELRAKHRQEIQELLTT---- 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1920237982 1548 aeaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREE 1583
Cdd:pfam15665 152 ----QRAQSASSLAEQEKLEELHKAELESLRKEVED 183
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
838-1795 |
2.21e-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: 44.40 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 838 EAQEAIARLEAQHQALVAlwhQLHTEMKSLLAWQSLGRDMQLIRSWSLATFRTLKpEEQRQALRSLELHYQAFLRDSQDA 917
Cdd:pfam01576 219 DLQEQIAELQAQIAELRA---QLAKKEEELQAALARLEEETAQKNNALKKIRELE-AQISELQEDLESERAARNKAEKQR 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 918 GGFGPE-DRLQAEREYGSCSRHYQQLLQSleQGEQEESRCQRCISElkdirlqleacETRtVHRLRLPLDKEPARECAQR 996
Cdd:pfam01576 295 RDLGEElEALKTELEDTLDTTAAQQELRS--KREQEVTELKKALEE-----------ETR-SHEAQLQEMRQKHTQALEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 997 ITEQQKaQAEVDGLGKGVARLSAEAEkVLALPEPSPAAPTLRSELELTLGKLE-QVRSLSAIYLEKLKtislvirstQEA 1075
Cdd:pfam01576 361 LTEQLE-QAKRNKANLEKAKQALESE-NAELQAELRTLQQAKQDSEHKRKKLEgQLQELQARLSESER---------QRA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1076 EEVLRAHEEQLkEAQAVPATLPELEATKAALKKLRAQAEAQ-QPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1154
Cdd:pfam01576 430 ELAEKLSKLQS-ELESVSSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1155 VtlllerwqavlaqtdVRQRELEqlgRQLRyyresadPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIEr 1234
Cdd:pfam01576 509 E---------------EAKRNVE---RQLS-------TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE- 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1235 hgEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPK----VQSGSESIIQEYVDLRTRYS----ELSTLTSQ 1306
Cdd:pfam01576 563 --EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKkfdqMLAEEKAISARYAEERDRAEaearEKETRALS 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1307 YIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEreaqglqrRMQEEVARREEVAVEAQ 1386
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVE--------EMKTQLEELEDELQATE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1387 EQKRSIQEELQHLRQSSEAEIQAKArqvEAAERSRLRIEEEIRVVRLQLEATERQRGGA-------EGELQALRARAEEA 1459
Cdd:pfam01576 713 DAKLRLEVNMQALKAQFERDLQARD---EQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAA 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1460 EAQKRQAQEEAERLRRQVQDetqrkRQAEAELALRVQAEAEA-AREKQRALQALEELRLQAEE----AERRLRQAEAERA 1534
Cdd:pfam01576 790 NKGREEAVKQLKKLQAQMKD-----LQRELEEARASRDEILAqSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERD 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1535 R-QVQVALETAQRSAeaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQqaeaeraraeaerelerwqlkaN 1613
Cdd:pfam01576 865 ElADEIASGASGKSA---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQ----------------------V 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1614 EALRLRLQAEEVAQQKSltqaeaekqkeeaerearrrgkaeEQAVRQRELAEQELEKQRQLAEGTAQQRLAAeqELIRLR 1693
Cdd:pfam01576 920 EQLTTELAAERSTSQKS------------------------ESARQQLERQNKELKAKLQEMEGTVKSKFKS--SIAALE 973
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1694 AETEQgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVRAEMEvllaSKARAEEESRSTSEKSKQRLEAEAGRFREL 1773
Cdd:pfam01576 974 AKIAQ-------LEEQLEQESRERQAANKLVRRTEKKLKEVLLQVE----DERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
970 980
....*....|....*....|..
gi 1920237982 1774 AEEAArlRALAEEAKRQRQLAE 1795
Cdd:pfam01576 1043 EEEAS--RANAARRKLQRELDD 1062
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2010-2445 |
2.22e-03 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 44.19 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2010 LQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAE 2089
Cdd:COG4995 1 LLALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2090 RLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQL 2169
Cdd:COG4995 81 ALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2170 EETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQ 2249
Cdd:COG4995 161 AAAALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2250 VAEEAARLSvAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQ 2329
Cdd:COG4995 241 LALAAAAAA-LAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2330 QLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEM-SRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTL 2408
Cdd:COG4995 320 LAALLLLLAALALLALLLLLAAAALLAAALAAALALAaALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAA 399
|
410 420 430
....*....|....*....|....*....|....*..
gi 1920237982 2409 ETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQL 2445
Cdd:COG4995 400 LLALAAAQLLRLLLAALALLLALAAYAAARLALLALI 436
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1449-1573 |
2.24e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1449 LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEaarekqralQALEELRLQAEEAERRLRQ 1528
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ---------QAIKEAKKEADEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1920237982 1529 AEAERARQVqvaletaqrsAEAELQSEHASFAEKTAQLERTLKEE 1573
Cdd:PRK00409 596 LQKGGYASV----------KAHELIEARKRLNKANEKKEKKKKKQ 630
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2406-2589 |
2.31e-03 |
|
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: 44.34 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2406 QTLETQRQQSDR----DAERLREAIAELEHEKDKLKqeaqllqlKSEEMQTVRQEQLLQETQ--ALQQSFLSEKDSLLQR 2479
Cdd:pfam17380 281 QKAVSERQQQEKfekmEQERLRQEKEEKAREVERRR--------KLEEAEKARQAEMDRQAAiyAEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2480 ERcIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEK 2559
Cdd:pfam17380 353 IR-QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190
....*....|....*....|....*....|.
gi 1920237982 2560 LLAEENQRL-RERLQHLEEERRAALARSEEI 2589
Cdd:pfam17380 432 ARQREVRRLeEERAREMERVRLEEQERQQQV 462
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1688-2035 |
2.32e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1688 ELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAElaKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA 1767
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE--RQRRELESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1768 GRFRELAEEAARLRAlAEEAKRQRQLAEEDAVrqRAEAERVLaeklaaiseatrlkteaeialkEKEAENERLRRLAEDE 1847
Cdd:pfam07888 108 ASSEELSEEKDALLA-QRAAHEARIRELEEDI--KTLTQRVL----------------------ERETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1848 AFQRRLLEEQAAQHKADIEARLAQLRKASeSELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRG 1927
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLS-KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1928 TAE-------------------DTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALE----- 1983
Cdd:pfam07888 242 LQErlnaserkveglgeelssmAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADkdrie 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237982 1984 ----EVERLKAKVEEARRLRERAEQESARQ--LQLAQEAAQKRLQAEEKAhAFAVQQK 2035
Cdd:pfam07888 322 klsaELQRLEERLQEERMEREKLEVELGREkdCNRVQLSESRRELQELKA-SLRVAQK 378
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1337-1544 |
2.36e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1337 AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQ--RRMQEEVARREEVAVEAQEQKRSIQE-----------ELQHLRQSS 1403
Cdd:PHA03247 1150 STVDAAVRAHGVLADAVAALSPAVRDPACPLAflVALADSAAGYVKATRLALDARRAIARlgalgaaaadlAVAVRRENP 1229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1404 EAE------IQAKARQVEAAERSRLRIEEEIRVVrLQLEATERQRGGAEGELQAL-------RARAEEAEAQkrqAQEEA 1470
Cdd:PHA03247 1230 QAEgdraalLEAAARAVTAAREGLAACEGEFGGL-LHAEGSAGDPSPSGRALQELgkvvgatRRRADELEAA---AADLA 1305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 1471 ERLRRQVQDETQRKRQAEAELAL-RVQAEAEAAREKQRALQALE-ELRLQAEEAERRLRQAEAERARQVQVALETA 1544
Cdd:PHA03247 1306 EKMAARRARASRERWAADVEAALdRVENRAEFDAVELRRLQALAaTHGYNPRDFRKRAEQALAANAKTATLALEAA 1381
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1434-1549 |
2.36e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1434 QLEATERQR-GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQAL 1512
Cdd:PRK09039 67 DLLSLERQGnQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237982 1513 EELR---------LQAEEAERRLRQAE-AERARQVQVALetAQRSAE 1549
Cdd:PRK09039 147 AALRrqlaaleaaLDASEKRDRESQAKiADLGRRLNVAL--AQRVQE 191
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1343-1549 |
2.50e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1343 LEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEvaRREEVAVEAQEQKRSIQEELQHLrQSSEAEIQAKARQVEAaersrl 1422
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREEL-QREEERLVQKEEQLDA------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1423 RIEEeirvvrlqLEATERQRGGAEgelQALRARAEEAEAQKRQAQEEAERLrrqvqdETQRKRQAEAELALRVQAEAEaa 1502
Cdd:PRK12705 96 RAEK--------LDNLENQLEERE---KALSARELELEELEKQLDNELYRV------AGLTPEQARKLLLKLLDAELE-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1920237982 1503 REKQRALQALEelrlqaEEAerrlrQAEAERARQVQVAlETAQRSAE 1549
Cdd:PRK12705 157 EEKAQRVKKIE------EEA-----DLEAERKAQNILA-QAMQRIAS 191
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1313-1585 |
2.57e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.94 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1313 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEaHAQAKAQAEREAQGLQRRMQEevARREEVAVEAQEQKRSI 1392
Cdd:pfam03528 96 DEVKSQWQEEVASLQAIMKETVREYEVQFHRRLEQERAQ-WNQYRESAEREIADLRRRLSE--GQEEENLEDEMKKAQED 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1393 QEELQHLRQSSEAEIQA-KARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALraraeeaEAQKRQAQEEAE 1471
Cdd:pfam03528 173 AEKLRSVVMPMEKEIAAlKAKLTEAEDKIKELEASKMKELNHYLEAEKSCRTDLEMYVAVL-------NTQKSVLQEDAE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1472 RLRRQVQDETQRkrqaeaeLALRVQAEAEAAREKQRAL-QALEELRLQAEEAERRLRQAEAERARQVqvalETAQRSAEA 1550
Cdd:pfam03528 246 KLRKELHEVCHL-------LEQERQQHNQLKHTWQKANdQFLESQRLLMRDMQRMESVLTSEQLRQV----EEIKKKDQE 314
|
250 260 270
....*....|....*....|....*....|....*
gi 1920237982 1551 ELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAT 1585
Cdd:pfam03528 315 EHKRARTHKEKETLKSDREHTVSIHAVFSPAGVET 349
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1367-2032 |
2.64e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.97 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1367 LQRRMQeevARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRL---RIEEEIRVVR-LQLEATERQR 1442
Cdd:pfam07111 21 LERRLD---TQRPTVTMWEQDVSGDGQGPGRRGRSLELEGSQALSQQAELISRQLQelrRLEEEVRLLReTSLQQKMRLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1443 GGA-EGELQALRARAEEAEAQK-RQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKqralqALEELRLQAE 1520
Cdd:pfam07111 98 AQAmELDALAVAEKAGQAEAEGlRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQAHEE-----ALSSLTSKAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1521 EAERRLRQAEAERARQVQvALETAQRsaEAELQSEHASFAEKTAQLERTLKEEHVAVV--QLREEATRRAQQQAEAERAR 1598
Cdd:pfam07111 173 GLEKSLNSLETKRAGEAK-QLAEAQK--EAELLRKQLSKTQEELEAQVTLVESLRKYVgeQVPPEVHSQTWELERQELLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1599 AEAERELERWQLKAN-EALRLRLQaeevaqqkSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEG 1677
Cdd:pfam07111 250 TMQHLQEDRADLQATvELLQVRVQ--------SLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1678 TAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQReaaAATQKRRELEAELAKVRA-EMEVLLASKARAEEESRSTS 1756
Cdd:pfam07111 322 LKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQR---ALQDKAAEVEVERMSAKGlQMELSRAQEARRRQQQQTAS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1757 EKSKQRLEAEAGRFRELAEEAARLRaLAEEAKRQRQLAEE--DAVRQRAEAERVLAEKLAAIS---EATRLKTEAEIALK 1831
Cdd:pfam07111 399 AEEQLKFVVNAMSSTQIWLETTMTR-VEQAVARIPSLSNRlsYAVRKVHTIKGLMARKVALAQlrqESCPPPPPAPPVDA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1832 EKEAENERLRRlaedeafQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKA 1911
Cdd:pfam07111 478 DLSLELEQLRE-------ERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVA 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1912 AAGKAELELELGRIRGTAEDTLRSKEQAEQEA-----ARQRQLAAEEERRRREAEERVQK---SLAAEEEAARQRKAALE 1983
Cdd:pfam07111 551 RQGQQESTEEAASLRQELTQQQEIYGQALQEKvaeveTRLREQLSDTKRRLNEARREQAKavvSLRQIQHRATQEKERNQ 630
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 1984 EVERLK--AKVEEARRLRERAEQ-ESARQLQLAQEAAQKRLQAEEKAHAFAV 2032
Cdd:pfam07111 631 ELRRLQdeARKEEGQRLARRVQElERDKNLMLATLQQEGLLSRYKQQRLLAV 682
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1655-1799 |
2.67e-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: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1655 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1734
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237982 1735 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAV 1799
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAI 356
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2131-2295 |
2.73e-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: 42.60 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2131 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQ 2210
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2211 mEELGKLKARIEAENRALVLRDkDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2290
Cdd:COG1579 89 -KEYEALQKEIESLKRRISDLE-DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*
gi 1920237982 2291 QAVQE 2295
Cdd:COG1579 167 ELAAK 171
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2250-2493 |
2.87e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.56 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2250 VAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML--KEKMQAVQEATRLKAEAELLQQQKELAQEQAR--------- 2318
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYlaKEEDLKRQNAVLQEAQVELDALQNQLALARAEmenikavat 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2319 ----RLQEDKEQMAQQLAQETQGFQKTL-ETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRfrkqaedigerlyR 2393
Cdd:pfam03528 86 vsenTKQEAIDEVKSQWQEEVASLQAIMkETVREYEVQFHRRLEQERAQWNQYRESAEREIADLRR-------------R 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2394 TELATQEkvmlvQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQA--------- 2464
Cdd:pfam03528 153 LSEGQEE-----ENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKELNHYLEAekscrtdle 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1920237982 2465 -------LQQSFLSEKDSLLQRE-----RCIEQEKAKLEQL 2493
Cdd:pfam03528 228 myvavlnTQKSVLQEDAEKLRKElhevcHLLEQERQQHNQL 268
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
496-590 |
2.87e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.01 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 496 LRYLQDLLAWVEENQRRLDSAEWGVDLPSVEAQLGSHRGLHQSVEEFRTKIERARTDEGQL---SPATRGAYRDCLGRLD 572
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1920237982 573 LQYAKLLSSSKARLRSLE 590
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1397-1886 |
2.99e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1397 QHLRQSSEAEIQAKARqVEAAERSRLRIEEEIRVVRLQLEATERQRGGA--EGELQALRARAEEAEAQKRQAQEEAERLR 1474
Cdd:COG3064 2 QEALEEKAAEAAAQER-LEQAEAEKRAAAEAEQKAKEEAEEERLAELEAkrQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1475 RQVQDETQRKRQAEAELAlRVQAEAEAAREKQRALQALEELRLQAEEaerrlRQAEAERARQVQVALETAQRSAEAELQS 1554
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKA-KAAKEAEAAAAAEKAAAAAEKEKAEEAK-----RKAEEEAKRKAEEERKAAEAEAAAKAEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1555 EHASFAEKTAQLERTLKEEhVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQA 1634
Cdd:COG3064 155 EAARAAAAAAAAAAAAAAR-AAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1635 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQ 1714
Cdd:COG3064 234 LAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1715 REAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1794
Cdd:COG3064 314 EEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1795 EEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRK 1874
Cdd:COG3064 394 AAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDG 473
|
490
....*....|..
gi 1920237982 1875 ASESELERQKGL 1886
Cdd:COG3064 474 GAVLADLLLLGG 485
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1322-1583 |
3.09e-03 |
|
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: 43.66 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1322 ERLAEQQRAEERERLAEVEaALEKQRQLAEAHAQAkaqaereaqgLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRq 1401
Cdd:pfam10174 453 ERLKEQREREDRERLEELE-SLKKENKDLKEKVSA----------LQPELTEKESSLIDLKEHASSLASSGLKKDSKLK- 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1402 SSEAEIQA-------------KARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQK----- 1463
Cdd:pfam10174 521 SLEIAVEQkkeecsklenqlkKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKndkdk 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1464 ----------RQAQEEAERLR--RQVQDETQRKRQAEAELALRVQ-AEAEAAREKQRA--LQALEELRLQAEEAERRLRQ 1528
Cdd:pfam10174 601 kiaelesltlRQMKEQNKKVAniKHGQQEMKKKGAQLLEEARRREdNLADNSQQLQLEelMGALEKTRQELDATKARLSS 680
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237982 1529 AE--------------AERARQVQVALETAQRSAEAELQSEHASFA--EKTAQLERTLKEEhvaVVQLREE 1583
Cdd:pfam10174 681 TQqslaekdghltnlrAERRKQLEEILEMKQEALLAAISEKDANIAllELSSSKKKKTQEE---VMALKRE 748
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2256-2374 |
3.55e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2256 RLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELaQEQARRLQEDKEQMAQQLA 2332
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEihkLRNEFEKELRERRNEL-QKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 2333 ------QETQGFQKTLETERQRQLEMSAEAERLR-------LRVAEMSRAQARAE 2374
Cdd:PRK12704 104 llekreEELEKKEKELEQKQQELEKKEEELEELIeeqlqelERISGLTAEEAKEI 158
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1400-1553 |
3.58e-03 |
|
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: 42.80 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1400 RQSSEAEIQAKARQVEA-AERSRLRIE-EEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQV 1477
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-RRVL 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 1478 QDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQ 1553
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3734-3765 |
3.63e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.63e-03
10 20 30
....*....|....*....|....*....|..
gi 1920237982 3734 RLLSAERAVTGYRDPYTEQTISLFQAMKKDLI 3765
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2703-2736 |
3.63e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.63e-03
10 20 30
....*....|....*....|....*....|....
gi 1920237982 2703 LLEAQAASGFLLDPVRNRRLAVNEAVKEGIVGPE 2736
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2236-2369 |
3.63e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.47 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2236 AQRLLQE-----EAEKMK-QVAEEAAR---LSVAAQEAARlrQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELL 2306
Cdd:PTZ00491 672 AELLEQEargrlERQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRI 748
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237982 2307 QQQKELAQEQARRLQEdkeqmaqqLAQETQgfQKTLETERQRQLeMSAEAERL--------RLRVAEMSRA 2369
Cdd:PTZ00491 749 EAEAELEKLRKRQELE--------LEYEQA--QNELEIAKAKEL-ADIEATKFerivealgRETLIAIARA 808
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1040-1256 |
3.74e-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: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1040 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKAALkklraqaEAQQPV 1119
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1120 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDvrqrELEQLGRQLRYYResadpLGAWLRD 1199
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE----AAEDLARLELRAL-----LEERFAA 757
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 1200 AKQRqeqiqavplANSQAVREQLRQE-KALLEDIERHGEKVEEC-QRFAKQYINAIKDY 1256
Cdd:COG4913 758 ALGD---------AVERELRENLEERiDALRARLNRAEEELERAmRAFNREWPAETADL 807
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1448-1582 |
3.76e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1448 ELQALRARAEEAEAQKRQAQEEAERLRRQVQdetqrkrqaE-AELALRVQAEAEAAREKQRaLQALEELRLQAEEAERRL 1526
Cdd:COG0497 166 AWRALKKELEELRADEAERARELDLLRFQLE---------ElEAAALQPGEEEELEEERRR-LSNAEKLREALQEALEAL 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 1527 RQAEAerarQVQVALETAQRSAEaELQSEHASFAEKTAQLERtlkeehvAVVQLRE 1582
Cdd:COG0497 236 SGGEG----GALDLLGQALRALE-RLAEYDPSLAELAERLES-------ALIELEE 279
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1669-1942 |
3.80e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 42.92 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1669 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQllEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASK 1745
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQ--YDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1746 ARAEEESRSTSEK---SKQRLEAEAGRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAVRQRAEA 1805
Cdd:pfam03148 81 RRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAARHKLEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1806 ErvLAEKLAAI---SEATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRLLE--EQAAQHKADIEARLAQLRKASES 1878
Cdd:pfam03148 159 D--LSDKKEALeidEKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIEraEKERAASAQLRELIDSILEQTAN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 1879 ELERQKGLVEDTLRQRrqVEEeilalkgsFEKAaagKAELELELGRIRgtaedtlrsKEQAEQE 1942
Cdd:pfam03148 237 DLRAQADAVNFALRKR--IEE--------TEDA---KNKLEWQLKKTL---------QEIAELE 278
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1159-1432 |
3.80e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1159 LERWQAVLAQTDVRQRELEQLGRQLryyrESADplgawlRDAKQRQEQIQAVPLANSQAVREQLrqEKALLEDIERhgeK 1238
Cdd:PRK11281 65 LEQTLALLDKIDRQKEETEQLKQQL----AQAP------AKLRQAQAELEALKDDNDEETRETL--STLSLRQLES---R 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1239 VEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYVDLRTRYSelSTLTSQyiRFISETLR-R 1317
Cdd:PRK11281 130 LAQTLDQLQNAQNDLAEYNSQLVSLQTQPE---------RAQAALYANSQRLQQIRNLLK--GGKVGG--KALRPSQRvL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1318 MEEEERLAEQQRAEERERLA---EVEAALEKQRQLAEAHAQakaQAEREAQGLQRRM-QEEVARREEVAVEAQEQKRS-- 1391
Cdd:PRK11281 197 LQAEQALLNAQNDLQRKSLEgntQLQDLLQKQRDYLTARIQ---RLEHQLQLLQEAInSKRLTLSEKTVQEAQSQDEAar 273
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1392 ------IQEELQHLRQSSEAEIQAKAR-------------QVEAAERSRLRIEEEIRVVR 1432
Cdd:PRK11281 274 iqanplVAQELEINLQLSQRLLKATEKlntltqqnlrvknWLDRLTQSERNIKEQISVLK 333
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1785-2034 |
3.87e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1785 EEAKRQRQLAEEDAVRQRAEAERVLAEKLAA-ISEATRLKTEAEIALKEKEAENerlrrlaedeafqrrlLEEQAAQHKA 1863
Cdd:PRK07735 2 DPEKDLEDLKKEAARRAKEEARKRLVAKHGAeISKLEEENREKEKALPKNDDMT----------------IEEAKRRAAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1864 DIEARLAQLRKASESELERQkglvedtlrqrrqVEEEILALKGSFEKAAAGKAElELELGRIRGTAEDTLRSKEQAEQEA 1943
Cdd:PRK07735 66 AAKAKAAALAKQKREGTEEV-------------TEEEKAKAKAKAAAAAKAKAA-ALAKQKREGTEEVTEEEKAAAKAKA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1944 ARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQA 2023
Cdd:PRK07735 132 AAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAA 211
|
250
....*....|.
gi 1920237982 2024 EEKAHAFAVQQ 2034
Cdd:PRK07735 212 KAKAAALAKQK 222
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2248-2589 |
3.98e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2248 KQVAEEAARLSVAA--QEAARLRQLAEEDLAQQRALAEKmlkekmqavqEATRLKAEAELLQQQKELAQEQARR--LQED 2323
Cdd:PRK04863 260 KHLITESTNYVAADymRHANERRVHLEEALELRRELYTS----------RRQLAAEQYRLVEMARELAELNEAEsdLEQD 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2324 KEQMA--QQLAQETQGFQKTLE------TERQRQLEMSAEAERLRLRVAEMSRAQA-RAEEDARRFRKQAEDIGERL--- 2391
Cdd:PRK04863 330 YQAASdhLNLVQTALRQQEKIEryqadlEELEERLEEQNEVVEEADEQQEENEARAeAAEEEVDELKSQLADYQQALdvq 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2392 YRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEaqLLQLksEEMQTVRQEQLLQETQALQ--QSF 2469
Cdd:PRK04863 410 QTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEE--LLSL--EQKLSVAQAAHSQFEQAYQlvRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2470 LSEKDsllqRERCIEQEKAKLEQL--FQDEVAKAQALReeqqrqqqqmqqekqqlaASMEEARRRQHEAEEGVRRQQEEL 2547
Cdd:PRK04863 486 AGEVS----RSEAWDVARELLRRLreQRHLAEQLQQLR------------------MRLSELEQRLRQQQRAERLLAEFC 543
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1920237982 2548 QRLAQQQQQQEkLLAEENQRLRERLQHLEEERRAALARSEEI 2589
Cdd:PRK04863 544 KRLGKNLDDED-ELEQLQEELEARLESLSESVSEARERRMAL 584
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2291-2588 |
3.98e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.32 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2291 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRvaemsrAQ 2370
Cdd:pfam02029 6 EAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQK------RL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2371 ARAEEDARRFRKQAEDIGErlyrtELATQEKVMLVQTLETQRQQSDRDAERLREAIAELE------------------HE 2432
Cdd:pfam02029 80 QEALERQKEFDPTIADEKE-----SVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEirekeyqenkwstevrqaEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2433 KDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQ 2512
Cdd:pfam02029 155 EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2513 QQMQQEKQQLAA--SMEEARRRQHEAEEgvrrqqEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRA-------AL 2583
Cdd:pfam02029 235 EREEEAEVFLEAeqKLEELRRRRQEKES------EEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRrkqeeaeRK 308
|
....*
gi 1920237982 2584 ARSEE 2588
Cdd:pfam02029 309 LREEE 313
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1423-1553 |
4.10e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.12 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1423 RIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAA 1502
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDLAREALERKAELEAQ 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 1503 REKQRAL-----QALEELRLQAEEAERRLRQAEAERArqvqvALETAQRSAEAELQ 1553
Cdd:COG1842 100 AEALEAQlaqleEQVEKLKEALRQLESKLEELKAKKD-----TLKARAKAAKAQEK 150
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1349-1536 |
4.29e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.92 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1349 LAEAHAQAKAQAEREAQGLQRRMQEEVARreevaveAQEQKRSIQEELQHLRQsseaeiqakarqveaaERSRLRIEEEI 1428
Cdd:COG3524 160 LAESEELVNQLSERAREDAVRFAEEEVER-------AEERLRDAREALLAFRN----------------RNGILDPEATA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1429 RVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAL-RVQAEaeaarekqr 1507
Cdd:COG3524 217 EALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLaSLLAE--------- 287
|
170 180 190
....*....|....*....|....*....|.
gi 1920237982 1508 alqaLEELRLQAEEAERRLRQAEA--ERARQ 1536
Cdd:COG3524 288 ----YERLELEREFAEKAYTSALAalEQARI 314
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1415-1532 |
4.40e-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: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1415 EAAerSRLRIE-----EEIRVVRLQLEATERqrggaegELQALRaraeeaEAQKRQAQEEAERLRRQVQDETQRKRQAEA 1489
Cdd:COG0542 397 EAA--ARVRMEidskpEELDELERRLEQLEI-------EKEALK------KEQDEASFERLAELRDELAELEEELEALKA 461
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237982 1490 elalRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAE 1532
Cdd:COG0542 462 ----RWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEE 500
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1461-1933 |
4.46e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1461 AQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQR--ALQALEELRLQAEEAERRLRQAEAERARQvQ 1538
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELeaKRQAEEEAREAKAEAEQRAAELAAEAAKK-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1539 VALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVA----VVQLREEATRRAQQQAEAERARAEAERELERWQLKANE 1614
Cdd:COG3064 80 AEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAekekAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1615 ALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRA 1694
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1695 ETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELA 1774
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1775 EEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLL 1854
Cdd:COG3064 320 AAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237982 1855 EEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTL 1933
Cdd:COG3064 400 LLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLA 478
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1350-1538 |
4.53e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1350 AEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEir 1429
Cdd:PRK12678 67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1430 vvRLQLEATERQRGGAEGELQALRARAEEAEA--QKRQAQEEAERLRRQVQDETQRKRQaEAELALRVQAEAEAAREKQR 1507
Cdd:PRK12678 145 --AGEGGEQPATEARADAAERTEEEERDERRRrgDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRREERGRR 221
|
170 180 190
....*....|....*....|....*....|.
gi 1920237982 1508 ALQALEELRLQAEEAERRLRQAEAERARQVQ 1538
Cdd:PRK12678 222 DGGDRRGRRRRRDRRDARGDDNREDRGDRDG 252
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2151-2584 |
4.61e-03 |
|
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: 43.27 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2151 ALRQKAQVEQ-ELTALRLQLEEtdhQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEaeNRALV 2229
Cdd:pfam10174 335 AKEQRAAILQtEVDALRLRLEE---KESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE--NLQEQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2230 LRDKDsaqRLLQEEAEKMKQVAEEAARLSVA---AQEAARLRQLAEEDLAQQRALAEKMLKEKMQAV-QEATRLKAEAEL 2305
Cdd:pfam10174 410 LRDKD---KQLAGLKERVKSLQTDSSNTDTAlttLEEALSEKERIIERLKEQREREDRERLEELESLkKENKDLKEKVSA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2306 LQQQKelaQEQARRLQEDKEQmAQQLAQ---ETQGFQKTLETERQRQLEmsaEAERLrlrVAEMSRAQaRAEEDARrfrk 2382
Cdd:pfam10174 487 LQPEL---TEKESSLIDLKEH-ASSLASsglKKDSKLKSLEIAVEQKKE---ECSKL---ENQLKKAH-NAEEAVR---- 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2383 QAEDIGERLYRTELATQEKVMlvqtlETQRQQSDrdAERLREAIAELEHEK-DKLKQEAQLLQLKSEEMQTvrQEQLLQE 2461
Cdd:pfam10174 552 TNPEINDRIRLLEQEVARYKE-----ESGKAQAE--VERLLGILREVENEKnDKDKKIAELESLTLRQMKE--QNKKVAN 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2462 TQALQQsflsekdsllqrercieQEKAKLEQLFQDevakaqALREEQQRQQQQMQQEKQQLAASMEEARRrqhEAEEGVR 2541
Cdd:pfam10174 623 IKHGQQ-----------------EMKKKGAQLLEE------ARRREDNLADNSQQLQLEELMGALEKTRQ---ELDATKA 676
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1920237982 2542 RQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALA 2584
Cdd:pfam10174 677 RLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAAIS 719
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1695-1917 |
4.68e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1695 ETEQGEQQRQLLEEELARLQ-----------REAAAATQKRRELEAELAKVRAEMEV-----LLASKARAEEESRSTSEK 1758
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHgaeiskleeenREKEKALPKNDDMTIEEAKRRAAAAAkakaaALAKQKREGTEEVTEEEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1759 SKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED--AVRQRAEAERVLAEKLAAISEATRLKTEAEIAL---KEK 1833
Cdd:PRK07735 91 AKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAkaAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKakaKAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1834 EAENERLRRLAEDEAFQRRLLEEQAAQH-KADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEE-ILALKGSFEKA 1911
Cdd:PRK07735 171 AAAKAKAAALAKQKAAEAGEGTEEVTEEeKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKaIAAAKAKAAAA 250
|
....*.
gi 1920237982 1912 AAGKAE 1917
Cdd:PRK07735 251 ARAKTK 256
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2080-2266 |
4.69e-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: 43.02 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2080 QSRRQVEEAERLKQsAEEQAQAQAQAQAAAEKLRKeaeqeaarraqaeqAALRQKQAADAEMEKHKQFAEQALRQKAQVE 2159
Cdd:pfam15709 360 QRRLQQEQLERAEK-MREELELEQQRRFEEIRLRK--------------QRLEEERQRQEEEERKQRLQLQAAQERARQQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2160 QEltALRLQLEETDHQKsildeelQRLKAEVTEAARQRGQVEEElfslrvQMEELGKLKARIEAENRALVLRDKDSAQRL 2239
Cdd:pfam15709 425 QE--EFRRKLQELQRKK-------QQEEAERAEAEKQRQKELEM------QLAEEQKRLMEMAEEERLEYQRQKQEAEEK 489
|
170 180 190
....*....|....*....|....*....|..
gi 1920237982 2240 LQEEAEKMKQVAEEAARLSVA-----AQEAAR 2266
Cdd:pfam15709 490 ARLEAEERRQKEEEAARLALEeamkqAQEQAR 521
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2292-2546 |
4.72e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2292 AVQEATRLKAEAELLQQQKEL--AQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA 2369
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELseLQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2370 QARAEEDARRFRKQ------------AEDIGE---RLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKD 2434
Cdd:COG3883 85 REELGERARALYRSggsvsyldvllgSESFSDfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2435 KLKQEAQLLQLKSEEmqtvrQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQ 2514
Cdd:COG3883 165 ELEAAKAELEAQQAE-----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260 270
....*....|....*....|....*....|..
gi 1920237982 2515 MQQEKQQLAASMEEARRRQHEAEEGVRRQQEE 2546
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA 271
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1858-2034 |
4.75e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1858 AAQHKADIEARLAQLRKasesELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKE 1937
Cdd:COG4942 18 QADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1938 QAEQEAARQRQLAAEEERRRREAEER--------------VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRErAE 2003
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE-AE 172
|
170 180 190
....*....|....*....|....*....|.
gi 1920237982 2004 QESARQLQLAQEAAQKRLQAEEKAHAFAVQQ 2034
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLAR 203
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2245-2339 |
4.76e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 42.27 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2245 EKMKQVAEEAARLSVAAQEAARLRQLAEEDL----AQQRALAE--KMLKEKMQAVQEatRLKAEAELLQQQKElaQEQAR 2318
Cdd:pfam02841 201 AKEKAIEAERAKAEAAEAEQELLREKQKEEEqmmeAQERSYQEhvKQLIEKMEAERE--QLLAEQERMLEHKL--QEQEE 276
|
90 100
....*....|....*....|.
gi 1920237982 2319 RLQEDKEQMAQQLAQETQGFQ 2339
Cdd:pfam02841 277 LLKEGFKTEAESLQKEIQDLK 297
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1653-1753 |
4.81e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1653 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELA 1732
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 1920237982 1733 KvRAEMEVLLaskarAEEESR 1753
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2212-2340 |
4.81e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2212 EELGKLKARIEAENRALVLRDKDSAQrlLQEeaekmkQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQ 2291
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQD------SVANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237982 2292 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ----------QLAQETQGFQK 2340
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAKiadlgrrlnvALAQRVQELNR 194
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1772-1900 |
4.98e-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: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1772 ELAEEAARLRALAE-EAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 1850
Cdd:COG2268 196 EIIRDARIAEAEAErETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANA 275
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1920237982 1851 RRLLEEQAAQHKADIEARLAQLRKA-SESELERQKGLVEDTLRQRRQVEEE 1900
Cdd:COG2268 276 EREVQRQLEIAEREREIELQEKEAErEEAELEADVRKPAEAEKQAAEAEAE 326
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1292-1553 |
5.11e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 42.72 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1292 DLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQRAEERERLAEVEAAlekQRQLAEAHAQaKAQAEREAQGLQRRM 1371
Cdd:COG1538 77 EVAQAYFDLLAAQEQ-LALAEENLALAEELLELARARYEAGLASRLDVLQA---EAQLAQARAQ-LAQAEAQLAQARNAL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1372 QEEVARREEVAVEAQEQKRSIQEELQHLRQSSEA------EIQAKARQVEAAERsRLRIEEEIRVVRLQLEATERQRGGA 1445
Cdd:COG1538 152 ALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEalerrpDLRAAEAQLEAAEA-EIGVARAAFLPSLSLSASYGYSSSD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1446 EGELQ-------------------ALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ 1506
Cdd:COG1538 231 DLFSGgsdtwsvglslslplfdggRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEAAE 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 1507 RALQALEEL-------RLQAEEAERRLRQAEAERarqvqVALETAQRSAEAELQ 1553
Cdd:COG1538 311 EALELARARyraglasLLDVLDAQRELLQAQLNL-----IQARYDYLLALVQLY 359
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1317-1504 |
5.43e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.68 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1317 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQglqrrmQEEVARREEVAVEAQEQKRSIQEEL 1396
Cdd:pfam05262 206 RESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQ------QEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1397 QHLRQSSEAEIQAKARQVeaaersrlrieeeirvvrlqLEATERQRGGAEGElqalrARAEEAEAQKRqaQEEAERLRRQ 1476
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEA--------------------LKAKDHKAFDLKQE-----SKASEKEAEDK--ELEAQKKREP 332
|
170 180
....*....|....*....|....*....
gi 1920237982 1477 VQDETQR-KRQAEAElalrVQAEAEAARE 1504
Cdd:pfam05262 333 VAEDLQKtKPQVEAQ----PTSLNEDAID 357
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1319-1506 |
5.46e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.06 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1319 EEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAER--------EAQGLQRRMQ-----EEVARREEVAVEA 1385
Cdd:TIGR00927 649 GERPTEAEGENGEESGGEAEQE---GETETKGENESEGEIPAERkgeqegegEIEAKEADHKgeteaEEVEHEGETEAEG 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1386 QEQKRSIQ--EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQA---LRARAEEAE 1460
Cdd:TIGR00927 726 TEDEGEIEtgEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGE--------TEAEGKEDEDEGEIQAgedGEMKGDEGA 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1920237982 1461 AQKRQAQEEAERlRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ 1506
Cdd:TIGR00927 798 EGKVEHEGETEA-GEKDEHEGQSETQADDTEVKDETGEQELNAENQ 842
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1766-1875 |
5.59e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1766 EAGRFRELAEEAARLRALAEEAKRQRQLAEE--------DAVRQRAEAERVLAEKLAAISEATRLKTEAEIA-LKEKEAE 1836
Cdd:PRK11448 130 KPGPFVPPEDPENLLHALQQEVLTLKQQLELqarekaqsQALAEAQQQELVALEGLAAELEEKQQELEAQLEqLQEKAAE 209
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237982 1837 NErlrrlAEDEAFQRRLLEEQAAQHKAD-IEARL---AQLRKA 1875
Cdd:PRK11448 210 TS-----QERKQKRKEITDQAAKRLELSeEETRIlidQQLRKA 247
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1443-1583 |
5.62e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1443 GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQrkrqaEAELALRVQAEAEAAREKQralqaleelRLQAEEa 1522
Cdd:PRK12705 19 GVLVVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAK-----ELLLRERNQQRQEARRERE---------ELQREE- 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 1523 ERRLRQAEAERARQVQVALETAQRS-AEAELQSEHASFAEKTAQLERTLKEehvaVVQLREE 1583
Cdd:PRK12705 84 ERLVQKEEQLDARAEKLDNLENQLEeREKALSARELELEELEKQLDNELYR----VAGLTPE 141
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1445-1554 |
5.67e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1445 AEGELQALRARAE-EAEAQKR----QAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALE-ELRLQ 1518
Cdd:PRK12704 36 AEEEAKRILEEAKkEAEAIKKeallEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREeELEKK 115
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237982 1519 AEEAERRLRQAEAERARqvqvaLETAQRSAEAELQS 1554
Cdd:PRK12704 116 EKELEQKQQELEKKEEE-----LEELIEEQLQELER 146
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1094-1504 |
5.68e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 42.36 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1094 ATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGaqevgerLQQRHGERDVEVERWRERvtllLERWQAVLAQTDVRQ 1173
Cdd:pfam19220 38 AILRELPQAKSRLLELEALLAQERAAYGKLRRELAG-------LTRRLSAAEGELEELVAR----LAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1174 RELEQLGRQLRYYRESADplgawlRDAKQRQEQIQAVPLANsQAVREQLRQEKALLEDIERHGEKVEECQRFAKQyinai 1253
Cdd:pfam19220 107 EELRIELRDKTAQAEALE------RQLAAETEQNRALEEEN-KALREEAQAAEKALQRAEGELATARERLALLEQ----- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1254 kdyelqlvtykaqlepvaspaKKPKVQSGSESIIQEYVDLRTRYSELSTL---TSQYIRFISETLRRMEEEERLAEQQRA 1330
Cdd:pfam19220 175 ---------------------ENRRLQALSEEQAAELAELTRRLAELETQldaTRARLRALEGQLAAEQAERERAEAQLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1331 EERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLrqssEAEIQAK 1410
Cdd:pfam19220 234 EAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGL----EADLERR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1411 ARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqaeAE 1490
Cdd:pfam19220 310 TQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRLKEELQRER---AE 386
|
410
....*....|....
gi 1920237982 1491 LALrVQAEAEAARE 1504
Cdd:pfam19220 387 RAL-AQGALEIARE 399
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1316-1723 |
6.12e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.72 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1316 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAK-AQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQE 1394
Cdd:COG3064 24 EKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEqRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1395 ELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLR 1474
Cdd:COG3064 104 AEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1475 RQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQS 1554
Cdd:COG3064 184 AAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1555 EHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQA 1634
Cdd:COG3064 264 LAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1635 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQ 1714
Cdd:COG3064 344 LAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVL 423
|
....*....
gi 1920237982 1715 REAAAATQK 1723
Cdd:COG3064 424 LALAGAAGA 432
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1311-1419 |
6.16e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 41.90 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1311 ISETLRR----MEEEE-RLAeqqRAEERERLAEVEAALEKQRQLAEahaqakaqAEREAQGLQRRMQEEVARReevavEA 1385
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLL---IAEQHQKVVEKEAETERKRAVIE--------AEKDAEVAKIQMQQKIMEK-----EA 223
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237982 1386 QEQKRSIQEELQHLRQSS--EAEIQAKARQVEAAER 1419
Cdd:cd03406 224 EKKISEIEDEMHLAREKAraDAEYYRALREAEANKL 259
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2148-2401 |
6.41e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2148 AEQALRQKAQVEQELTALRLQLEETDHQK----------SILDEELQRLKAEVTEAARQRGQVEEELF-SLRVQMEELGK 2216
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLIRGATEGLCVHSLSkELDVLKEENML 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2217 LKARIEAEnRALVLRDKDSAQRLLQEEAEKM---KQVAEEAARLSVAAQEAARLRQLAEED------------------- 2274
Cdd:PLN02939 238 LKDDIQFL-KAELIEVAETEERVFKLEKERSlldASLRELESKFIVAQEDVSKLSPLQYDCwwekvenlqdlldratnqv 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2275 ------LAQQRALAEK--MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTL---- 2342
Cdd:PLN02939 317 ekaalvLDQNQDLRDKvdKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLsklk 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237982 2343 ETERQRQLEMSAEA------ERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEK 2401
Cdd:PLN02939 397 EESKKRSLEHPADDmpsefwSRILLLIDGWLLEKKISNNDAKLLREMVWKRDGRIREAYLSCKGK 461
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1094-1537 |
6.58e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1094 ATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDVRQ 1173
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1174 RELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAI 1253
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1254 KDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEER 1333
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1334 ERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQ 1413
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1414 VEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAL 1493
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1920237982 1494 RVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV 1537
Cdd:COG5278 483 ALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1703-2015 |
6.67e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1703 RQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESrstsEKSKQRLEAEAGRFRELAEEAARLRA 1782
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1783 LAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHK 1862
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1863 ADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQE 1942
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237982 1943 AARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2015
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3659-3697 |
6.69e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.92 E-value: 6.69e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1920237982 3659 YLYGTGCVAGIYRPGSRQTLTIYQALKKGQLSAEVARQL 3697
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2149-2590 |
6.74e-03 |
|
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: 42.75 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2149 EQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQ-RGQVEEELFSLRVQMEELGKLKARIEAENRA 2227
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2228 LVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEE------DLAQQRALAEKMLKEKMQAVQEATRLKA 2301
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEyaelkeELEDLRAELEEVDKEFAETRDELKDYRE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2302 EAELLQQQKELAQEQARRLQEDKEQMAQQLAQetqgFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFR 2381
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2382 KQAEDIGERLYRTELATQEKVMLVQTLETQRQQSdRDAERLREAIAELEHEKDK--LKQEAQLLQLKSE----------- 2448
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARAS-EERVRGGRAVEEVLKASIQgvHGTVAQLGSVGERyataievaagn 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2449 ---------EMQTVRQEQLLQETQALQQSFL-------SEKD-SLLQRERCI----------EQEKAKLEQLFQDEV--- 2498
Cdd:TIGR02169 548 rlnnvvvedDAVAKEAIELLKRRKAGRATFLplnkmrdERRDlSILSEDGVIgfavdlvefdPKYEPAFKYVFGDTLvve 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2499 ----------------------------------------------AKAQALREEQQRQQQQMQQEKQQLA---ASMEEA 2529
Cdd:TIGR02169 628 dieaarrlmgkyrmvtlegelfeksgamtggsraprggilfsrsepAELQRLRERLEGLKRELSSLQSELRrieNRLDEL 707
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237982 2530 RRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEenqrLRERLQHLEEERRAALARSEEIA 2590
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE----LEEDLSSLEQEIENVKSELKELE 764
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1405-1558 |
6.75e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.58 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1405 AEIQAKARQVEAAERSRLRIEEEIrvvrlqlEATERQRGGAEGElqALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1484
Cdd:PRK12678 29 PELRALAKQLGIKGTSGMRKGELI-------AAIKEARGGGAAA--AAATPAAPAAAARRAARAAAAARQAEQPAAEAAA 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237982 1485 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHAS 1558
Cdd:PRK12678 100 AKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERR 173
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1680-2091 |
6.93e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1680 QQRLAAEQELIRLRAETEQGEQQRQLL---EEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTS 1756
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLdelEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1757 EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAE 1836
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1837 NERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKA 1916
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1917 ELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEAR 1996
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1997 RLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAER 2076
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410
....*....|....*
gi 1920237982 2077 EAAQSRRQVEEAERL 2091
Cdd:COG5278 483 ALAEAEAAAALAAAA 497
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1909-2391 |
7.09e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1909 EKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERvQKSLAAEEEAARQRKAALEEVERL 1988
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1989 KAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRseaeaARRAAEEAE 2068
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-----LQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2069 AARERAEREAAQSRRQVEEAERLKQsAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFA 2148
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2149 EQAL---------RQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAArqrgqveEELFSLRVQMEELGKLKA 2219
Cdd:COG4717 282 VLGLlallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP-------EELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2220 RIE-AENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLkekmqAVQEATR 2298
Cdd:COG4717 355 EAEeLEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-----EALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2299 LKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQ-ETQGFQKTLETERQRQLEMSAEAER--LRLRVAE--MSRAQARA 2373
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEewAALKLALelLEEAREEY 509
|
490
....*....|....*....
gi 1920237982 2374 EEDAR-RFRKQAEDIGERL 2391
Cdd:COG4717 510 REERLpPVLERASEYFSRL 528
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2179-2274 |
7.32e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2179 LDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALvlrdkdsAQRLLQEEAEKMKQVAEEAARLS 2258
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQEL-------EAQLEQLQEKAAETSQERKQKRK 219
|
90
....*....|....*.
gi 1920237982 2259 VAAQEAARLRQLAEED 2274
Cdd:PRK11448 220 EITDQAAKRLELSEEE 235
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
988-1585 |
7.34e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 988 EPARECAQRITEQQKAQAEVDGLGKGVARLSaeaekvLALPepspaAPTLRSELEltlGKLEQVRSLSAIYlEKLKTISL 1067
Cdd:PRK10246 254 ELQQEASRRQQALQQALAAEEKAQPQLAALS------LAQP-----ARQLRPHWE---RIQEQSAALAHTR-QQIEEVNT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1068 VIRSTQEAEEVLRAHeeQLKEAQAVPATLPELeatkaalkklrAQAEAQQPVFDALRDELRG-----AQEVGERLQQRhg 1142
Cdd:PRK10246 319 RLQSTMALRARIRHH--AAKQSAELQAQQQSL-----------NTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLR-- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1143 erdveveRWRERVTLLLERWQAVLAQT-----DVRQRELEQLGRQlRYYRESADPLGAWLRDAKQRQEQIQAvplANSQA 1217
Cdd:PRK10246 384 -------QWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQV---AIQNV 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1218 VREQLRQEKALLEDIERHGEKVEE-------CQRFAKqyinaIKDYELQ--------------------LVTYKAqLEPV 1270
Cdd:PRK10246 453 TQEQTQRNAALNEMRQRYKEKTQQladvktiCEQEAR-----IKDLEAQraqlqagqpcplcgstshpaVEAYQA-LEPG 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1271 ASPAKKPKVQSGSESIIQEYVDLRtrySELSTLTSQYIRFISETLRRMEEEERLAEQQRaeererlaEVEAALEKQRQLA 1350
Cdd:PRK10246 527 VNQSRLDALEKEVKKLGEEGAALR---GQLDALTKQLQRDESEAQSLRQEEQALTQQWQ--------AVCASLNITLQPQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1351 EAHAQ-AKAQAEREAQGLQRRMQEEVarrEEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQV--EAAERSRL--RIE 1425
Cdd:PRK10246 596 DDIQPwLDAQEEHERQLRLLSQRHEL---QGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLpqEDEEASWLatRQQ 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1426 EEIRVVRLQLEATERQRGGAE--------GELQALRARAEEAEAQK-RQAQEEAERLRRQVQ-------DETQRKRQAEA 1489
Cdd:PRK10246 673 EAQSWQQRQNELTALQNRIQQltplletlPQSDDLPHSEETVALDNwRQVHEQCLSLHSQLQtlqqqdvLEAQRLQKAQA 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1490 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLrqaeaERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERT 1569
Cdd:PRK10246 753 QFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNL-----ENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQI 827
|
650
....*....|....*.
gi 1920237982 1570 LKEEHVAVVQLREEAT 1585
Cdd:PRK10246 828 QQELAQLAQQLRENTT 843
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2209-2504 |
7.60e-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: 42.59 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2209 VQMEE---LGKLKARIEAEN-RALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLA-EEDLAQQRALAE 2283
Cdd:pfam15964 341 VQMTEeanFEKTKALIQCEQlKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLAlSQNVAQLEAQVE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2284 KMLKEKMQAVQEATrlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLAQETQgfqKTLETERQRQLEMS-AEAERLRL 2361
Cdd:pfam15964 421 KVTREKNSLVSQLE--EAQKQLASQEMDVTKVCGEmRYQLNQTKMKKDEAEKEH---REYRTKTGRQLEIKdQEIEKLGL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2362 RVAEMSRAQARAEEDARRFRKQAEDIGERLYRTE----LATQEKVMLVQTL----ETQRQQSDRDAERLREAIAELE--H 2431
Cdd:pfam15964 496 ELSESKQRLEQAQQDAARAREECLKLTELLGESEhqlhLTRLEKESIQQSFsneaKAQALQAQQREQELTQKMQQMEaqH 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2432 EKD----------------KLKQEAQLLQLKSEEM-QTVRQE--QLLQETQALQQSFLSEK-------DSLLQRERCIEQ 2485
Cdd:pfam15964 576 DKTvneqyslltsqntfiaKLKEECCTLAKKLEEItQKSRSEveQLSQEKEYLQDRLEKLQkrneeleEQCVQHGRMHER 655
|
330
....*....|....*....
gi 1920237982 2486 EKAKLEQLFQDEVAKAQAL 2504
Cdd:pfam15964 656 MKQRLRQLDKHCQATAQQL 674
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2161-2504 |
7.61e-03 |
|
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: 42.70 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2161 ELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELG----KLKARIEA-ENralvlrDKDS 2235
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNnkynDLKKQKEElEN------ELNL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2236 AQRLLQEEAEKMKQVAEEAAR----LSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQ 2309
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKlellLSNLKKKIQKNKSLESQisELKKQNNQLKDNIEKKQQEINE---KTTEISNTQTQ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2310 -KELAQEQarrlQEDKEQMAQQLAQETQGFQKTLETERQRQlEMSAEAERLRlrvaemsraqaraeedarrfRKQAEDIG 2388
Cdd:TIGR04523 255 lNQLKDEQ----NKIKKQLSEKQKELEQNNKKIKELEKQLN-QLKSEISDLN--------------------NQKEQDWN 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2389 ERLyRTELATQEKVmlVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQlkseemqtvrqEQLLQETQALQQs 2468
Cdd:TIGR04523 310 KEL-KSELKNQEKK--LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQ-----------RELEEKQNEIEK- 374
|
330 340 350
....*....|....*....|....*....|....*.
gi 1920237982 2469 FLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQAL 2504
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK 410
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1726-1847 |
7.61e-03 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 42.61 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1726 ELEAELAKVRAEM--EVLLASKARAEEesrstseKSKQRLEAEAGRFR---ELAEEAARLRALAEEAKRQRQLAEEDAVR 1800
Cdd:pfam04147 155 EEEPERKKSKKEVmeEVIAKSKLHKYE-------RQKAKEEDEELREEldkELKDLRSLLSGSKRPKPEQAKKPEEKPDR 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237982 1801 QRAEAE-----RVLA-EKLAAISEatRLKTEAEIALKEKE----AENERLRRLAEDE 1847
Cdd:pfam04147 228 KKPDDDydklvRELAfDKRAKPSD--RTKTEEELAEEEKErlekLEEERLRRMRGEE 282
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1152-1423 |
7.77e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1152 RERVTLLLERWQAVLAQTDVR---QRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKAL 1228
Cdd:COG4942 2 RKLLLLALLLALAAAAQADAAaeaEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1229 LEDIERHGEKVEECQRFAKQYINAIKdyELQLVTYKAQLEPvaspakKPKVQSGSESIIQEYvdlrtRYSELSTLTSQYI 1308
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELA--ELLRALYRLGRQP------PLALLLSPEDFLDAV-----RRLQYLKYLAPAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1309 RFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRqlaeahaQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQ 1388
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERAELEALLAELEEER-------AALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
250 260 270
....*....|....*....|....*....|....*
gi 1920237982 1389 KRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLR 1423
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1652-1792 |
8.05e-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: 41.51 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1652 KAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA-- 1729
Cdd:pfam12037 52 KKQEQ-TRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELlr 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237982 1730 ---ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA-GRFRELAE-EAARLRALAEEAKRQRQ 1792
Cdd:pfam12037 131 kqeESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAeARAKEEREnEDLNLEQLREKANEERE 198
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2083-2464 |
8.23e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2083 RQVEEAERlkqsaeeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAeQALRQKAQVEQEL 2162
Cdd:pfam07888 73 RQRRELES--------------------RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKD-ALLAQRAAHEARI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2163 TALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRAL--VLRDKDSAQRLL 2240
Cdd:pfam07888 132 RELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELrnSLAQRDTQVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2241 QEEAEKMKQVAEEAARlSVAAQEAAR--LRQLAEEDLAQQRALAekMLKEKMQAVQeATRLKAEAELLQQQKELAQ---- 2314
Cdd:pfam07888 212 QDTITTLTQKLTTAHR-KEAENEALLeeLRSLQERLNASERKVE--GLGEELSSMA-AQRDRTQAELHQARLQAAQltlq 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2315 --EQARRLQEDKEQMaqqlAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEmsraqaraeedARRFRKQAEdigerly 2392
Cdd:pfam07888 288 laDASLALREGRARW----AQERETLQQSAEADKDRIEKLSAELQRLEERLQE-----------ERMEREKLE------- 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 2393 rTELATQEKVMLVQTLETQRQQSDrdaerLREAIAELEHEKDKLKQEAQllqlksEEMQTVRQEQLLQETQA 2464
Cdd:pfam07888 346 -VELGREKDCNRVQLSESRRELQE-----LKASLRVAQKEKEQLQAEKQ------ELLEYIRQLEQRLETVA 405
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1306-1500 |
8.48e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1306 QYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahaqakAQAEREAQgLQRRMQEEVARREEVAVEA 1385
Cdd:pfam13868 156 RILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQD---------EKAERDEL-RAKLYQEEQERKERQKERE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1386 QEQKRsiQEELQHLRQSSEAEIQAKARQvEAAERSRLRIEEEiRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQ 1465
Cdd:pfam13868 226 EAEKK--ARQRQELQQAREEQIELKERR-LAEEAEREEEEFE-RMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
170 180 190
....*....|....*....|....*....|....*
gi 1920237982 1466 AQEEAERLRRQVQDETQRKRQAEAELALRVQAEAE 1500
Cdd:pfam13868 302 REEQRAAEREEELEEGERLREEEAERRERIEEERQ 336
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1660-1753 |
8.50e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.13 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1660 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLraeteqgEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEME 1739
Cdd:pfam20492 21 ETKKAQEELEESEETAEELEEERRQAEEEAERL-------EQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIA 93
|
90
....*....|....
gi 1920237982 1740 VLLASKARAEEESR 1753
Cdd:pfam20492 94 RLEEEVERKEEEAR 107
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3658-3694 |
8.80e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 36.69 E-value: 8.80e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1920237982 3658 RYLYGTGCVAGIYRPGSRQTLTIYQALKKGQLSAEVA 3694
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1192-1392 |
9.04e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1192 PLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKVEECQRfakqyinAIKDYELQLVTYKAQL-EPV 1270
Cdd:PRK11637 37 AFSAHASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASR-------KLRETQNTLNQLNKQIdELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1271 ASPAKKPKVQSGSESIIQEYVDLRTRYSE-------LSTLTSQ-------YIRFISE----------------TLRRMEE 1320
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAAFRQGEhtglqliLSGEESQrgerilaYFGYLNQarqetiaelkqtreelAAQKAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1321 EERLAEQQ----------------RAEERERLAEVEAALEK-QRQLAE--------------AHAQAKAQAEREAQGLQR 1369
Cdd:PRK11637 190 EEKQSQQKtllyeqqaqqqkleqaRNERKKTLTGLESSLQKdQQQLSElranesrlrdsiarAEREAKARAEREAREAAR 269
|
250 260
....*....|....*....|....
gi 1920237982 1370 -RMQEEVARREEVAVEAQEQKRSI 1392
Cdd:PRK11637 270 vRDKQKQAKRKGSTYKPTESERSL 293
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2159-2589 |
9.06e-03 |
|
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: 42.12 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2159 EQELTALRLQLEETDHQKSILDEELQRLKAEVTeAARQRGQV-EEELFSLRVQMEElgklKARIEAEnRALVLRDKDSAQ 2237
Cdd:pfam10174 302 ESELLALQTKLETLTNQNSDCKQHIEVLKESLT-AKEQRAAIlQTEVDALRLRLEE----KESFLNK-KTKQLQDLTEEK 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2238 RLLQEEAEKMKQVAEEAARLSVAAQEaaRLRQLAEEDLAQQRALAEkmLKEKMQAVQEATRLKAEAelLQQQKELAQEQA 2317
Cdd:pfam10174 376 STLAGEIRDLKDMLDVKERKINVLQK--KIENLQEQLRDKDKQLAG--LKERVKSLQTDSSNTDTA--LTTLEEALSEKE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2318 R---RLQEDKEQMAQQLAQEtqgfqktLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRT 2394
Cdd:pfam10174 450 RiieRLKEQREREDRERLEE-------LESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2395 ELATQEKVMLVQTLETQRQ--QSDRDAERLREAIAelehekDKLKQEAQLLQLKSEEMQTVRqeqllqetqalqqsflSE 2472
Cdd:pfam10174 523 EIAVEQKKEECSKLENQLKkaHNAEEAVRTNPEIN------DRIRLLEQEVARYKEESGKAQ----------------AE 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2473 KDSLLQRERCIEQEK-------AKLEQLFQDEVaKAQALREEQQRQQQQMQQEKQqlAASMEEARRRQHEAEEGVRRQQ- 2544
Cdd:pfam10174 581 VERLLGILREVENEKndkdkkiAELESLTLRQM-KEQNKKVANIKHGQQEMKKKG--AQLLEEARRREDNLADNSQQLQl 657
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1920237982 2545 ----EELQRLAQQQQQQEKLLAEENQRLRERLQHLEE---ERRAALarsEEI 2589
Cdd:pfam10174 658 eelmGALEKTRQELDATKARLSSTQQSLAEKDGHLTNlraERRKQL---EEI 706
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1313-1426 |
9.15e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.02 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1313 ETLRRMEEEERLAEQQRA-EERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGL-QRRMQEEVARREEVAVEAQEQKR 1390
Cdd:pfam05672 11 EAARILAEKRRQAREQRErEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237982 1391 SIQEELQHLRQSSEAeiqAKARQVEAAERSRLRIEE 1426
Cdd:pfam05672 91 REQEEQERLQKQKEE---AEAKAREEAERQRQEREK 123
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1457-1520 |
9.29e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.16 E-value: 9.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237982 1457 EEAEAQKRQAQEEAERLRrqvQDETQRKRQAE--AELALRVQAEAEAAREKQRALQALEELRLQAE 1520
Cdd:PLN02316 253 EKRRELEKLAKEEAERER---QAEEQRRREEEkaAMEADRAQAKAEVEKRREKLQNLLKKASRSAD 315
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1316-1411 |
9.34e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 39.60 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1316 RRMEEEERLAEQQRAEERERLAEVEA-ALEKQRQLAEAHAQAK---AQAEREAQGLqrrmqeevaRREEVAV---EAQEQ 1388
Cdd:PRK07353 32 KVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARKQAQaviAEAEAEADKL---------AAEALAEaqaEAQAS 102
|
90 100
....*....|....*....|...
gi 1920237982 1389 KRSIQEELQHLRQSSEAEIQAKA 1411
Cdd:PRK07353 103 KEKARREIEQQKQAALAQLEQQV 125
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1310-1526 |
9.48e-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: 40.82 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1310 FISETLRRMEEEERLAEQQRAEERERLAEVEaalekqRQLAEAHAQAKaQAEREAqglqRRMQEEVARREEVAVEAQEQK 1389
Cdd:pfam04012 12 NIHEGLDKAEDPEKMLEQAIRDMQSELVKAR------QALAQTIARQK-QLERRL----EQQTEQAKKLEEKAQAALTKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1390 RsiqeelQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE 1469
Cdd:pfam04012 81 N------EELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTSL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237982 1470 AERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQaLEELRLQAEEAERRL 1526
Cdd:pfam04012 155 GSLSTSSATDSFERIEEKIEEREARADAAAELASAVDLDAK-LEQAGIQMEVSEDVL 210
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1911-2412 |
9.68e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.15 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1911 AAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKA 1990
Cdd:COG3899 736 PPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGEL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1991 KVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQ-----KEQELQQTLQQEQSVLERLRSEAEAARRAAE 2065
Cdd:COG3899 816 ALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAgletgDAALALLALAAAAAAAAAAAALAAAAAAAAR 895
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2066 EAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHK 2145
Cdd:COG3899 896 LLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAA 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2146 QFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAEN 2225
Cdd:COG3899 976 AAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAA 1055
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2226 RALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2305
Cdd:COG3899 1056 AAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAAL 1135
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2306 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAE 2385
Cdd:COG3899 1136 LLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALL 1215
|
490 500
....*....|....*....|....*..
gi 1920237982 2386 DIGERLYRTELATQEKVMLVQTLETQR 2412
Cdd:COG3899 1216 ALEAAALLLLLLLAALALAAALLALRL 1242
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1680-1942 |
9.73e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1680 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRstseKS 1759
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVK----EL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1760 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAVRQR--------------AEAERVLAEKLAaiseatRLKTE 1825
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGG--SIDKLRKEierlewrqqtevlsPEEEKELVEKIK------ELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 1826 AEIALKEKEAENERLRRLAEDEAFQrrlleEQAAQHKADIEARLAQLRKASES------ELERQKGLVEDTLRQRRQVEE 1899
Cdd:COG1340 149 LEKAKKALEKNEKLKELRAELKELR-----KEAEEIHKKIKELAEEAQELHEEmielykEADELRKEADELHKEIVEAQE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1920237982 1900 EILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQE 1942
Cdd:COG1340 224 KADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2145-2336 |
9.94e-03 |
|
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: 42.12 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2145 KQFAEQALRQKAQVEQELTALRlqleETDHQKSILDEELQRLkaevtEAARQRGQVEEELFSLRVQMEELGKLKARIEAE 2224
Cdd:pfam10174 568 ARYKEESGKAQAEVERLLGILR----EVENEKNDKDKKIAEL-----ESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLL 638
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237982 2225 NRALVLRD---KDSAQRLLQE---EAEKMKQVAEEA-ARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAT 2297
Cdd:pfam10174 639 EEARRREDnlaDNSQQLQLEElmgALEKTRQELDATkARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAAI 718
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170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1920237982 2298 RLK----AEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQ 2336
Cdd:pfam10174 719 SEKdaniALLELSSSKKKKTQEEVMALKREKDRLVHQLKQQTQ 761
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