|
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 ... |
54-158 |
1.91e-75 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 246.16 E-value: 1.91e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 54 DRVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNI 133
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 736215636 134 RNDDIADGNPKLTLGLIWTIILHFQ 158
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
51-169 |
3.92e-73 |
|
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: 240.31 E-value: 3.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 51 DERDRVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 130
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 736215636 131 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQSD 169
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
50-167 |
3.17e-70 |
|
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: 232.57 E-value: 3.17e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 50 ADERDRVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 129
Cdd:cd21236 11 KDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVK 90
|
90 100 110
....*....|....*....|....*....|....*...
gi 736215636 130 LVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQ 167
Cdd:cd21236 91 LVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
171-276 |
1.06e-66 |
|
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: 221.43 E-value: 1.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 171 MTAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLD 250
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 736215636 251 PEDVDVLHPDEKSIITYVSSLYDAMP 276
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
172-276 |
4.01e-63 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 211.10 E-value: 4.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDP 251
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 736215636 252 EDVDVLHPDEKSIITYVSSLYDAMP 276
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
51-168 |
1.99e-62 |
|
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: 209.50 E-value: 1.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 51 DERDRVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 130
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 736215636 131 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQS 168
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
172-276 |
4.96e-57 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 193.66 E-value: 4.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERdLGVTRLLDP 251
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 736215636 252 EDVDVLHPDEKSIITYVSSLYDAMP 276
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
170-276 |
1.71e-50 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 175.23 E-value: 1.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 170 DMTAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERdLGVTRLL 249
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 736215636 250 DPEDVDVLHPDEKSIITYVSSLYDAMP 276
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
56-159 |
4.97e-50 |
|
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: 173.72 E-value: 4.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 56 VQKKTFTKWVNKHLMKSQR-HITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 134
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 736215636 135 NDDIADGNPKLTLGLIWTIILHFQI 159
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
50-155 |
5.17e-49 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 171.40 E-value: 5.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 50 ADERDRVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQV 128
Cdd:cd21246 10 ADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQRV 89
|
90 100
....*....|....*....|....*..
gi 736215636 129 KLVNIRNDDIADGNPKLTLGLIWTIIL 155
Cdd:cd21246 90 HLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
52-159 |
3.55e-45 |
|
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: 160.23 E-value: 3.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 52 ERDRVQKKTFTKWVNKHLMKSQR--HITDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 127
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 736215636 128 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 159
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
172-272 |
3.83e-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: 159.88 E-value: 3.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDP 251
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 736215636 252 EDVDVLHPDEKSIITYVSSLY 272
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
50-155 |
3.85e-44 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 157.07 E-value: 3.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 50 ADERDRVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLkHRQV 128
Cdd:cd21193 10 QEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL-KTKV 88
|
90 100
....*....|....*....|....*..
gi 736215636 129 KLVNIRNDDIADGNPKLTLGLIWTIIL 155
Cdd:cd21193 89 RLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
172-272 |
6.15e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 156.40 E-value: 6.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDP 251
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 736215636 252 EDVDVLHPDEKSIITYVSSLY 272
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
50-155 |
9.77e-43 |
|
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: 154.41 E-value: 9.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 50 ADERDRVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQV 128
Cdd:cd21318 32 ADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQRV 111
|
90 100
....*....|....*....|....*..
gi 736215636 129 KLVNIRNDDIADGNPKLTLGLIWTIIL 155
Cdd:cd21318 112 HLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
50-272 |
4.35e-42 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 166.65 E-value: 4.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 50 ADERDRVQKKTFTKWVNKHLMKS-QRHITDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHR 126
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 127 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQsddMTAKEKLLLWSQRMVEGYQ-GLRCDNFTTGWRDGKL 205
Cdd:COG5069 83 GVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGE---LTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 206 FNAIIHKHRPTLIDMGKVYRQSNQE--NLEQAFSVAERDLGVTRLLDPEDV-DVLHPDEKSIITYVSSLY 272
Cdd:COG5069 160 FSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
50-155 |
1.08e-41 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 150.97 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 50 ADERDRVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQV 128
Cdd:cd21317 25 ADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLKEQKV 104
|
90 100
....*....|....*....|....*..
gi 736215636 129 KLVNIRNDDIADGNPKLTLGLIWTIIL 155
Cdd:cd21317 105 HLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
52-159 |
1.55e-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: 149.64 E-value: 1.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 52 ERDRVQKKTFTKWVNKHLMK--SQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 127
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKlsQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 736215636 128 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 159
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1454-2652 |
2.46e-39 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 162.69 E-value: 2.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1454 DVAVDAEQQKQNIQHELHHLKSLSEQEIKSKSQQLEHALVSH----TKIEEEIHTIRIQLEMTIKQ-----KKTAESEL- 1523
Cdd:NF041483 69 DIGYQAEQLLRNAQIQADQLRADAERELRDARAQTQRILQEHaehqARLQAELHTEAVQRRQQLDQelaerRQTVESHVn 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1524 ------QQLRDKA------------AEAEKLRKAAQEDAERL----RKQVAEETQKKKNAEDELKRKSEAEKE-----AA 1576
Cdd:NF041483 149 envawaEQLRARTesqarrlldesrAEAEQALAAARAEAERLaeeaRQRLGSEAESARAEAEAILRRARKDAErllnaAS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1577 KQKQKALDDLQKF-----------KMQAEE----AERRMKQAeEEKLRQI-----KVVEEvAQKSAATQLQShSMSFNVK 1636
Cdd:NF041483 229 TQAQEATDHAEQLrsstaaesdqaRRQAAElsraAEQRMQEA-EEALREAraeaeKVVAE-AKEAAAKQLAS-AESANEQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1637 ---------------ASKLEESLKKEQGTVLQ-LQEEAEQLRKqqEEANKAREQAEKELETWRQK-ANEALRLRLQAEEE 1699
Cdd:NF041483 306 rtrtakeeiarlvgeATKEAEALKAEAEQALAdARAEAEKLVA--EAAEKARTVAAEDTAAQLAKaARTAEEVLTKASED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1700 AQKKSK-TQEEAERQKVEAERDAKK-RAKAEDAALKQKDNAEKELEKQRtfAEQVAQQklsaeQECIRLKADfdhAEQQR 1777
Cdd:NF041483 384 AKATTRaAAEEAERIRREAEAEADRlRGEAADQAEQLKGAAKDDTKEYR--AKTVELQ-----EEARRLRGE---AEQLR 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1778 GLLDNELQRLKKE-----VSATEKQRKLLEEELAKVRSEMDSL-LKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEA 1851
Cdd:NF041483 454 AEAVAEGERIRGEarreaVQQIEEAARTAEELLTKAKADADELrSTATAESERVRTEAIERATTLRRQAEETLERTRAEA 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1852 TRLRSVAEE-AKKQRQTAEEEAARQRAEAEKILKEKLA-AINEATRLRTEAEIALKAKE-------AENERLKRKAEDEA 1922
Cdd:NF041483 534 ERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEERLTAAEealadarAEAERIRREAAEET 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1923 YQrklLEDQAAqhkhdiqEKIIHLKSSSDSEMVRQKTIVEETLRQKKIVEEEIhiirinfekASKGKSDLENELKKLKVI 2002
Cdd:NF041483 614 ER---LRTEAA-------ERIRTLQAQAEQEAERLRTEAAADASAARAEGENV---------AVRLRSEAAAEAERLKSE 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2003 AEETqKSKLKAEAEAeklkklaaeeekkrkeseekvkritAAE---EEAARQCKAAQEEVARLEKKADEANKQKEKaeke 2079
Cdd:NF041483 675 AQES-ADRVRAEAAA-------------------------AAErvgTEAAEALAAAQEEAARRRREAEETLGSARA---- 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2080 aekqvivakEAAQKCSSAEQKAQEVLSKnkedslAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAE--AEKQK 2157
Cdd:NF041483 725 ---------EADQERERAREQSEELLAS------ARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDsvAGLQE 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2158 KSAEEEAAKQAKAQKDAEKLKKAAEEEASkRAAAEAEALKQKKQADA----EMAKHKKEADQALKLKSQVEKELTMVKLR 2233
Cdd:NF041483 790 QAEEEIAGLRSAAEHAAERTRTEAQEEAD-RVRSDAYAERERASEDAnrlrREAQEETEAAKALAERTVSEAIAEAERLR 868
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2234 LDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVR----IQMDELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEA 2309
Cdd:NF041483 869 SDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDEARAEA 948
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2310 GKMKSLA------------EEAARLSVEAEET--------ARQRQIAESNLAEQRALAEKMLKEkmqAIQEATKLKAEA- 2368
Cdd:NF041483 949 ERVRADAaaqaeqliaeatGEAERLRAEAAETvgsaqqhaERIRTEAERVKAEAAAEAERLRTE---AREEADRTLDEAr 1025
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2369 QELQKQKDQAQEKAKKLLEDKQQIQQRL--DKETEGFQKSLEAERKRQLEVSA---EAETLrlkvkeLSDAQSKAENEAK 2443
Cdd:NF041483 1026 KDANKRRSEAAEQADTLITEAAAEADQLtaKAQEEALRTTTEAEAQADTMVGAarkEAERI------VAEATVEGNSLVE 1099
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2444 KFKKQADEAkarLKDTEKQSTeTVVQKLETQRLQSTREADGLKEaiadlekereklkkeaeelqNKSNKMANTQKEEIEQ 2523
Cdd:NF041483 1100 KARTDADEL---LVGARRDAT-AIRERAEELRDRITGEIEELHE--------------------RARRESAEQMKSAGER 1155
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2524 QKAIIQKSFISERELLLKRQKAVEDEKKKLQKQFEDEVKKAEALKDEQERQRKLMEEEKKKLQAIMDAavkkqkEAEADM 2603
Cdd:NF041483 1156 CDALVKAAEEQLAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKAELVREAEKIKAEAEA------EAKRTV 1229
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*
gi 736215636 2604 KNKQTEMEVLEKKRLDqekqLGAENQKLREKLQCLE------GASKQSATKQVAS 2652
Cdd:NF041483 1230 EEGKRELDVLVRRRED----INAEISRVQDVLEALEsfeapsGGGKGNGVKAGAA 1280
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
172-272 |
3.27e-39 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 143.22 E-value: 3.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDP 251
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
|
90 100
....*....|....*....|.
gi 736215636 252 EDVDVLHPDEKSIITYVSSLY 272
Cdd:cd21319 85 EDVFTENPDEKSIITYVVAFY 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1494-2390 |
9.30e-39 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 161.46 E-value: 9.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1494 SHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLR--KQVAEETQKKKNAE--DELKRKS 1569
Cdd:PTZ00121 1064 AHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEeaKKKAEDARKAEEARkaEDARKAE 1143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1570 EAEK-EAAKQKQKA--LDDLQKFKmQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQSHSMSFNVKasKLEESLKK 1646
Cdd:PTZ00121 1144 EARKaEDAKRVEIArkAEDARKAE-EARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEER--KAEEARKA 1220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1647 EQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQeeaERQKVEAERDAKKRAK 1726
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD---ELKKAEEKKKADEAKK 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1727 AEDaaLKQKDNAEKELEKQRTfAEQVAQQKLSAEQECIRLKADFDHAEQqrglldnelqrlKKEVSATEKQRKLLEEELA 1806
Cdd:PTZ00121 1298 AEE--KKKADEAKKKAEEAKK-ADEAKKKAEEAKKKADAAKKKAEEAKK------------AAEAAKAEAEAAADEAEAA 1362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1807 KVRSEMDsllKMKTEAEKKTMSNTEKSKQllesEALKMKQLADEATRLRSVAEEAKKQrqtaeeEAARQRAEAekiLKEK 1886
Cdd:PTZ00121 1363 EEKAEAA---EKKKEEAKKKADAAKKKAE----EKKKADEAKKKAEEDKKKADELKKA------AAAKKKADE---AKKK 1426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1887 LAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSSDSEMVRQKTiveETLR 1966
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA---DEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1967 QKkivEEEihiirinfekasKGKSDlenELKKlkviAEETQKS-KLKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAE 2045
Cdd:PTZ00121 1504 KA---AEA------------KKKAD---EAKK----AEEAKKAdEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2046 E-EAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAK----EAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKE 2120
Cdd:PTZ00121 1562 EkKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2121 EFENAKRLAQAAEKAKEKAEKEAallrQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEeaskraAAEAEALKQKK 2200
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAA----EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE------AKKAEELKKKE 1711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2201 QADAEMAKHKKEADQALKLKSQVEKeltmvklRLDETDKQKAlldEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELL 2280
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAK-------KEAEEDKKKA---EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2281 KLKLKIEEQNRSLM--KKDKD-KTQKVLAEEAGKMKSLAEEAARlsvEAEETARQRQIAESNLaeQRALAEKMLKEKMQA 2357
Cdd:PTZ00121 1782 EEELDEEDEKRRMEvdKKIKDiFDNFANIIEGGKEGNLVINDSK---EMEDSAIKEVADSKNM--QLEEADAFEKHKFNK 1856
|
890 900 910
....*....|....*....|....*....|...
gi 736215636 2358 IQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQ 2390
Cdd:PTZ00121 1857 NNENGEDGNKEADFNKEKDLKEDDEEEIEEADE 1889
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
56-157 |
2.36e-38 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 140.23 E-value: 2.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 56 VQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 133
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 736215636 134 RNDDIADGNPKLTLGLIWTIILHF 157
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
52-159 |
2.44e-38 |
|
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: 140.35 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 52 ERDRVQKKTFTKWVNKHLMKSQ--RHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 129
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 736215636 130 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 159
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
171-276 |
2.54e-38 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 140.53 E-value: 2.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 171 MTAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLD 250
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 736215636 251 PEDVDVLHPDEKSIITYVSSLYDAMP 276
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
159-274 |
2.81e-38 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 140.58 E-value: 2.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 159 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSV 238
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 736215636 239 AERDLGVTRLLDPED-VDVLHPDEKSIITYVSSLYDA 274
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
54-155 |
7.23e-38 |
|
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: 139.06 E-value: 7.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 54 DRVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQVKLVN 132
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 736215636 133 IRNDDIADGNPKLTLGLIWTIIL 155
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1534-2448 |
2.97e-37 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 156.45 E-value: 2.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1534 EKLRKAAQEDAERLRKQVAEEtQKKKNAEDELKRKSEA-EKEAAKQKQKALDDLQKFKMQAEEA-ERRMKQAEEEKLRQI 1611
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDIIDE-DIDGNHEGKAEAKAHVgQDEGLKPSYKDFDFDAKEDNRADEAtEEAFGKAEEAKKTET 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1612 KVVEEV-----AQKSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQqEEANKAREQAEKEletwrqKA 1686
Cdd:PTZ00121 1109 GKAEEArkaeeAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKA-EEARKAEDAKKAE------AA 1181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1687 NEALRLRlqAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAalkQKDNAEKELEKQRTFAEQV--AQQKLSAEQECI 1764
Cdd:PTZ00121 1182 RKAEEVR--KAEELRKAEDARKAEAARKAEEERKAEEARKAEDA---KKAEAVKKAEEAKKDAEEAkkAEEERNNEEIRK 1256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1765 RLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLlkmKTEAEKKTMSNTEKSKqlleseALKM 1844
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA---KKKAEEAKKADEAKKK------AEEA 1327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1845 KQLADEAtrlRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAEN--ERLKRKAEDEA 1922
Cdd:PTZ00121 1328 KKKADAA---KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkaDEAKKKAEEDK 1404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1923 YQRKLLEDQAAQHKHDIQEKiihlkssSDSEMVRQKTIVEETLRQKKIVEEeihiirinFEKASKGKSDLENELKKlkvi 2002
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAK-------KKAEEKKKADEAKKKAEEAKKADE--------AKKKAEEAKKAEEAKKK---- 1465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2003 AEETQKS-KLKAEAEaEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEvarleKKADEANKQKEKAEKEAe 2081
Cdd:PTZ00121 1466 AEEAKKAdEAKKKAE-EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA-----KKADEAKKAEEAKKADE- 1538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2082 kqvivAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLaqaaekakekaekeaallrQKAAEAEKQKKSAE 2161
Cdd:PTZ00121 1539 -----AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL-------------------RKAEEAKKAEEARI 1594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2162 EEAAKQAKAQKD--AEKLKKAAEEEASKRAAAEAEALKQK-KQADAEMAKHKKEADQALKLKSQVEKELTMVKlRLDETD 2238
Cdd:PTZ00121 1595 EEVMKLYEEEKKmkAEEAKKAEEAKIKAEELKKAEEEKKKvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA-KKAEED 1673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2239 KQKAlldEELQRVKGEVNDAVKQKAQVEDELAKVriqmdELLKlKLKIEEQNRSLMKKDKDKTQKVLAEEAgkmKSLAEE 2318
Cdd:PTZ00121 1674 KKKA---EEAKKAEEDEKKAAEALKKEAEEAKKA-----EELK-KKEAEEKKKAEELKKAEEENKIKAEEA---KKEAEE 1741
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2319 AARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEaqelqKQKDQAQEKAKKLLEDKQQIQqrldk 2398
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE-----KRRMEVDKKIKDIFDNFANII----- 1811
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 736215636 2399 etegfqkslEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQ 2448
Cdd:PTZ00121 1812 ---------EGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKH 1852
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1956-2691 |
7.86e-37 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 154.91 E-value: 7.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1956 RQKTIVEETLRQKKIVEEEIhiirinfEKASKGKSDLENELKKLKVIAEETQKSKLKAEAE----AEKLKKLAAEEEKKR 2031
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEA-------KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEdarkAEEARKAEDAKRVEI 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2032 KESEEKVKRITAAEE-EAARQCKAAQ--EEVARLE--KKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLS 2106
Cdd:PTZ00121 1157 ARKAEDARKAEEARKaEDAKKAEAARkaEEVRKAEelRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2107 KNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAE---------AEKQKKSAE----EEAAKQAKAQKD 2173
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElkkaeekkkADEAKKAEEkkkaDEAKKKAEEAKK 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2174 AEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKEltmvKLRLDEtDKQKAlldEELQRVKG 2253
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA----EKKKEE-AKKKA---DAAKKKAE 1388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2254 EVNDAVKQKAQVEDELAKVriqmdELLKLKLKIEEQNRSLMKKDKDKTQkvlAEEAGKMKSLAEEAARLSVEAEETARQR 2333
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKA-----DELKKAAAAKKKADEAKKKAEEKKK---ADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2334 QIAESnlAEQRALAEKmLKEKMQAIQEATKLKAEAQELQKQKDQAQEKA---KKLLEDKQQIQQRLDKETEGFQKSLEAE 2410
Cdd:PTZ00121 1461 EAKKK--AEEAKKADE-AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAeakKKADEAKKAEEAKKADEAKKAEEAKKAD 1537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2411 RKRQLEVSAEAETLRlKVKELSDAQSKAENEAKKFKKQADEAKAR----LKDTEKQSTETVVQKLETQRLQSTREADGLK 2486
Cdd:PTZ00121 1538 EAKKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2487 EAIADLEKEREKLKKEAEELQNKsnKMANTQKEEIEQQKAIIQKSFISERELllkRQKAVEDEKK--KLQKQFEDEVKKA 2564
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLK--KKEAEEKKKAEELKKAEEENKIKAAEE---AKKAEEDKKKaeEAKKAEEDEKKAA 1691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2565 EALKDEQERQRKL------MEEEKKKLQAImdaavkKQKEAEADMKNKQTEMEVLEKKRLDQEKQLGAENQKlreKLQCL 2638
Cdd:PTZ00121 1692 EALKKEAEEAKKAeelkkkEAEEKKKAEEL------KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK---KIAHL 1762
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 736215636 2639 EGASKQSATKQVASKTIEVQTDVVSEEQLVTMTKVGTTKTVF-NGSVEVDGAKK 2691
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFdNFANIIEGGKE 1816
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
935-1012 |
8.67e-37 |
|
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: 134.65 E-value: 8.67e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 935 LSYQYLMRDIHIIKTWNVTMFKTLRVEEYRLALRNLELHYQDFLRDSQDSETFGAEDRMQVESNYNKANQHYNTMVSS 1012
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
168-272 |
2.18e-36 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 135.18 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 168 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTR 247
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 736215636 248 LLDPEDVDVLHPDEKSIITYVSSLY 272
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
51-159 |
6.94e-36 |
|
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: 133.51 E-value: 6.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 51 DERDRVQKKTFTKWVNKHLMKSQR-HITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 129
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 736215636 130 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 159
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
171-272 |
3.03e-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: 131.52 E-value: 3.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 171 MTAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLD 250
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 736215636 251 PEDVDVLHPDEKSIITYVSSLY 272
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1772-2634 |
4.78e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 149.14 E-value: 4.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1772 HAEQQRGL----LDNELQRLKKEVS--ATEKQRKLLEEelAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMK 1845
Cdd:PTZ00121 1065 HVGQDEGLkpsyKDFDFDAKEDNRAdeATEEAFGKAEE--AKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKA 1142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1846 QLADEATRLRSV-----AEEAKKQRQTAEEEAARQRAEAEKILKEKLAainEATRLRTEAEIALKAKEAENERL---KRK 1917
Cdd:PTZ00121 1143 EEARKAEDAKRVeiarkAEDARKAEEARKAEDAKKAEAARKAEEVRKA---EELRKAEDARKAEAARKAEEERKaeeARK 1219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1918 AEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSSDSEMVRQKTIVEETLRQKKIVEEEihiirinfekasKGKSDlenELK 1997
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE------------ARKAD---ELK 1284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1998 KLKVIAEETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKvkritaaeEEAARQCKAAQEEvARLEKKADEANKQKEKAE 2077
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA--------EEAKKKADAAKKK-AEEAKKAAEAAKAEAEAA 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2078 KEAEKQVIVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKaekeaallRQKAAEAEK-- 2155
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA--------KKKADEAKKka 1427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2156 QKKSAEEEAAKQAKAQKDAEKLKKAAEEeasKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKEltmvklrld 2235
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEE---AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA--------- 1495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2236 etdKQKAlldEELQRVKGEvndavKQKAQvEDELAKVRIQMDELLKL--KLKIEEQNRSLMKKDKDKTQKvlAEEAGKmk 2313
Cdd:PTZ00121 1496 ---KKKA---DEAKKAAEA-----KKKAD-EAKKAEEAKKADEAKKAeeAKKADEAKKAEEKKKADELKK--AEELKK-- 1559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2314 slAEEAARLSvEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQ 2393
Cdd:PTZ00121 1560 --AEEKKKAE-EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2394 QRLDKETEgfqksleaERKRQLEVSAEAETLRLKVKELSdaqSKAENEakkfKKQADEAKARLKDtEKQSTETVVQKLET 2473
Cdd:PTZ00121 1637 QLKKKEAE--------EKKKAEELKKAEEENKIKAAEEA---KKAEED----KKKAEEAKKAEED-EKKAAEALKKEAEE 1700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2474 QrlqstREADGLKEAIADLEKEREKLKKEAEELQNKSNKManTQKEEIEQQKAiiqksfiserelllKRQKAVEDEKKKL 2553
Cdd:PTZ00121 1701 A-----KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA--KKEAEEDKKKA--------------EEAKKDEEEKKKI 1759
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2554 QKQFEDEVKKAEALKDEQERQ-RKLMEEEKKKLQAIMDAAVKKQKEAEADMK----------NKQTEMEVLEKKRLDQEK 2622
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAViEEELDEEDEKRRMEVDKKIKDIFDNFANIIeggkegnlviNDSKEMEDSAIKEVADSK 1839
|
890
....*....|..
gi 736215636 2623 QLGAENQKLREK 2634
Cdd:PTZ00121 1840 NMQLEEADAFEK 1851
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
175-276 |
4.96e-35 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 130.63 E-value: 4.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 175 EKLLL-WSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDPED 253
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 736215636 254 VDVLHPDEKSIITYVSSLYDAMP 276
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
156-272 |
1.25e-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: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 156 HFQISDIQVNGQSDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQA 235
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 736215636 236 FSVAERDLGVTRLLDPEDVDVLHPDEKSIITYVSSLY 272
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
50-155 |
3.29e-34 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 130.55 E-value: 3.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 50 ADERDRVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQV 128
Cdd:cd21316 47 ADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRV 126
|
90 100
....*....|....*....|....*..
gi 736215636 129 KLVNIRNDDIADGNPKLTLGLIWTIIL 155
Cdd:cd21316 127 HLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
172-272 |
4.45e-34 |
|
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: 128.29 E-value: 4.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDP 251
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 736215636 252 EDVDVLHPDEKSIITYVSSLY 272
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1386-2214 |
2.13e-33 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 143.74 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1386 TETQRRLEDDEKASEKLKEEERKKMAEIQAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKrqdvavdAEQQKqn 1465
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARK-------AEDAK-- 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1466 iqhelhhlkslseqeiksksqqlehalvshtkieeeihtiriQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQ-EDA 1544
Cdd:PTZ00121 1153 ------------------------------------------RVEIARKAEDARKAEEARKAEDAKKAEAARKAEEvRKA 1190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1545 ERLRKqvAEETQKKKNAE--DELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSA 1622
Cdd:PTZ00121 1191 EELRK--AEDARKAEAARkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARR 1268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1623 ATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKArEQAEKELETWRQKANEAlrlRLQAEEEAQK 1702
Cdd:PTZ00121 1269 QAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAA---KKKAEEAKKA 1344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1703 KSKTQEEAERQKVEAERdAKKRAKAEDaalKQKDNAEKELEKQRTFAEQVAQ-QKLSAEQECIRLKADFDHAEQQRGLLD 1781
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEA-AEEKAEAAE---KKKEEAKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAAAAKKKA 1420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1782 NELQRLKKEVSATEKQRKLLEEelAKVRSEmdslLKMKTEAEKKTMSNTEKSKQLLESEALKMKqlADEATRlrsvAEEA 1861
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEE--AKKADE----AKKKAEEAKKAEEAKKKAEEAKKADEAKKK--AEEAKK----ADEA 1488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1862 KKQRQTAEEEA--ARQRAEAEKILKE--KLAAINEATRLRtEAEIALKAKEAENERLKRKAEDeayQRKLLEDQAAQHKH 1937
Cdd:PTZ00121 1489 KKKAEEAKKKAdeAKKAAEAKKKADEakKAEEAKKADEAK-KAEEAKKADEAKKAEEKKKADE---LKKAEELKKAEEKK 1564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1938 DIQEKiihLKSSSDSEMVRQKTiveETLRQkkIVEEEIHIIRINFEKASKGKSDlenELKKlkviaEETQKSKLKAEAEA 2017
Cdd:PTZ00121 1565 KAEEA---KKAEEDKNMALRKA---EEAKK--AEEARIEEVMKLYEEEKKMKAE---EAKK-----AEEAKIKAEELKKA 1628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2018 EKLKKLAAEEEKKRKESEEKVKRITAAEEEaaRQCKAAQEevarlEKKADEANKQKekaekeaekqvivakEAAQKCSSA 2097
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEE--NKIKAAEE-----AKKAEEDKKKA---------------EEAKKAEED 1686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2098 EQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKL 2177
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEE 1766
|
810 820 830
....*....|....*....|....*....|....*..
gi 736215636 2178 KKAAEEEASKRAAAEAEALKqKKQADAEMAKHKKEAD 2214
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEEELD-EEDEKRRMEVDKKIKD 1802
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1389-2416 |
1.48e-32 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 140.35 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1389 QRRLEDDEKAseklkeeerkkmaeiqaeldkqkqIAEAQAksvikaeqEAQELKLKMKEEASKRQDVAVDA-EQQKQNIQ 1467
Cdd:NF041483 264 EQRMQEAEEA------------------------LREARA--------EAEKVVAEAKEAAAKQLASAESAnEQRTRTAK 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1468 HELHHLKSLSEQEIKSKSQQLEHALVShTKIEEEihtiRIQLEMTIKQK-KTAESELQQLRDKAAEAEKLRKAAQEDAER 1546
Cdd:NF041483 312 EEIARLVGEATKEAEALKAEAEQALAD-ARAEAE----KLVAEAAEKARtVAAEDTAAQLAKAARTAEEVLTKASEDAKA 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1547 LRKQVAEETQK-KKNAEDELKR-KSEAEKEAAKQKQKALDDLQKFKMQAEE--AERRMKQAEEEKLRQIKVVE-----EV 1617
Cdd:NF041483 387 TTRAAAEEAERiRREAEAEADRlRGEAADQAEQLKGAAKDDTKEYRAKTVElqEEARRLRGEAEQLRAEAVAEgerirGE 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1618 AQKSAATQLQShsmsfnvKASKLEESLKKEQGTVLQLQE----EAEQLRKQQ-EEANKAREQAEKELETWRQkanEALRL 1692
Cdd:NF041483 467 ARREAVQQIEE-------AARTAEELLTKAKADADELRStataESERVRTEAiERATTLRRQAEETLERTRA---EAERL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1693 RLQAEEEAQkksKTQEEAERQKVEAerdakkRAKAEDAALKQKDNAEKELEKQRTFAEqvaQQKLSAEQEcirLKADFDH 1772
Cdd:NF041483 537 RAEAEEQAE---EVRAAAERAAREL------REETERAIAARQAEAAEELTRLHTEAE---ERLTAAEEA---LADARAE 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1773 AEQQRGLLDNELQRLKKEvsATEKQRKL---LEEELAKVRSEMDSLLKmKTEAEKKTMSNTEKSKQLLESEALKmKQLAD 1849
Cdd:NF041483 602 AERIRREAAEETERLRTE--AAERIRTLqaqAEQEAERLRTEAAADAS-AARAEGENVAVRLRSEAAAEAERLK-SEAQE 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1850 EATRLRS--------VAEEAKKQRQTAEEEAARQRAEAEKILKEKLA-AINEATRLRTEAEIALKA-------KEAENER 1913
Cdd:NF041483 678 SADRVRAeaaaaaerVGTEAAEALAAAQEEAARRRREAEETLGSARAeADQERERAREQSEELLASarkrveeAQAEAQR 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1914 LKRKAEDEAYQRKLLEDQAAQHKHD--------IQEKIIHLKSSSDSEMVRQKTIVEET---LRQKKIVEEEihiiRINf 1982
Cdd:NF041483 758 LVEEADRRATELVSAAEQTAQQVRDsvaglqeqAEEEIAGLRSAAEHAAERTRTEAQEEadrVRSDAYAERE----RAS- 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1983 EKASKGKSDLENELKKLKVIAEETQKsklKAEAEAEKLKKLAAeeEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARL 2062
Cdd:NF041483 833 EDANRLRREAQEETEAAKALAERTVS---EAIAEAERLRSDAS--EYAQRVRTEASDTLASAEQDAARTRADAREDANRI 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2063 EKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKE 2142
Cdd:NF041483 908 RSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQH 987
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2143 AALLRqkaAEAEKQKKSAEEEAAKQ-AKAQKDAEKLKKAAEEEASKRAAAEAEalkqkkQADAEMAKHKKEADQaLKLKS 2221
Cdd:NF041483 988 AERIR---TEAERVKAEAAAEAERLrTEAREEADRTLDEARKDANKRRSEAAE------QADTLITEAAAEADQ-LTAKA 1057
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2222 QvEKELTMVKLRLDETDKQKALLDEELQRVKGEVndAVKQKAQVEdelaKVRIQMDELLKLKLKIEEQNRSLMKKDKDKT 2301
Cdd:NF041483 1058 Q-EEALRTTTEAEAQADTMVGAARKEAERIVAEA--TVEGNSLVE----KARTDADELLVGARRDATAIRERAEELRDRI 1130
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2302 QkvlaeeaGKMKSLAEEAARLSVEAEETARQR-----QIAESNLAEQRALAEKMLKEkmqAIQEATKLKAEaqelqkqkd 2376
Cdd:NF041483 1131 T-------GEIEELHERARRESAEQMKSAGERcdalvKAAEEQLAEAEAKAKELVSD---ANSEASKVRIA--------- 1191
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|
gi 736215636 2377 qAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLE 2416
Cdd:NF041483 1192 -AVKKAEGLLKEAEQKKAELVREAEKIKAEAEAEAKRTVE 1230
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
55-160 |
1.68e-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: 124.49 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 55 RVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQ-VKLV 131
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 736215636 132 NIRNDDIADGNPKLTLGLIWTIILHFQIS 160
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
171-269 |
1.82e-32 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 123.69 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 171 MTAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLD 250
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 736215636 251 PEDVDVLHPDEKSIITYVS 269
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
56-159 |
3.59e-32 |
|
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: 122.81 E-value: 3.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 56 VQKKTFTKWVNKHLMKSQR-HITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 134
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 736215636 135 NDDIADGNPKLTLGLIWTIILHFQI 159
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
56-159 |
1.60e-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: 120.86 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 56 VQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 133
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 736215636 134 RNDDIADGNPKLTLGLIWTIILHFQI 159
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
159-274 |
4.07e-31 |
|
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: 119.94 E-value: 4.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 159 ISDIQVNGqsddMTAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSV 238
Cdd:cd21291 1 IADINEEG----LTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 736215636 239 AERDLGVTRLLDPEDV-DVLHPDEKSIITYVSSLYDA 274
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
171-269 |
4.18e-31 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 119.94 E-value: 4.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 171 MTAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLD 250
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 736215636 251 PEDVDVLHPDEKSIITYVS 269
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
52-161 |
1.47e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 118.45 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 52 ERDRVQKKTFTKWVNKHLMKSQR--HITDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQ 127
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 736215636 128 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 161
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
175-277 |
2.88e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 117.34 E-value: 2.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 175 EKLLL-WSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQ-ENLEQAFSVAERDLGVTRLLDPE 252
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 736215636 253 DVDVLHPDEKSIITYVSSLYDAMPR 277
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
55-157 |
4.47e-30 |
|
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: 116.81 E-value: 4.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 55 RVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 131
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 736215636 132 NIRNDDIADGNPKLTLGLIWTIILHF 157
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1588-2250 |
5.43e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 131.60 E-value: 5.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1588 KFKMQAEEAERRMKQAEE----------EKLRQIKVVEEvaQKSAAtqlqshsmsfnVKASKLEESLKKEQGTVL----- 1652
Cdd:COG1196 169 KYKERKEEAERKLEATEEnlerledilgELERQLEPLER--QAEKA-----------ERYRELKEELKELEAELLllklr 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1653 QLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAAL 1732
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1733 KQKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEM 1812
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1813 DSLLKMKTEAEKKtmsnTEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINE 1892
Cdd:COG1196 396 AELAAQLEELEEA----EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1893 ATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSssdseMVRQKTIVEETLRQKKIVE 1972
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA-----VLIGVEAAYEAALEAALAA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1973 EEIHIIRINFEKASKGKSDLENELKKLKVIAEETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAArqc 2052
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL--- 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2053 kAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQaa 2132
Cdd:COG1196 624 -GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL-- 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2133 ekakekaekeaaLLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKE 2212
Cdd:COG1196 701 ------------AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 736215636 2213 ADqalKLKSQVEK----------ELTMVKLRLDETDKQKALLDEELQR 2250
Cdd:COG1196 769 LE---RLEREIEAlgpvnllaieEYEELEERYDFLSEQREDLEEARET 813
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1385-2215 |
9.08e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 131.80 E-value: 9.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1385 ITETQRRLEDDEKASEKLKEEERKKMAEIQaELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQ 1464
Cdd:PTZ00121 1111 AEEARKAEEAKKKAEDARKAEEARKAEDAR-KAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRK 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1465 NIQ----------------HELHHLKSLSEQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRD 1528
Cdd:PTZ00121 1190 AEElrkaedarkaeaarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ 1269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1529 KAAEAEKLRKAAQ-EDAERLRKqvAEETQK--KKNAEDELKRKSEAEKEAAKQKQKAlddlQKFKMQAEEAErrmKQAEE 1605
Cdd:PTZ00121 1270 AAIKAEEARKADElKKAEEKKK--ADEAKKaeEKKKADEAKKKAEEAKKADEAKKKA----EEAKKKADAAK---KKAEE 1340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1606 EKLRqikvvEEVAQKSAATqlqshsmsfnvKASKLEESLKKEQGTVLQLQEE---AEQLRKQQEEANKArEQAEKELETW 1682
Cdd:PTZ00121 1341 AKKA-----AEAAKAEAEA-----------AADEAEAAEEKAEAAEKKKEEAkkkADAAKKKAEEKKKA-DEAKKKAEED 1403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1683 RQKANEalrlrLQAEEEAQKKS---KTQEEAERQKVEAERDAKKRAKAEDAALK--QKDNAEkELEKQRTFAEQVAQQKL 1757
Cdd:PTZ00121 1404 KKKADE-----LKKAAAAKKKAdeaKKKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKAE-EAKKKAEEAKKADEAKK 1477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1758 SAEQecirlKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLL 1837
Cdd:PTZ00121 1478 KAEE-----AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1838 ESEALKMkqladeatrlrsvAEEAKKQRQTAEEEAARQRA--EAEKILKEKLAAINEATRLRTEAEI--ALKAKEAENER 1913
Cdd:PTZ00121 1553 KAEELKK-------------AEEKKKAEEAKKAEEDKNMAlrKAEEAKKAEEARIEEVMKLYEEEKKmkAEEAKKAEEAK 1619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1914 LK----RKAEDEAYQRKLLEDQAAQHKHDIQEkiihLKSSSDSEMVRQKTIVEETLRQKKIVEEeihiirinfekASKGK 1989
Cdd:PTZ00121 1620 IKaeelKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKKAEE-----------AKKAE 1684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1990 SDLENELKKLKVIAEETQKSKLKAEAEAEKLKKlaaeeekkrkeseekVKRITAAEEEAARQCKAAQEEVARLEKKADEA 2069
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK---------------AEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2070 NKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSK--NKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLR 2147
Cdd:PTZ00121 1750 KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEedEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMED 1829
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2148 QKAAEAEKQKKSAEEEAakqakaqKDAEKLKKAAEEEASKRAAAEAEALKQK--KQADAEMAKHKKEADQ 2215
Cdd:PTZ00121 1830 SAIKEVADSKNMQLEEA-------DAFEKHKFNKNNENGEDGNKEADFNKEKdlKEDDEEEIEEADEIEK 1892
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1413-2017 |
1.95e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 129.67 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1413 IQAELDKQKQIAEAQAKsviKAEQeAQELKlkmkEEASKRQdvavdaeqqkqnIQHELHHLKSLSEQEiksksqqlehal 1492
Cdd:COG1196 194 ILGELERQLEPLERQAE---KAER-YRELK----EELKELE------------AELLLLKLRELEAEL------------ 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1493 vshTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQED-------AERLRKQVAEETQKKKNAEDEL 1565
Cdd:COG1196 242 ---EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyellaeLARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1566 KRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQ-----LQSHSMSFNVKASKL 1640
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEeeleeLAEELLEALRAAAEL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1641 EESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERD 1720
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1721 AKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKAD---FDHAEQQRGLLDNELQRLKKEVSATEKQ 1797
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAvliGVEAAYEAALEAALAAALQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1798 RKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRA 1877
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1878 EAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSSDSEMVRQ 1957
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1958 KTIVEETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKVIAEETQKSKLKAEAEA 2017
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
177-272 |
5.43e-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: 113.60 E-value: 5.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 177 LLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDPED-VD 255
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 736215636 256 VLHPDEKSIITYVSSLY 272
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1514-2401 |
1.05e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 127.87 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1514 KQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQV--AEETQKKKNAEDELKRK-SEAEKEAAKQKQKALDDLQKFK 1590
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAekAERYKELKAELRELELAlLVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1591 MQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAAtQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANK 1670
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIE-ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1671 AREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAE 1750
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1751 QVA--QQKLSAEQECIRLK---ADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKK 1825
Cdd:TIGR02168 411 RLEdrRERLQQEIEELLKKleeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1826 TMSnTEKSKQLLESEALKMKQLADEATRLR----SVAE--EAKKQRQTAEEEAARQRAEAekILKEKLAAINEATRLRTE 1899
Cdd:TIGR02168 491 LDS-LERLQENLEGFSEGVKALLKNQSGLSgilgVLSEliSVDEGYEAAIEAALGGRLQA--VVVENLNAAKKAIAFLKQ 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1900 AEI---------ALKAKEAENERLKRKAEDEAYQR--KLLEDQAAQHKHDIQEKIIHLK--SSSDSEMVRQKtiveETLR 1966
Cdd:TIGR02168 568 NELgrvtflpldSIKGTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRKALSYLLGGVLvvDDLDNALELAK----KLRP 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1967 QKKIVEEEIHIIR----INFEKASKGKSDLENELKklkvIAEETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKVKrIT 2042
Cdd:TIGR02168 644 GYRIVTLDGDLVRpggvITGGSAKTNSSILERRRE----IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ-LR 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2043 AAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSKnkedslaQQKMKEEF 2122
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQI 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2123 ENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEalkqkkqA 2202
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE-------L 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2203 DAEMAKHKKEADQALKLKSQVEKELTMVKLRLDEtdkqkalLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDellKL 2282
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEE-------LSEELRELESKRSELRRELEELREKLAQLELRLE---GL 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2283 KLKIEEQNRSLMKKdkdktQKVLAEEAGKMKSLAE---EAARLSVEAEETARQRqIAESNLAeqralaekmlkekmqAIQ 2359
Cdd:TIGR02168 935 EVRIDNLQERLSEE-----YSLTLEEAEALENKIEddeEEARRRLKRLENKIKE-LGPVNLA---------------AIE 993
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 736215636 2360 EATKLKAEAQELQKQKDQAqEKAKKLLEdkqQIQQRLDKETE 2401
Cdd:TIGR02168 994 EYEELKERYDFLTAQKEDL-TEAKETLE---EAIEEIDREAR 1031
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
175-276 |
1.06e-28 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 112.74 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 175 EKLLL-WSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDPED 253
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 736215636 254 VDVLHPDEKSIITYVSSLYDAMP 276
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1475-2403 |
7.86e-28 |
|
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: 124.70 E-value: 7.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1475 SLSEQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEE 1554
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1555 TQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQSHsmsfN 1634
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES----E 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1635 VKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQK 1714
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1715 VEAERDAKKRAKAEDAALKQKDNAEKELEKQRtfaeqvaqqklsAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSAT 1794
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEDLLKEEKKEELEIL------------EEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1795 EKQRKLLEEELAKVRSEmdsllKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAar 1874
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQ-----LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY-- 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1875 qraeaekilkekLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSSDSEM 1954
Cdd:pfam02463 542 ------------KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1955 VRQKTIVEETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKviAEETQKSKLKAEAEAEKLKKLAAEEEKKRKES 2034
Cdd:pfam02463 610 KATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLE--EGLAEKSEVKASLSELTKELLEIQELQEKAES 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2035 EEKVKRITAAEEEAARQCKAAQEEVARLEKKADEANkqkekaekeaekqvIVAKEAAQKCSSAEQKAQEVLSKNKEDSLA 2114
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL--------------ADRVQEAQDKINEELKLLKQKIDEEEEEEE 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2115 QQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAE 2194
Cdd:pfam02463 754 KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEE 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2195 ALKQKkqadAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKgevndavkqKAQVEDELAKVRI 2274
Cdd:pfam02463 834 ELEEL----ALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDE---------LESKEEKEKEEKK 900
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2275 QMDELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQiaeSNLAEQRALAEKMLKEK 2354
Cdd:pfam02463 901 ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEE---RNKRLLLAKEELGKVNL 977
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 736215636 2355 MQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGF 2403
Cdd:pfam02463 978 MAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELF 1026
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
51-159 |
4.00e-27 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 109.08 E-value: 4.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 51 DERDRVQKKTFTKWVNKHLMKSQR--HITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHR- 126
Cdd:cd21247 15 EQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLKTKv 94
|
90 100 110
....*....|....*....|....*....|...
gi 736215636 127 QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 159
Cdd:cd21247 95 PVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
55-160 |
4.69e-27 |
|
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: 108.96 E-value: 4.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 55 RVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLKHRQVKLV 131
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 736215636 132 NIRNDDIADGNPKLTLGLIWTIILHFQIS 160
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
55-157 |
5.07e-27 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 107.96 E-value: 5.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 55 RVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 131
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 736215636 132 NIRNDDIADGNPKLTLGLIWTIILHF 157
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1588-2451 |
6.98e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 121.70 E-value: 6.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1588 KFKMQAEEAERRMKQAEEEKLRQIKVVEEvaqksaatqlqshsmsfnvkaskLEESLKKeqgtvLQLQ-EEAEQLRKQQE 1666
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNE-----------------------LERQLKS-----LERQaEKAERYKELKA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1667 EANKAR--------EQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNA 1738
Cdd:TIGR02168 221 ELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1739 EKELEKQRtfaeqvaQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKM 1818
Cdd:TIGR02168 301 EQQKQILR-------ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1819 KTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRT 1898
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1899 EAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEkiihlksssdsemvrqktiveetlrqkkiveeeihiI 1978
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER------------------------------------L 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1979 RINFEKASKGKSDLENELKKLKVIAeETQKSKLKAEAEAEKLKKLAAEEEKKRkeseekvkrITAAEEEAARQCKAAQEE 2058
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSGLSGIL-GVLSELISVDEGYEAAIEAALGGRLQA---------VVVENLNAAKKAIAFLKQ 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2059 VARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEK 2138
Cdd:TIGR02168 568 NELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRI 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2139 AEKEAALL--------------------RQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQ 2198
Cdd:TIGR02168 648 VTLDGDLVrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2199 KKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDE 2278
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE 807
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2279 lLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAI 2358
Cdd:TIGR02168 808 -LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2359 QEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKsLEAERKRQLE-----VSAEAETLRLKVKELSD 2433
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQErlseeYSLTLEEAEALENKIED 965
|
890
....*....|....*...
gi 736215636 2434 AQSKAENEAKKFKKQADE 2451
Cdd:TIGR02168 966 DEEEARRRLKRLENKIKE 983
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1143-2012 |
2.06e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 120.63 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1143 IRNTKEAEAALKTYESRLLDVNKVPENEKEVEEQRSQLKSMRAEvEADQVIFDRLQDELRRASTIN--DKMTRIHSERDA 1220
Cdd:PTZ00121 1130 AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE-DAKKAEAARKAEEVRKAEELRkaEDARKAEAARKA 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1221 EMEhyrqlvssllERWQVVFAQMDMRQREldllgrhmnsynvsyewLIHWLGEARKRQEKIQAvpiggSKALREQLAEEK 1300
Cdd:PTZ00121 1209 EEE----------RKAEEARKAEDAKKAE-----------------AVKKAEEAKKDAEEAKK-----AEEERNNEEIRK 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1301 KLLEEIEKNKDKIDSCQKNAKAYIDSVKdyelqiltyKALQDPMASPLKKPKMDCASDNIIQEYVTLRtRYSELMTLTSQ 1380
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELK---------KAEEKKKADEAKKAEEKKKADEAKKKAEEAK-KADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1381 YIKFITETQRRLEDDEKASEKLKEEERKKmaeiQAELDKQKQIAEAQAKSVIKAEQEAQELKlKMKEEASKRQDVAVDAE 1460
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAA----ADEAEAAEEKAEAAEKKKEEAKKKADAAK-KKAEEKKKADEAKKKAE 1401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1461 QQKQNIQhelhHLKSLSE-----QEIKSKSQQLEHALVSHTKIEEEIHTirIQLEMTIKQKKTAEsELQQLRDKAAEAEK 1535
Cdd:PTZ00121 1402 EDKKKAD----ELKKAAAakkkaDEAKKKAEEKKKADEAKKKAEEAKKA--DEAKKKAEEAKKAE-EAKKKAEEAKKADE 1474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1536 LRKAAQE--DAERLRKQvAEETQKKKnaeDELKRKSEAEKEA-----AKQKQKAlDDLQKF--KMQAEE---AERRMKQA 1603
Cdd:PTZ00121 1475 AKKKAEEakKADEAKKK-AEEAKKKA---DEAKKAAEAKKKAdeakkAEEAKKA-DEAKKAeeAKKADEakkAEEKKKAD 1549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1604 EEEKLRQIKVVEEVAQKSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEE-----AEQLRKQQEEANKArEQAEKE 1678
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEekkmkAEEAKKAEEAKIKA-EELKKA 1628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1679 LETwRQKANEalrLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKrakaEDAALKQKDNAEKELEKQRTFAEQVAQQKLS 1758
Cdd:PTZ00121 1629 EEE-KKKVEQ---LKKKEAEEKKKAEELKKAEEENKIKAAEEAKK----AEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1759 AEQecirlkadfdhAEQQRGLLDNELQRlKKEVSATEKQRKLLEEELAKVRSEMdsllKMKTEAEKKTMSNTEKSKQLLE 1838
Cdd:PTZ00121 1701 AKK-----------AEELKKKEAEEKKK-AEELKKAEEENKIKAEEAKKEAEED----KKKAEEAKKDEEEKKKIAHLKK 1764
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1839 SEALKMKQLADEATRLrsVAEEAKKQRQTAEEEAARQraeaEKILKEKLAAINEATRLRTeaEIALKAKEAENERLKRKA 1918
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKK----IKDIFDNFANIIEGGKEGN--LVINDSKEMEDSAIKEVA 1836
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1919 EDEAYQRkllEDQAAQHKHDIQEKIIHLKSS-SDSEMVRQKTI-------VEETLRQKKIVEEEIHIIRINFEKASKGKS 1990
Cdd:PTZ00121 1837 DSKNMQL---EEADAFEKHKFNKNNENGEDGnKEADFNKEKDLkeddeeeIEEADEIEKIDKDDIEREIPNNNMAGKNND 1913
|
890 900
....*....|....*....|..
gi 736215636 1991 DLENELKKLKVIAEETQKSKLK 2012
Cdd:PTZ00121 1914 IIDDKLDKDEYIKRDAEETREE 1935
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
175-274 |
2.83e-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: 105.83 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 175 EKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDPEDV 254
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEM 82
|
90 100
....*....|....*....|.
gi 736215636 255 DVLH-PDEKSIITYVSSLYDA 274
Cdd:cd22198 83 ASLAvPDKLSMVSYLSQFYEA 103
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
157-274 |
3.21e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 106.32 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 157 FQISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAF 236
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 736215636 237 SVAERDLGVTRLLDPED-VDVLHPDEKSIITYVSSLYDA 274
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
159-274 |
6.50e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 105.55 E-value: 6.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 159 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSV 238
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 736215636 239 AERDLGVTRLLDPED-VDVLHPDEKSIITYVSSLYDA 274
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1648-2586 |
1.49e-24 |
|
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: 113.91 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1648 QGTVLQLQEEAEQLRKQQEEA------NKAREQAEKELEtwRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERdA 1721
Cdd:pfam02463 141 GGKIEIIAMMKPERRLEIEEEaagsrlKRKKKEALKKLI--EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLK-E 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1722 KKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAEQEciRLKADFDHAEQQRGLLDNElqrlKKEVSATEKQRKLL 1801
Cdd:pfam02463 218 KLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ--EIEKEEEKLAQVLKENKEE----EKEKKLQEEELKLL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1802 EEELAKVRSEMDSLLKMKTEAEKKTmSNTEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEK 1881
Cdd:pfam02463 292 AKEEEELKSELLKLERRKVDDEEKL-KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1882 ILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAaqhkhdiqekiihlksssDSEMVRQKTIV 1961
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLL------------------KEEKKEELEIL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1962 EETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKVIAEETQKSKLK-AEAEAEKLKKLAAEEEKKRKESEEKVKR 2040
Cdd:pfam02463 433 EEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQeQLELLLSRQKLEERSQKESKARSGLKVL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2041 ITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKE 2120
Cdd:pfam02463 513 LALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLK 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2121 EFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEeaakqakaQKDAEKLKKAAEEEASKRAAAEAEALKQKK 2200
Cdd:pfam02463 593 SIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTEL--------TKLKESAKAKESGLRKGVSLEEGLAEKSEV 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2201 QADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEvndAVKQKAQVEDELAKVRIQMDELL 2280
Cdd:pfam02463 665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE---AEELLADRVQEAQDKINEELKLL 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2281 KLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAarlsVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQE 2360
Cdd:pfam02463 742 KQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER----EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2361 ATKLKAEAQELQKQKDQAQEKAKKLLEDKQQiqqrldketegfQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAEN 2440
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKL------------EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2441 EAKKFKKQADEAKARLKDTEKQSTETVVQKLETQRLQSTREADglkeaiadlekereklkkeaeelqnkSNKMANTQKEE 2520
Cdd:pfam02463 886 DELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE--------------------------ILLKYEEEPEE 939
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736215636 2521 IEQQKAIIQKSFISERELLLKRQKAVEDEKKKLQKQ-----FEDEVKKAEALKDEQERQRklMEEEKKKLQ 2586
Cdd:pfam02463 940 LLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVnlmaiEEFEEKEERYNKDELEKER--LEEEKKKLI 1008
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
59-156 |
1.94e-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: 100.47 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 59 KTFTKWVNKHLMKS-QRHITDLYEDLRDGHNLISLLEVLSGETLPREK---GRMRFHKLQNVQIALDFLKHRQVKLVNIR 134
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 736215636 135 NDDIADGnPKLTLGLIWTIILH 156
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1382-1941 |
2.46e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.11 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1382 IKFITETQRRLEDDEKASEKLKEEERKKMAEIQAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQ 1461
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1462 QkqniqhelhhlkslsEQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQ 1541
Cdd:COG1196 328 L---------------EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1542 EDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKS 1621
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1622 AATQLQSHSMSFNVKASKLEESLKKEQgtVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQ 1701
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEA--EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1702 KKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLD 1781
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1782 NELQRLkkevsateKQRKLLEEELAKVRSEMDSLLkmktEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAEEA 1861
Cdd:COG1196 631 RLEAAL--------RRAVTLAGRLREVTLEGEGGS----AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1862 KKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQE 1941
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1859-2628 |
2.74e-24 |
|
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: 113.14 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1859 EEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHD 1938
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1939 IQEKIIHLKSSSDSEMVRQKTIVEETlRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKVIAEETQKSKLKAEAEAE 2018
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEE-KEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2019 KLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAE 2098
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2099 QKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEA--AKQAKAQKDAEK 2176
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETqlVKLQEQLELLLS 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2177 LKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVN 2256
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2257 DAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIA 2336
Cdd:pfam02463 572 ELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKG 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2337 ESNlaeqrALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAER----K 2412
Cdd:pfam02463 652 VSL-----EEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEElladR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2413 RQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTETVVQKLETQRLQSTREADGLKEAIADL 2492
Cdd:pfam02463 727 VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRAL 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2493 EKEREKLKKEAEELQNKSNKMANTQKEEIEQQKAIIQKSFISERELLLKRQKAVEDEKKKLQKQFEDEVKKAEALKDEQE 2572
Cdd:pfam02463 807 EEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKD 886
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 2573 RQRKLMEEEKKKLQAIMDAAVKKQKEAEADMKNK---QTEMEVLEKKRLDQEKQLGAEN 2628
Cdd:pfam02463 887 ELESKEEKEKEEKKELEEESQKLNLLEEKENEIEeriKEEAEILLKYEEEPEELLLEEA 945
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
172-272 |
3.79e-24 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 99.81 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERdLGVTRLLDP 251
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 736215636 252 EDVDVLH-PDEKSIITYVSSLY 272
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
177-272 |
4.43e-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: 99.53 E-value: 4.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 177 LLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDPEDVDV 256
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDMVT 84
|
90
....*....|....*..
gi 736215636 257 LH-PDEKSIITYVSSLY 272
Cdd:cd21197 85 MHvPDRLSIITYVSQYY 101
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
172-276 |
6.46e-24 |
|
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: 99.09 E-value: 6.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGYqGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDP 251
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 736215636 252 EDVDVLHPDEKSIITYVSSLYDAMP 276
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
171-277 |
7.08e-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: 7.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 171 MTAKEKLLLWSQRMVEGY-QGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQ--ENLEQAFSVAERDLGVTR 247
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDklENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 736215636 248 -LLDPEDVDvlHPDEKSIITYVSSLYDAMPR 277
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
56-159 |
4.44e-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: 4.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 56 VQKKTFTKWVNKHLMKSQRH--ITDLYEDLRDGHNLISLLEVLSGETLP-REKGRMRFHKLQNVQIALDFLKHRQ-VKLV 131
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 736215636 132 NIRNDDIADGNPKLTLGLIWTIILHFQI 159
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
159-274 |
5.53e-23 |
|
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: 97.10 E-value: 5.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 159 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSV 238
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 736215636 239 AERDLGVTRLLDPED-VDVLHPDEKSIITYVSSLYDA 274
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1147-1946 |
6.63e-23 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 109.08 E-value: 6.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1147 KEAEAALKTYESRLLDVNKVPENEKEVEEQRSQLKSMRAEvEADQVIFDRLQDELRRASTIN--------DKMTRIHSER 1218
Cdd:PTZ00121 1140 RKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAE-AARKAEEVRKAEELRKAEDARkaeaarkaEEERKAEEAR 1218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1219 DAEMEHYRQLVSSLLE---------RWQVVFAQMDMRQRELDLLGRHMNSYNVSYEWLIHWLGEARKRQEKIQAVPIGGS 1289
Cdd:PTZ00121 1219 KAEDAKKAEAVKKAEEakkdaeeakKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKA 1298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1290 KALR--EQLAEEKKLLEEIEKNKDKIDSCQKNAKAYIDSVKDYELQILTYKALQDPMASPLKKPKMDCASDNIIQEYvtl 1367
Cdd:PTZ00121 1299 EEKKkaDEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE--- 1375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1368 RTRYSELMTLTSQYIKFITETQRRLEDDEKASE--KLKEEERKKMAEIQAELDKQKQIAEAQAKSviKAEQEAQELKlKM 1445
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADelKKAAAAKKKADEAKKKAEEKKKADEAKKKA--EEAKKADEAK-KK 1452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1446 KEEASKRQDVAVDAEQQKQNIQHELHHLKSLSEQEIKSKSQQLEHALVSHTKIEEEIHTIRiQLEMTIKQKKTAESELQQ 1525
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAEEAKKADEAKKAE 1531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1526 LRDKAAE---AEKLRKAAQ-EDAERLRK----QVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDL--QKFKMQAEE 1595
Cdd:PTZ00121 1532 EAKKADEakkAEEKKKADElKKAEELKKaeekKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeEEKKMKAEE 1611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1596 AerrmKQAEEEKLRQIKVVEEVAQKSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQA 1675
Cdd:PTZ00121 1612 A----KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1676 EKELETWRQKANEALR---LRLQAEEEAQKKSKTQEEAERQKVEAErDAKKRAKAEdaalkqKDNAEkELEKQRTFAEQV 1752
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKaeeLKKKEAEEKKKAEELKKAEEENKIKAE-EAKKEAEED------KKKAE-EAKKDEEEKKKI 1759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1753 AQQKLSAEQECIRLKADFDHAEQqrglldnelQRLKKEvsaTEKQRKLLEEELAKVRSEMDSLLkmktEAEKKTMSNTEK 1832
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIE---------EELDEE---DEKRRMEVDKKIKDIFDNFANII----EGGKEGNLVIND 1823
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1833 SKQLLESEalkMKQLADEATRLRSVAEEAKKQRQTAEEEAARQ-----RAEAEKILKEKLAAINEATRLRTEAEIALKAK 1907
Cdd:PTZ00121 1824 SKEMEDSA---IKEVADSKNMQLEEADAFEKHKFNKNNENGEDgnkeaDFNKEKDLKEDDEEEIEEADEIEKIDKDDIER 1900
|
810 820 830
....*....|....*....|....*....|....*....
gi 736215636 1908 EAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHL 1946
Cdd:PTZ00121 1901 EIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIKI 1939
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
173-272 |
7.30e-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: 96.09 E-value: 7.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 173 AKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDPE 252
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 736215636 253 D-VDVLHPDEKSIITYVSSLY 272
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
175-275 |
7.92e-23 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 96.00 E-value: 7.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 175 EKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDPEDV 254
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 736215636 255 DVLHPDEKSIITYVSSLYDAM 275
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1647-2590 |
2.43e-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: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1647 EQGTVLQLQE-EAEQLRKQQEEA------NKAREQAEKELEtwrqKANEALrLRLQ---AEEEAQKKSktqeeAERQKVE 1716
Cdd:TIGR02168 142 EQGKISEIIEaKPEERRAIFEEAagiskyKERRKETERKLE----RTRENL-DRLEdilNELERQLKS-----LERQAEK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1717 AERdakkrakaedaaLKQKDNAEKELEKQRTfaeqvAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEK 1796
Cdd:TIGR02168 212 AER------------YKELKAELRELELALL-----VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1797 QRKLLEEELAKVRSEMDSLlkmkteaeKKTMSNTEKSKQLLESealKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQR 1876
Cdd:TIGR02168 275 EVSELEEEIEELQKELYAL--------ANEISRLEQQKQILRE---RLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1877 A---EAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKaedeayqRKLLEDQAAQHKHDIQEKIIHLKSSSDSe 1953
Cdd:TIGR02168 344 EkleELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK-------VAQLELQIASLNNEIERLEARLERLEDR- 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1954 mvRQKTIVEETLRQKKIVEEEIHiirinfekaskgksDLENELKKLKVIAEETQKSKLKAEAEAEKLKKLAAEEEKKRKE 2033
Cdd:TIGR02168 416 --RERLQQEIEELLKKLEEAELK--------------ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2034 SEEKvkritaaEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAK--EAAQKCSSAEQKA-----QEVLS 2106
Cdd:TIGR02168 480 AERE-------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEliSVDEGYEAAIEAAlggrlQAVVV 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2107 KNKEDSlaqqkmKEEFENakrLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEAS 2186
Cdd:TIGR02168 553 ENLNAA------KKAIAF---LKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLG 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2187 KRAAAE--AEALKQKKQADAEMAKHKKEADQALK----LKSQVEKELTMVKLR--LDETDKQKALLDEELQRVKGEVNDA 2258
Cdd:TIGR02168 624 GVLVVDdlDNALELAKKLRPGYRIVTLDGDLVRPggviTGGSAKTNSSILERRreIEELEEKIEELEEKIAELEKALAEL 703
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2259 VKQKAQVEDELAKVRIQMDELlklklkieEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAES 2338
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEEL--------SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2339 NLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLD---KETEGFQKSLEAERKRQL 2415
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAateRRLEDLEEQIEELSEDIE 855
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2416 EVSAEAETLRLKVKELSDAQSKAENEakkfKKQADEAKARLKDtEKQSTETVVQKLETQRLQSTREADGLKEAIADleke 2495
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLNE----RASLEEALALLRS-ELEELSEELRELESKRSELRRELEELREKLAQ---- 926
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2496 reklkkeaeelqnksnkmANTQKEEIEQQKAIIQKSFISERELLLKRQKAVEDEKKKLQKQFEDEVKKA----------- 2564
Cdd:TIGR02168 927 ------------------LELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLenkikelgpvn 988
|
970 980 990
....*....|....*....|....*....|....*.
gi 736215636 2565 ----EALKDEQER------QRKLMEEEKKKLQAIMD 2590
Cdd:TIGR02168 989 laaiEEYEELKERydfltaQKEDLTEAKETLEEAIE 1024
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
55-160 |
3.44e-22 |
|
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: 95.15 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 55 RVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 131
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 736215636 132 NIRNDDIADGNPKLTLGLIWTIILHFQIS 160
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1412-2062 |
3.74e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 106.29 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1412 EIQAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVavdaEQQKQNIQHELHHLKslseQEIKSKSQQLEHa 1491
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL----EEEIEELQKELYALA----NEISRLEQQKQI- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1492 lvshtkIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAE---DELKRK 1568
Cdd:TIGR02168 307 ------LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELEsrlEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1569 SEAEKEAAKQKQKALDDLQKfkmQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQSHSMSFnvkaSKLEESLKKEQ 1648
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNN---EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL----EELEEELEELQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1649 GTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKAnEALRLRLQAEEEAQKKSKTQEEAERQ------------KVE 1716
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARL-DSLERLQENLEGFSEGVKALLKNQSGlsgilgvlseliSVD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1717 AERDA-----------------KKRAKAEDAALKQKD-------------------NAEKELEKQRTF------------ 1748
Cdd:TIGR02168 533 EGYEAaieaalggrlqavvvenLNAAKKAIAFLKQNElgrvtflpldsikgteiqgNDREILKNIEGFlgvakdlvkfdp 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1749 ----------------------------------------------------AEQVAQQKLSAEQECIRLKADFDHAEQQ 1776
Cdd:TIGR02168 613 klrkalsyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1777 RGLLDNELQRLKKEVSATEKQ----RKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEAlKMKQLADEAT 1852
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEEleqlRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA-EIEELEERLE 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1853 RLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAeialKAKEAENERLKRKAEDEAYQRKLLEDQA 1932
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQI 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1933 AQHKHDIqEKIIHLKSSSDSEMVRQKTIVEETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKVIAEETQKSKLK 2012
Cdd:TIGR02168 848 EELSEDI-ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 2013 AEAEAEKLK--------KLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARL 2062
Cdd:TIGR02168 927 LELRLEGLEvridnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
55-160 |
5.40e-22 |
|
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: 94.38 E-value: 5.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 55 RVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 131
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 736215636 132 NIRNDDIADGNPKLTLGLIWTIILHFQIS 160
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1962-2628 |
1.95e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.48 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1962 EETLRQKKIVEEeiHIIRINfekaskgksDLENELKKlkviaeetQKSKLKAEAE-AEKLKKLAAEEEKKRKeseekvkr 2040
Cdd:COG1196 175 EEAERKLEATEE--NLERLE---------DILGELER--------QLEPLERQAEkAERYRELKEELKELEA-------- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2041 itaaeEEAARQCKAAQEEVARLEKKADEANKQKEKAekeaekqvivAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKE 2120
Cdd:COG1196 228 -----ELLLLKLRELEAELEELEAELEELEAELEEL----------EAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2121 EFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKK 2200
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2201 QADAEMAKHKKEADQALKLKSQVEKELTmVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELL 2280
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAA-QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2281 KLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQE 2360
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2361 ATKLKAEAQELQKQkDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAEN 2440
Cdd:COG1196 532 VEAAYEAALEAALA-AALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLRE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2441 EAKKFKKQADEAKARLKDTEKQSTETVVQK-LETQRLQSTREADGLKEAIADLEKEREKLKKEAEELQNKSNKMANTQKE 2519
Cdd:COG1196 611 ADARYYVLGDTLLGRTLVAARLEAALRRAVtLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2520 EIEQQKAIIQksfisERELLLKRQKAVEDEKKKLQKQFEDEVKKAEALKDEQERQRKLMEEEkkklqaiMDAAVKKQKEA 2599
Cdd:COG1196 691 EELELEEALL-----AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL-------LEEEALEELPE 758
|
650 660
....*....|....*....|....*....
gi 736215636 2600 EADMKNKQTEMEVLEKKRldqeKQLGAEN 2628
Cdd:COG1196 759 PPDLEELERELERLEREI----EALGPVN 783
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
159-274 |
2.07e-21 |
|
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: 92.83 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 159 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSV 238
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 736215636 239 AERDLGVTRLLDPED-VDVLHPDEKSIITYVSSLYDA 274
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1854-2636 |
3.65e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 102.83 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1854 LRSVAEEA------KKQRQTAEEEAARQRAEAEK---ILKEKLAAINeatRLRTEAEIALKAKEAENER---------LK 1915
Cdd:TIGR02168 157 RRAIFEEAagiskyKERRKETERKLERTRENLDRledILNELERQLK---SLERQAEKAERYKELKAELrelelallvLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1916 RKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSSdsemvrqktiVEETLRQKKIVEEEIHIIRINFEKASKGKSDLENE 1995
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEK----------LEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1996 LKKLKVIAEETQKSKLKAEAEAEKLKklaaeeekkrkeseekvkritaaeeeaaRQCKAAQEEVARLEKKADEANKQKEK 2075
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELE----------------------------SKLDELAEELAELEEKLEELKEELES 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2076 AEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEK 2155
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2156 QKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLK----SQVEKELTMVK 2231
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfSEGVKALLKNQ 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2232 LRLD----------ETDKQ-----KALLDEELQRVKGEVNDAVKQ--KAQVEDELAKV------RIQMDELLKLKLKIEE 2288
Cdd:TIGR02168 516 SGLSgilgvlseliSVDEGyeaaiEAALGGRLQAVVVENLNAAKKaiAFLKQNELGRVtflpldSIKGTEIQGNDREILK 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2289 QNRSLMK------KDKDKTQKVLA------------EEAGKMKSLAEEAARLSVEAEETARQRQIaesnLAEQRALAEKM 2350
Cdd:TIGR02168 596 NIEGFLGvakdlvKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGV----ITGGSAKTNSS 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2351 LKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKE 2430
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2431 LSDAQSKAENEAKKFKKQADEAKARLKDTEKQST--ETVVQKLETQRLQSTREADGLKEAIADlekereklkkEAEELQN 2508
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEelEAQIEQLKEELKALREALDELRAELTL----------LNEEAAN 821
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2509 KSNKMANTQKEEIEQQKAI--IQKSFISERELLLKRQKAVEDEKKKLQKqFEDEVKKAEALKDEQERQRKLMEEEKKKLQ 2586
Cdd:TIGR02168 822 LRERLESLERRIAATERRLedLEEQIEELSEDIESLAAEIEELEELIEE-LESELEALLNERASLEEALALLRSELEELS 900
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 736215636 2587 AIMDAAVKKQKEAEADMKNKQTEMEVLEkKRLDQEKQLGAENQ-KLREKLQ 2636
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLE-LRLEGLEVRIDNLQeRLSEEYS 950
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1780-2413 |
4.54e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.32 E-value: 4.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1780 LDNELQRLKKEVSATEKQRKLleeelakvrsemdsllkmKTEAEKKtmsntEKSKQLLESEALKMKQLADEATRLRSVAE 1859
Cdd:COG1196 198 LERQLEPLERQAEKAERYREL------------------KEELKEL-----EAELLLLKLRELEAELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1860 EAKKQRQTAEEEAARQRAEAEkiLKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDI 1939
Cdd:COG1196 255 LEELEAELAELEAELEELRLE--LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1940 QEKiihlksssDSEMVRQKTIVEETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKVIAEETQKSKLKAEAEAEK 2019
Cdd:COG1196 333 EEL--------EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2020 LKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQ 2099
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2100 KAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQkksAEEEAAKQAKAQKDAEKLKK 2179
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE---AALAAALQNIVVEDDEVAAA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2180 AAEEEASKRA--AAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRvkgevnd 2257
Cdd:COG1196 562 AIEYLKAAKAgrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA------- 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2258 AVKQKAQVEDELAKVRIQMDELLKLKLKIEEQNRSLmkkdkdKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAE 2337
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL------LAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 2338 SNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLE--DKQQIQQRLDKetegfqksLEAERKR 2413
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEppDLEELERELER--------LEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1413-2251 |
4.55e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 102.44 E-value: 4.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1413 IQAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQHELHHLKSLSEQEIKSKSQQLEHAL 1492
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1493 VSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRkqvaeetQKKKNAEDELKRKSEAE 1572
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE-------SKLDELAEELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1573 KEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEklrqikvVEEVAQKSAATQLQSHSMsfNVKASKLEESLKKEQGTVL 1652
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQ-------LETLRSKVAQLELQIASL--NNEIERLEARLERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1653 QLQEEAEQLRKQQEEANKAREQAEKELEtwrQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAAL 1732
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAELEEL---EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1733 kqkdnaEKELEKQRTFAEQVAQQKLSAEQ---------ECIRLKADFDHAeqqrglLDNELQ-RLKKEVSATEKQRKLLE 1802
Cdd:TIGR02168 495 ------ERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGYEAA------IEAALGgRLQAVVVENLNAAKKAI 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1803 EELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLR--------------SVAEEAKKQRQT- 1867
Cdd:TIGR02168 563 AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvdDLDNALELAKKLr 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1868 ---------------------AEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEayQRK 1926
Cdd:TIGR02168 643 pgyrivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL--RKE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1927 LLEDQAAQHKHDIQEKIIHLKSSSDSEMVRQKTI-VEETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKVIAEE 2005
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKeLTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2006 TQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVI 2085
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2086 VAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENA-KRLAQAAEKAKEKAEKEAALLRQKAAE----AEKQKKSA 2160
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELrEKLAQLELRLEGLEVRIDNLQERLSEEysltLEEAEALE 960
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2161 EEEAAKQAKAQKDAEKLKKAAEE--EASKRAAAEAEALKQKKQadaEMAKHKKEADQALK-LKSQVEKELTMVKLRLDET 2237
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKElgPVNLAAIEEYEELKERYD---FLTAQKEDLTEAKEtLEEAIEEIDREARERFKDT 1037
|
890
....*....|....
gi 736215636 2238 DKQkalLDEELQRV 2251
Cdd:TIGR02168 1038 FDQ---VNENFQRV 1048
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1854-2490 |
7.42e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.55 E-value: 7.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1854 LRSVAEEA------KKQRQTAEE--EAARQR-AEAEKILKEKLAAINeatRLRTEAEIALKAKEAENERLKRKAEDEAYQ 1924
Cdd:COG1196 157 RRAIIEEAagiskyKERKEEAERklEATEENlERLEDILGELERQLE---PLERQAEKAERYRELKEELKELEAELLLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1925 RKLLEDQAAQHKHDIQEKiihlksssdsEMVRQKTIVEETLRQKKIVEEEIHIIRINFEkaskgksdlenelkklkviAE 2004
Cdd:COG1196 234 LRELEAELEELEAELEEL----------EAELEELEAELAELEAELEELRLELEELELE-------------------LE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2005 ETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEAnkqkekaEKEAEKQV 2084
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA-------EEELEEAE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2085 IVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQ-QKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEE 2163
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELlEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2164 AAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKEltmVKLRLDETDKQKAL 2243
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE---ADYEGFLEGVKAAL 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2244 LDEELQRVKGEVNDAVKQKAQVEDELAK------VRIQMDELLKLKLKIEEQNRSL--------MKKDKDKTQKVLAEEA 2309
Cdd:COG1196 515 LLAGLRGLAGAVAVLIGVEAAYEAALEAalaaalQNIVVEDDEVAAAAIEYLKAAKagratflpLDKIRARAALAAALAR 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2310 GKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDK 2389
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2390 QQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTETVVQ 2469
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
650 660
....*....|....*....|...
gi 736215636 2470 KLET--QRLQSTREADGLKEAIA 2490
Cdd:COG1196 755 ELPEppDLEELERELERLEREIE 777
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
834-900 |
7.66e-20 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 86.16 E-value: 7.66e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 834 QLRPRNpaTAIKGKQPIQAVCDFKQMEITVHRGDECALLNNSQPYKWRVLNDKGNESSVPSICFLVP 900
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1369-2437 |
8.48e-20 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 98.32 E-value: 8.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1369 TRYSELMTLTSQYIKFITETQRRLEDDEKaseklkeeerkKMAEIQAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEE 1448
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELK-----------ELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1449 ASKRQDVAVDAE---QQKQNIQHELHHLKSLSEQEIKSKSQQLEhalvshtkiEEEIHTIRIQLE-MTIKQK-KTAESEL 1523
Cdd:pfam01576 70 KQELEEILHELEsrlEEEEERSQQLQNEKKKMQQHIQDLEEQLD---------EEEAARQKLQLEkVTTEAKiKKLEEDI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1524 QQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKN--------------AEDELKR--KSEAEKEAAKQKQKA-LDDL 1586
Cdd:pfam01576 141 LLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSlsklknkheamisdLEERLKKeeKGRQELEKAKRKLEGeSTDL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1587 Q----KFKMQAEEAERRMKQAEEE-KLRQIKVVEEVAQKSAAtqlqshsmsfnvkasklEESLKKEQGTVLQLQEEAEQL 1661
Cdd:pfam01576 221 QeqiaELQAQIAELRAQLAKKEEElQAALARLEEETAQKNNA-----------------LKKIRELEAQISELQEDLESE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1662 RKQQEEANKAREQAEKELETWRQKANEALrlrlqAEEEAQKKSKTQEEAERQKVE-AERDAKKRAKAEDAALKQKDNA-- 1738
Cdd:pfam01576 284 RAARNKAEKQRRDLGEELEALKTELEDTL-----DTTAAQQELRSKREQEVTELKkALEEETRSHEAQLQEMRQKHTQal 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1739 ---EKELEKQRTFAEQVAQQKLSAEQECIRLKADFD-------HAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKV 1808
Cdd:pfam01576 359 eelTEQLEQAKRNKANLEKAKQALESENAELQAELRtlqqakqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1809 RSEMDSLLKMKTEAEKKTMSNTeKSKQLLESEALKMKQLADEATRLRsvAEEAKKQRQTAEEEAArqraeaekiLKEKLA 1888
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLS-KDVSSLESQLQDTQELLQEETRQK--LNLSTRLRQLEDERNS---------LQEQLE 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1889 AINEATRlrtEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSSDSemvrqktiVEETLRQK 1968
Cdd:pfam01576 507 EEEEAKR---NVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA--------YDKLEKTK 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1969 KIVEEEIHIIRINFEKASKGKSDLENELKKL-KVIAEETQKSKLKAEaEAEKLKKLAAEEEKKRKESEEKVKRITAAEEE 2047
Cdd:pfam01576 576 NRLQQELDDLLVDLDHQRQLVSNLEKKQKKFdQMLAEEKAISARYAE-ERDRAEAEAREKETRALSLARALEEALEAKEE 654
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2048 AARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFEnaKR 2127
Cdd:pfam01576 655 LERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFE--RD 732
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2128 LAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKkAAEEEASKraaAEAEALKQKKQADAEMA 2207
Cdd:pfam01576 733 LQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELE-AQIDAANK---GREEAVKQLKKLQAQMK 808
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2208 KHKKEADQAL---------------KLKSqVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQK---------- 2262
Cdd:pfam01576 809 DLQRELEEARasrdeilaqskesekKLKN-LEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKsalqdekrrl 887
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2263 ----AQVEDEL----AKVRIQMDELLKLKLKIEEQN------RSLMKKDKDKTQ------KVLAEEAGKMKSLAEEAARL 2322
Cdd:pfam01576 888 eariAQLEEELeeeqSNTELLNDRLRKSTLQVEQLTtelaaeRSTSQKSESARQqlerqnKELKAKLQEMEGTVKSKFKS 967
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2323 SVEAEEtARQRQIAESNLAE--QRALAEKMLKEKMQAIQEATklkAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKET 2400
Cdd:pfam01576 968 SIAALE-AKIAQLEEQLEQEsrERQAANKLVRRTEKKLKEVL---LQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAE 1043
|
1130 1140 1150
....*....|....*....|....*....|....*..
gi 736215636 2401 EGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSK 2437
Cdd:pfam01576 1044 EEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
176-273 |
9.67e-20 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 87.40 E-value: 9.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 176 KLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLD-PEDV 254
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 736215636 255 DVLHPDEKSIITYVSSLYD 273
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
172-271 |
1.41e-19 |
|
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: 86.77 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERdLGVTRLLDP 251
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|..
gi 736215636 252 EDVdVLH--PDEKSIITYVSSL 271
Cdd:cd21255 80 ADM-VLLpiPDKLIVMTYLCQL 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1995-2590 |
2.47e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.93 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1995 ELKKLKVIAEETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEAnkqke 2074
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL----- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2075 kaekeaekqvivAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQaaekakekaekEAALLRQKAAEAE 2154
Cdd:COG1196 308 ------------EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE-----------ELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2155 KQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRL 2234
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2235 DETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQNRSLMKKDKD-KTQKVLAEEAGKMK 2313
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2314 SLAEEAARLSVE--AEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKK------- 2384
Cdd:COG1196 525 AVAVLIGVEAAYeaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIgaavdlv 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2385 --LLEDKQQIQQRLDKETEGfqKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQ 2462
Cdd:COG1196 605 asDLREADARYYVLGDTLLG--RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2463 STETVVQKLETQRLQSTREADGLKEAIADLEKEREKLKKEAEELQNKSNKMANTQKEEIEQQKAIIQKSFISERELLLKR 2542
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 2543 QkAVEDEKKKLQKQFE----------DEVKKAEALKDEQERQRKLMEEEKKKLQAIMD 2590
Cdd:COG1196 763 E-ELERELERLEREIEalgpvnllaiEEYEELEERYDFLSEQREDLEEARETLEEAIE 819
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
57-157 |
2.66e-19 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 85.71 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 57 QKKTFTKWVNKHL--MKSQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQVKLVN 132
Cdd:cd21212 1 EIEIYTDWANHYLekGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 736215636 133 IRNDDIADGNPKLTLGLIWTIILHF 157
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
172-271 |
3.30e-19 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 85.67 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERdLGVTRLLDP 251
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 736215636 252 EDVDVLH-PDEKSIITYVSSL 271
Cdd:cd21254 80 SDMVLLAvPDKLTVMTYLYQI 100
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
172-272 |
3.73e-19 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 85.47 E-value: 3.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDP 251
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 736215636 252 EDVDVL--HPDEKSIITYVSSLY 272
Cdd:cd21200 81 EDMVRMgnRPDWKCVFTYVQSLY 103
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1478-2586 |
3.79e-19 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 96.40 E-value: 3.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1478 EQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLR-------KAAQEDAERLRKQ 1550
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRarlaarkQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1551 VAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKL----------RQIKVVEE---- 1616
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILlledqnsklsKERKLLEErise 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1617 -----VAQKSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQ----QEEANKAREQAEKELETWRQKAN 1687
Cdd:pfam01576 164 ftsnlAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEstdlQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1688 EALRLRLQAEEEAQKKSKTQE---EAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQV-----AQQKLSA 1759
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKkirELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTldttaAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1760 EQEcirlkadfdhaeqqrglldNELQRLKKevsATEKQRKLLEEELAKVRSEMDSLLKMKTEA---EKKTMSNTEKSKQL 1836
Cdd:pfam01576 324 KRE-------------------QEVTELKK---ALEEETRSHEAQLQEMRQKHTQALEELTEQleqAKRNKANLEKAKQA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1837 LESEALKMkqladeATRLRSVaeeakkqrQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKR 1916
Cdd:pfam01576 382 LESENAEL------QAELRTL--------QQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSS 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1917 KAED-EAYQRKLLEDQAA--QHKHDIQEKIihlksssdSEMVRQKTIVEETLRQkkiVEEEIHIIRINFEKASKGKSDLE 1993
Cdd:pfam01576 448 LLNEaEGKNIKLSKDVSSleSQLQDTQELL--------QEETRQKLNLSTRLRQ---LEDERNSLQEQLEEEEEAKRNVE 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1994 NELKKLKVIAEETQKsKLKAEAEAeklkklaaeeekkrkeseekvkrITAAEEEAARQCKAAQEEVARLEKKA---DEAN 2070
Cdd:pfam01576 517 RQLSTLQAQLSDMKK-KLEEDAGT-----------------------LEALEEGKKRLQRELEALTQQLEEKAaayDKLE 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2071 KQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKA 2150
Cdd:pfam01576 573 KTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAK 652
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2151 AEAEKQKKSAEEEAAKQAKAQKDA-------EKLKKAAEEEASKrAAAEAEALKQKKQAdAEMAKHKKEAD-QALKlkSQ 2222
Cdd:pfam01576 653 EELERTNKQLRAEMEDLVSSKDDVgknvhelERSKRALEQQVEE-MKTQLEELEDELQA-TEDAKLRLEVNmQALK--AQ 728
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2223 VEKELtmvKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDelAKVRIQMDeLLKLKLKIEEQNrslmkKDKDKTQ 2302
Cdd:pfam01576 729 FERDL---QARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVA--AKKKLELD-LKELEAQIDAAN-----KGREEAV 797
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2303 KVLAEEAGKMKSLaeeaarlsveaeetarQRQIAESNLAEQRALAEKMLKEKmqaiqeatKLKA-EAQELQKQKD-QAQE 2380
Cdd:pfam01576 798 KQLKKLQAQMKDL----------------QRELEEARASRDEILAQSKESEK--------KLKNlEAELLQLQEDlAASE 853
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2381 KAKKLLE-DKQQIQQRLDKETEGfqKSLEAERKRQLEvsaeAETLRLKvKELSDAQSKAENEAKKFKKQADEAKARlkDT 2459
Cdd:pfam01576 854 RARRQAQqERDELADEIASGASG--KSALQDEKRRLE----ARIAQLE-EELEEEQSNTELLNDRLRKSTLQVEQL--TT 924
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2460 EKQSTETVVQKLETQRLQSTREADGLKEAIADLEKEREKLKKEAEELQNKsnKMANTQkEEIEQQkaiiqksfISERELL 2539
Cdd:pfam01576 925 ELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEA--KIAQLE-EQLEQE--------SRERQAA 993
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*..
gi 736215636 2540 LKRQKAVEDEKKKLQKQFEDEVKKAEALKDEQERQRKLMEEEKKKLQ 2586
Cdd:pfam01576 994 NKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
172-276 |
1.82e-18 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 83.44 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGYqglRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVY-RQSNQENLEQAFSVAERDLGVTRLLD 250
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|....*.
gi 736215636 251 PEDVDVLHPDEKSIITYVSSLYDAMP 276
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSYFRNAKV 103
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
168-273 |
1.92e-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: 83.84 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 168 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTR 247
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 736215636 248 LLDPEDV-DVLHPDEKSIITYVSSLYD 273
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1508-1879 |
4.12e-18 |
|
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: 92.49 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1508 QLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERL-RKQVAEETQKKKNAEDELKRKSEAEKE-AAKQKQKALDd 1585
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVeRRRKLEEAEKARQAEMDRQAAIYAEQErMAMERERELE- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1586 lqkfKMQAEEAERRMKQAEEEKLR-QIKVVEEVAQKSAATQLQSHSMSFNVKASKLEESLKKE-QGTVLQLQEEAEQLRK 1663
Cdd:pfam17380 352 ----RIRQEERKRELERIRQEEIAmEISRMRELERLQMERQQKNERVRQELEAARKVKILEEErQRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1664 QQEEANKAR-----EQAEKELETWRQKanealrlRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEdaalkqkdna 1738
Cdd:pfam17380 428 EQEEARQREvrrleEERAREMERVRLE-------EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE---------- 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1739 ekelekqrtfaeqvaqqklsaeqecirlkadfdhaEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEM-DSLLK 1817
Cdd:pfam17380 491 -----------------------------------EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIyEEERR 535
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736215636 1818 MKTEAEKKTMSNTEKSKQLLEsealKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEA 1879
Cdd:pfam17380 536 REAEEERRKQQEMEERRRIQE----QMRKATEERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1551-2401 |
4.13e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 92.82 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1551 VAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRmkQAEEEKLRQIKVVEEVAQKSAatqlqshs 1630
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERY--QALLKEKREYEGYELLKEKEA-------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1631 msfnvkaskLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETwrqkANEALRlRLQAEEEAQKKSKTQE-E 1709
Cdd:TIGR02169 235 ---------LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE----LNKKIK-DLGEEEQLRVKEKIGElE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1710 AERQKVEAERDAKKRaKAEDAALKQKdNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKK 1789
Cdd:TIGR02169 301 AEIASLERSIAEKER-ELEDAEERLA-KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1790 EVSATEKQRKLLEEELAKVRSEMDSLlkmKTEAEKKTMSNTEKSKQLLESEAlKMKQLADEATRLRSVAEEAKKQRQTAE 1869
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINEL---KRELDRLQEELQRLSEELADLNA-AIAGIEAKINELEEEKEDKALEIKKQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1870 EEAARQRAEAEKILKEKLAAINEATRL---RTEAEIALKAKEAENERLKRKAEDEAYQRKLLED---------------- 1930
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDLKEEYDRVekeLSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgtvaqlgsvg 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1931 ---QAA--------------QHKHDIQEKIIHLKSSSDSEM-------VRQKTIVEETLRQKKIVEEEIHIIRIN--FEK 1984
Cdd:TIGR02169 535 eryATAievaagnrlnnvvvEDDAVAKEAIELLKRRKAGRAtflplnkMRDERRDLSILSEDGVIGFAVDLVEFDpkYEP 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1985 ASK---GKSDLENELKKLKVIAEETQKSKLkaeaEAEKLKKLAA---------EEEKKRKESEEKVKRITAAEEEAARQC 2052
Cdd:TIGR02169 615 AFKyvfGDTLVVEDIEAARRLMGKYRMVTL----EGELFEKSGAmtggsraprGGILFSRSEPAELQRLRERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2053 KAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKcssaEQKAQEVLSKNKEDslaQQKMKEEFENAKRLAQAA 2132
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE----EEKLKERLEELEED---LSSLEQEIENVKSELKEL 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2133 EKAKEKaekeaalLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKE 2212
Cdd:TIGR02169 764 EARIEE-------LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2213 ADQALKLKSQVEKEltMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDEllkLKLKIEEQNRS 2292
Cdd:TIGR02169 837 ELQEQRIDLKEQIK--SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE---LERKIEELEAQ 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2293 L-MKKDKDKTQKVLAEEA-GKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALaEKMLKEKMQAIQeatklkaEAQE 2370
Cdd:TIGR02169 912 IeKKRKRLSELKAKLEALeEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQ-------EYEE 983
|
890 900 910
....*....|....*....|....*....|.
gi 736215636 2371 LQKQKDQAQEKAKKLLEDKQQIQQRLDKETE 2401
Cdd:TIGR02169 984 VLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
175-271 |
5.23e-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: 81.98 E-value: 5.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 175 EKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQ----ENLEQAFSVAERDLGVTRLLD 250
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 736215636 251 PEDVDVLHPDEKSIITYVSSL 271
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1641-2643 |
9.70e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 91.78 E-value: 9.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1641 EESLKKEQGTVLQLQEEAEQLRKQQ----EEANKAREQAEKELETWRQKanEALRLRLQAEEEAQKKSKTQEEAerqKVE 1716
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHqqlcEEKNALQEQLQAETELCAEA--EEMRARLAARKQELEEILHELES---RLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1717 AERDAKKRAKAEDAALKQKdnaEKELEKQRTfAEQVAQQKLSAEQecIRLKADFDHAEQQRGLLDNELQRLKKEvsatek 1796
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQH---IQDLEEQLD-EEEAARQKLQLEK--VTTEAKIKKLEEDILLLEDQNSKLSKE------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1797 qRKLLEEELAKVRSEMdsllkmkTEAEkktmsntEKSKQLLESEALKMKQLADEATRLRSvaEEakKQRQtaEEEAARQR 1876
Cdd:pfam01576 154 -RKLLEERISEFTSNL-------AEEE-------EKAKSLSKLKNKHEAMISDLEERLKK--EE--KGRQ--ELEKAKRK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1877 AEAEKI-LKEKLAainEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRklleDQAAQHKHDIQEKIIHLKSSSDSEmv 1955
Cdd:pfam01576 213 LEGESTdLQEQIA---ELQAQIAELRAQLAKKEEELQAALARLEEETAQK----NNALKKIRELEAQISELQEDLESE-- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1956 rqktiveetlrqkkiveeeihiiRINFEKASKGKSDLENELKKLKVIAEET-------QKSKLKAEAEAEKLKK-LAAEE 2027
Cdd:pfam01576 284 -----------------------RAARNKAEKQRRDLGEELEALKTELEDTldttaaqQELRSKREQEVTELKKaLEEET 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2028 EKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSK 2107
Cdd:pfam01576 341 RSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQAR 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2108 NKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQ-KDAEKLKKAAEEEAS 2186
Cdd:pfam01576 421 LSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKlNLSTRLRQLEDERNS 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2187 KRaaaeaEALKQKKQADAEMAKHKKEADQAL-KLKSQVEKELTMVKLRldETDKQKALLDEELQRVKGEVNDAVKQKAqv 2265
Cdd:pfam01576 501 LQ-----EQLEEEEEAKRNVERQLSTLQAQLsDMKKKLEEDAGTLEAL--EEGKKRLQRELEALTQQLEEKAAAYDKL-- 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2266 edELAKVRIQMD-ELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARlsveAEETARQRQIAESNLAeqR 2344
Cdd:pfam01576 572 --EKTKNRLQQElDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDR----AEAEAREKETRALSLA--R 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2345 ALAEkmLKEKMQAIQEATK-LKAEAQELQKQKDQAQ------EKAKKLLEdkqQIQQRLDKETEGFQKSLEA--ERKRQL 2415
Cdd:pfam01576 644 ALEE--ALEAKEELERTNKqLRAEMEDLVSSKDDVGknvhelERSKRALE---QQVEEMKTQLEELEDELQAteDAKLRL 718
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2416 EVSAEAETLRLKvKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTETVV--QKLETQRLQSTREADGLKEAIADLE 2493
Cdd:pfam01576 719 EVNMQALKAQFE-RDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAakKKLELDLKELEAQIDAANKGREEAV 797
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2494 KEREKLKKEAEELQNKSNKMANTQKEEIEQQKAIIQKSFISERELL-----------LKRQkaVEDEKKKLQKQFEDEVK 2562
Cdd:pfam01576 798 KQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLqlqedlaaserARRQ--AQQERDELADEIASGAS 875
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2563 KAEALKDEQER---QRKLMEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEM---EVLEKKRLDQEKQLGAENQKLREKLQ 2636
Cdd:pfam01576 876 GKSALQDEKRRleaRIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELaaeRSTSQKSESARQQLERQNKELKAKLQ 955
|
....*..
gi 736215636 2637 CLEGASK 2643
Cdd:pfam01576 956 EMEGTVK 962
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
58-155 |
1.22e-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: 81.23 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 58 KKTFTKWVNKHL-MKSQRHITDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQV-KLVNI 133
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 736215636 134 RNDDI-ADGNPKLTLGLIWTIIL 155
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1417-2269 |
4.19e-17 |
|
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: 89.72 E-value: 4.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1417 LDKQKQIAEAQAKSVIKAEQEAQELKlKMKEEASKRQDVAVDAEQQKQNIQhELHHLKSLSEQEIKSKSQQLEHALVSHT 1496
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLK-QYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1497 KIEEEIHTiriqLEMTIKQKKTAESELQQLRDK-------------------AAEAEKLRKAAQEDAERLRKQVAEETQK 1557
Cdd:TIGR00606 266 KLDNEIKA----LKSRKKQMEKDNSELELKMEKvfqgtdeqlndlyhnhqrtVREKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1558 KKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAE--------EAERRMKQAEEEKLRQikvvEEVAQKSAATQLQSH 1629
Cdd:TIGR00606 342 KTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfergpFSERQIKNFHTLVIER----QEDEAKTAAQLCADL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1630 SMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAE------KELETWRQKANEALRLRLQAEEEAQKK 1703
Cdd:TIGR00606 418 QSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQqlegssDRILELDQELRKAERELSKAEKNSLTE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1704 SKTQEEAERQKVEAERDAKKRAKAEDaalkqkdNAEKELEKQ-RTFAEQVAQQKLSAEQECIRLKAD-FDHAEQQRGLLD 1781
Cdd:TIGR00606 498 TLKKEVKSLQNEKADLDRKLRKLDQE-------MEQLNHHTTtRTQMEMLTKDKMDKDEQIRKIKSRhSDELTSLLGYFP 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1782 NELQrLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLES--EALKMKQLADEATRLRSVAE 1859
Cdd:TIGR00606 571 NKKQ-LEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1860 EAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATR-LRTEAEIALKAKEAENERLKRKAEDEAYQRKLledqaaQHKHD 1938
Cdd:TIGR00606 650 KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRvFQTEAELQEFISDLQSKLRLAPDKLKSTESEL------KKKEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1939 IQEKIIHLKSSSDSEMVRQKTIVEETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKVIAE-------------- 2004
Cdd:TIGR00606 724 RRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTdvtimerfqmelkd 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2005 -ETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQ 2083
Cdd:TIGR00606 804 vERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2084 VIVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEe 2163
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIEN- 962
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2164 aakqaKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRldetDKQKAL 2243
Cdd:TIGR00606 963 -----KIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRE----NELKEV 1033
|
890 900
....*....|....*....|....*.
gi 736215636 2244 LDEELQRVKGEVNDAVKQKAQVEDEL 2269
Cdd:TIGR00606 1034 EEELKQHLKEMGQMQVLQMKQEHQKL 1059
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
174-285 |
1.98e-16 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 78.11 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 174 KEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDPED 253
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 736215636 254 -VDVLHPDEKSIITYVSSLYDAMprvpdVQEGV 285
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1382-2179 |
3.10e-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: 86.56 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1382 IKFITETQRRLEDDEKASEKLKEEERKKMAEIQAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQ 1461
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1462 QKQniqhELHHLKSLSEQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIK-QKKTAESELQQLRDKAAEAEKLRKAA 1540
Cdd:pfam02463 360 ELE----KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQlLLELARQLEDLLKEEKKEELEILEEE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1541 QEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKalDDLQKFKMQAEEAERRMKQAEEE-KLRQIKVVEEVAQ 1619
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE--TQLVKLQEQLELLLSRQKLEERSqKESKARSGLKVLL 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1620 KSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEE 1699
Cdd:pfam02463 514 ALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKS 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1700 AQKKSKTQEEAERQKVEAERDAkkRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAEQeciRLKADFDHAEQQRGL 1779
Cdd:pfam02463 594 IAVLEIDPILNLAQLDKATLEA--DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVS---LEEGLAEKSEVKASL 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1780 LDNELQRLKKEVsatEKQRKLLEEELAKVRSEMdslLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAE 1859
Cdd:pfam02463 669 SELTKELLEIQE---LQEKAESELAKEEILRRQ---LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLK 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1860 EAKKQRQtAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKaKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDI 1939
Cdd:pfam02463 743 QKIDEEE-EEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK-VEEEKEEKLKAQEEELRALEEELKEEAELLEEE 820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1940 QEKIIHLKSSSDSEMVRQKTIVEETLRQKKIVEEEIHIirinfekaskgksdLENELKKLKVIAEETQKSKLKAEAEAEK 2019
Cdd:pfam02463 821 QLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELER--------------LEEEITKEELLQELLLKEEELEEQKLKD 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2020 LKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEankqkeKAEKEAEKQVIVAKEAAQKCSSAEQ 2099
Cdd:pfam02463 887 ELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEE------EPEELLLEEADEKEKEENNKEEEEE 960
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2100 KAQEVLSKNKEDSLAQQKMKEEFENakrlaqaaekakekaekeaALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKK 2179
Cdd:pfam02463 961 RNKRLLLAKEELGKVNLMAIEEFEE-------------------KEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
174-273 |
3.28e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 77.31 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 174 KEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDPED 253
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 736215636 254 VDVL--HPDEKSIITYVSSLYD 273
Cdd:cd21261 83 MMVMgrKPDPMCVFTYVQSLYN 104
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
174-277 |
3.72e-16 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 77.40 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 174 KEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDPED 253
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 736215636 254 VDVL--HPDEKSIITYVSSLYDAMPR 277
Cdd:cd21258 83 MMIMgkKPDSKCVFTYVQSLYNHLRR 108
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1407-2025 |
5.35e-16 |
|
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: 85.79 E-value: 5.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1407 RKKMAEIQAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQHELHHLKSLSEQEIKS--K 1484
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQShaY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1485 SQQLEHALVSHTKIEEEIHTIRIQLEmTIKQKKTAESELQQLRDKAAEAEKLrKAAQEDAERLRKQVAEETQKKKNAEDE 1564
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIE-ELRAQEAVLEETQERINRARKAAPL-AAHIKAVTQIEQQAQRIHTELQSKMRS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1565 LKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQ---SHSMSFNVKASKLE 1641
Cdd:TIGR00618 323 RAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQqqkTTLTQKLQSLCKEL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1642 ESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQK-----KSKTQEEAERQKVe 1716
Cdd:TIGR00618 403 DILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsaqslKEREQQLQTKEQI- 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1717 AERDAKKRAKAEDAALKQKDNaEKELEKQRTFAEQVAQQKLSAEQECIRLKAdfdhAEQQRGLLDNELQRLKKEVSATEK 1796
Cdd:TIGR00618 482 HLQETRKKAVVLARLLELQEE-PCPLCGSCIHPNPARQDIDNPGPLTRRMQR----GEQTYAQLETSEEDVYHQLTSERK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1797 QRKLLEEELAKVRSEMdSLLKMKTEAEKKTMSNTEKSKQLLEsealkmKQLADEATRLRSVAEEAKKQRQTAEEEAARQR 1876
Cdd:TIGR00618 557 QRASLKEQMQEIQQSF-SILTQCDNRSKEDIPNLQNITVRLQ------DLTEKLSEAEDMLACEQHALLRKLQPEQDLQD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1877 AEAEKILKEKLAAINEATRLRTEAEIAlKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSSDSEMVR 1956
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQLTLT-QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRE 708
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 1957 QKTIVEETLRQKkiveEEIHIIRINFEKASKGKSDLENELKKLkviAEETQKSKLKAEAEAEKLKKLAA 2025
Cdd:TIGR00618 709 LETHIEEYDREF----NEIENASSSLGSDLAAREDALNQSLKE---LMHQARTVLKARTEAHFNNNEEV 770
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1310-1914 |
6.22e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 85.88 E-value: 6.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1310 KDKIDSCQKNAKAYIDSVKDYELQILTYKALQDpmASPLKKPKMDCASDNIIQEYVTLRTRYSELmtltSQYIKFITETQ 1389
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLE--ELRLEVSELEEEIEELQKELYALANEISRL----EQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1390 RRLEDDEKASEKLKEEERKKMAEIQAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQHE 1469
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1470 LHHLKSLSEQeIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMtiKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRK 1549
Cdd:TIGR02168 392 ELQIASLNNE-IERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1550 QVAEETQKKKNAEDELKRKS-----------------------------------------------EAEKEAA------ 1576
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQarldslerlqenlegfsegvkallknqsglsgilgvlselisvdegyEAAIEAAlggrlq 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1577 -----------------KQKQK------ALDDLQKFKMQAEEAERRMKQ-------AEEEK------------LRQIKVV 1614
Cdd:TIGR02168 549 avvvenlnaakkaiaflKQNELgrvtflPLDSIKGTEIQGNDREILKNIegflgvaKDLVKfdpklrkalsylLGGVLVV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1615 EEVAQksaATQLQS---HSMSFNVKASKL--------EESLKKEQGTvLQLQEEAEQLRKQQEEANKAREQAEKELETWR 1683
Cdd:TIGR02168 629 DDLDN---ALELAKklrPGYRIVTLDGDLvrpggvitGGSAKTNSSI-LERRREIEELEEKIEELEEKIAELEKALAELR 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1684 QKANEalrlrlqAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAEQEC 1763
Cdd:TIGR02168 705 KELEE-------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1764 IRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQL---LESE 1840
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELsedIESL 857
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736215636 1841 ALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERL 1914
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
176-273 |
6.47e-16 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 76.46 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 176 KLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLD-PEDV 254
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 736215636 255 DVLHPDEKSIITYVSSLYD 273
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1480-2068 |
9.27e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 85.12 E-value: 9.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1480 EIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLrkqvaeeTQKKK 1559
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI-------EELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1560 NAEDELKRKsEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQksaatqlqshsmsFNVKASK 1639
Cdd:PRK03918 246 ELESLEGSK-RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE-------------YLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1640 LEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEK------ELETWRQKANEALRLRLQAEE-EAQKKSKTQEEAER 1712
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekrleELEERHELYEEAKAKKEELERlKKRLTGLTPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1713 QKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAqqklSAEQECIRLKADFDhaEQQRGLLdneLQRLKKEVS 1792
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK----KAKGKCPVCGRELT--EEHRKEL---LEEYTAELK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1793 ATEKQRKLLEEELAKVRSEmdsllkmKTEAEKKTmsntekskqLLESEALKMKQLADEATRLRSV--------AEEAKKQ 1864
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKE-------LRELEKVL---------KKESELIKLKELAEQLKELEEKlkkynleeLEKKAEE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1865 RQTAEEEAARQRAEAeKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKII 1944
Cdd:PRK03918 527 YEKLKEKLIKLKGEI-KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYL 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1945 HLKSSSDSemvrqktiVEETLRQKKIVEEEIhiirinfEKASKGKSDLENELKKLKVIAEETQKSklKAEAEAEKLKKLA 2024
Cdd:PRK03918 606 ELKDAEKE--------LEREEKELKKLEEEL-------DKAFEELAETEKRLEELRKELEELEKK--YSEEEYEELREEY 668
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 736215636 2025 AEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADE 2068
Cdd:PRK03918 669 LELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
54-153 |
1.06e-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: 76.03 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 54 DRVQKKTFTKWVNKHLMKSQ-RHITDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFL-KHRQV 128
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIeEDLKI 81
|
90 100
....*....|....*....|....*
gi 736215636 129 KLVNIRNDDIADGNPKLTLGLIWTI 153
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1717-2491 |
1.30e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 84.73 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1717 AERDAKKRAkaedaALKQKDNAEKELEKQRTFAEQVAQQ--KLSAEQE-CIRLKADFDHAEQQRG-LLDNELQRLKKEVS 1792
Cdd:TIGR02169 166 AEFDRKKEK-----ALEELEEVEENIERLDLIIDEKRQQleRLRREREkAERYQALLKEKREYEGyELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1793 ATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEAL----KMKQLADEATRLRSVAEEAKKQRQTA 1868
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrvkeKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1869 EEEAARQRAEAEKILKEKLA---AINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIqEKIIH 1945
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL-EKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1946 LKSSSDSEMVRqktiVEETLRQKKIVEEEIHiirinfeKASKGKSDLENELK-KLKVIAEETQKSKLKAEAEAEKLKKLA 2024
Cdd:TIGR02169 400 EINELKRELDR----LQEELQRLSEELADLN-------AAIAGIEAKINELEeEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2025 AEEEKKRKESEEKVKRITAAEEEAAR---QCKAAQEEVaRLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKC--SSAEQ 2099
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEaeaQARASEERV-RGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAieVAAGN 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2100 KAQEVLSKNKEDS-----------------LAQQKMK------------------------------------------E 2120
Cdd:TIGR02169 548 RLNNVVVEDDAVAkeaiellkrrkagratfLPLNKMRderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvvE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2121 EFENAKRLAQAAEKAKEK--------------AEKEAALLRQKAAEAEKQKKSAEEEAAKQAKA--QKDAEKLKKAAEEE 2184
Cdd:TIGR02169 628 DIEAARRLMGKYRMVTLEgelfeksgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSslQSELRRIENRLDEL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2185 ASKRAAAEA---EALKQKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDavkq 2261
Cdd:TIGR02169 708 SQELSDASRkigEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND---- 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2262 kaqVEDELAKVRIQ-----MDELLKLKLKIEEQNRSLMKKDKDKTQ-KVLAEEagKMKSLAEEaaRLSVEAEETARQRQI 2335
Cdd:TIGR02169 784 ---LEARLSHSRIPeiqaeLSKLEEEVSRIEARLREIEQKLNRLTLeKEYLEK--EIQELQEQ--RIDLKEQIKSIEKEI 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2336 AESN--LAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQ------KSL 2407
Cdd:TIGR02169 857 ENLNgkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleeelSEI 936
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2408 EAERKRQLEVSAE---AETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDtekqstetvvqkLETQRLQSTREADG 2484
Cdd:TIGR02169 937 EDPKGEDEEIPEEelsLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDE------------LKEKRAKLEEERKA 1004
|
....*..
gi 736215636 2485 LKEAIAD 2491
Cdd:TIGR02169 1005 ILERIEE 1011
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1414-1977 |
4.48e-15 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 82.46 E-value: 4.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1414 QAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVaVDAEQQKQNIQHELHHLKSLSEQEIKSKSQQLEHALV 1493
Cdd:pfam05483 105 ENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDL-IKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1494 SHTKIEEEIHTIRIQLEMTIKQKKTAESELQ-QLRDKAAEAEKLRKAAQEDAERLRKQVAE---ETQKKKNAEDELKRKS 1569
Cdd:pfam05483 184 VYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQVSLlliQITEKENKMKDLTFLL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1570 EAEKEAAKQKQkalddlQKFKMQAEEaerrMKQAEEEKLRQIKVVEEVA---QKSAATQlqshsmsfnvkaSKLEESLKK 1646
Cdd:pfam05483 264 EESRDKANQLE------EKTKLQDEN----LKELIEKKDHLTKELEDIKmslQRSMSTQ------------KALEEDLQI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1647 EQGTVLQLQEEAEqlrKQQEEANKAREQAE---KELETWRQKANEALRLRLQAEE-----------EAQKKSKTQEEAER 1712
Cdd:pfam05483 322 ATKTICQLTEEKE---AQMEELNKAKAAHSfvvTEFEATTCSLEELLRTEQQRLEknedqlkiitmELQKKSSELEEMTK 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1713 QK--VEAERDAKKRAKAEDAAL----KQKDNAEKEL---EKQRTFAEQVAQQKL-SAEQECIRLKADFDHAEQQRGLLDN 1782
Cdd:pfam05483 399 FKnnKEVELEELKKILAEDEKLldekKQFEKIAEELkgkEQELIFLLQAREKEIhDLEIQLTAIKTSEEHYLKEVEDLKT 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1783 ELQRLK-KEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMK--QLADEatrLRSVAE 1859
Cdd:pfam05483 479 ELEKEKlKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKemNLRDE---LESVRE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1860 EAKKQR-------QTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKE---AENERLKRKAEDE-----AYQ 1924
Cdd:pfam05483 556 EFIQKGdevkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEelhQENKALKKKGSAEnkqlnAYE 635
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 736215636 1925 RKL--LEDQAAQHKHDIQEKIIHLKSSSDSEMVRQKTIVEETLRQKKIVEEEIHI 1977
Cdd:pfam05483 636 IKVnkLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKL 690
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3108-3146 |
5.95e-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: 5.95e-15
10 20 30
....*....|....*....|....*....|....*....
gi 736215636 3108 LLEAQAATGFVIDPVKNERVTVDEAVKSGLVGPELHERL 3146
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
174-285 |
7.34e-15 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 73.58 E-value: 7.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 174 KEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDPED 253
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 736215636 254 -VDVLHPDEKSIITYVSSLYDAMprvpdVQEGV 285
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL-----VQKGL 110
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4091-4129 |
8.21e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.82 E-value: 8.21e-15
10 20 30
....*....|....*....|....*....|....*....
gi 736215636 4091 LLEAQIATGGIIDPQESHRLPVEAAYERGLFDEEMNEIL 4129
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
57-157 |
9.45e-15 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 73.10 E-value: 9.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 57 QKKTFTKWVNKHLMK--SQRHITDLYEDLRDGHNLISLLEVLSGETL------PREKGRMRfhklQNVQIALDFLKHRQV 128
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 736215636 129 KLVNIRNDDIADGNPKLTLGLIWTIILHF 157
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1679-2250 |
1.92e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.47 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1679 LETWRQKANEAlRLRLQAEEEAQKKSKTQEEAERQKVEaERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQvaqqKLS 1758
Cdd:PRK02224 164 LEEYRERASDA-RLGVERVLSDQRGSLDQLKAQIEEKE-EKDLHERLNGLESELAELDEEIERYEEQREQARE----TRD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1759 AEQECIRlkadfDHAEQQRGL--LDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAekktMSNTEKSKQL 1836
Cdd:PRK02224 238 EADEVLE-----EHEERREELetLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL----LAEAGLDDAD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1837 LESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIA----------LKA 1906
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAreavedrreeIEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1907 KEAENERLKRKAEDEAYQRKLLED---QAAQHKHDIQEKIIHLKSSSDSEmvrQKTIVE-ETLRQK-------KIVEEEI 1975
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDfleELREERDELREREAELEATLRTA---RERVEEaEALLEAgkcpecgQPVEGSP 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1976 HIIRInfEKASKGKSDLENELKKLkviaeETQKSKLKAEAE-AEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKA 2054
Cdd:PRK02224 466 HVETI--EEDRERVEELEAELEDL-----EEEVEEVEERLErAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2055 AQ---EEVARLEKKADEAnkqkekaekeaekqvivaKEAAQKcssAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQA 2131
Cdd:PRK02224 539 AEelrERAAELEAEAEEK------------------REAAAE---AEEEAEEAREEVAELNSKLAELKERIESLERIRTL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2132 AEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALkqkKQADAEMAKHKK 2211
Cdd:PRK02224 598 LAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYL---EQVEEKLDELRE 674
|
570 580 590
....*....|....*....|....*....|....*....
gi 736215636 2212 EADQALKLKSQVEKELTmvklRLDETDKQKALLDEELQR 2250
Cdd:PRK02224 675 ERDDLQAEIGAVENELE----ELEELRERREALENRVEA 709
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1853-2633 |
2.08e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.88 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1853 RLRSVAE-EAKKQRQTAEEEAARQR-AEAEKILKEKlaaINEATRLRTEAEIALKAKEAenerLKRKAEDEAYqrklled 1930
Cdd:TIGR02169 161 EIAGVAEfDRKKEKALEELEEVEENiERLDLIIDEK---RQQLERLRREREKAERYQAL----LKEKREYEGY------- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1931 qaaqhkhdiqekiIHLKSssdsemvrqktiVEETLRQKKIVEEEIHIIRINFEKASKGKSDLENEL-KKLKVIAEETQKS 2009
Cdd:TIGR02169 227 -------------ELLKE------------KEALERQKEAIERQLASLEEELEKLTEEISELEKRLeEIEQLLEELNKKI 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2010 KLKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKE 2089
Cdd:TIGR02169 282 KDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2090 AAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAK 2169
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2170 AQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQ 2249
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2250 RVKGEVNDAVKQKAQ-----------------VEDEL-AKVRIQMDELLKL---------KLKIEEQNRSLMKKD----- 2297
Cdd:TIGR02169 522 GVHGTVAQLGSVGERyataievaagnrlnnvvVEDDAvAKEAIELLKRRKAgratflplnKMRDERRDLSILSEDgvigf 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2298 -------KDKTQKV--------------------------------LAEEAGKM--------------KSLAEEAARLSV 2324
Cdd:TIGR02169 602 avdlvefDPKYEPAfkyvfgdtlvvedieaarrlmgkyrmvtlegeLFEKSGAMtggsraprggilfsRSEPAELQRLRE 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2325 EAEETARQRqiaeSNLAEQRALAEKMLKEKMQAIQEATK----LKAEAQELQKQKDQAQEKAKKLLEDKQQIQQ-RLDKE 2399
Cdd:TIGR02169 682 RLEGLKREL----SSLQSELRRIENRLDELSQELSDASRkigeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeIENVK 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2400 TEgfQKSLEAERKRQLEVSA---------EAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARL--KDTEKQSTETVV 2468
Cdd:TIGR02169 758 SE--LKELEARIEELEEDLHkleealndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLnrLTLEKEYLEKEI 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2469 QKLETQRLQSTREADGLKEAIADLEKEREKLKKEAEELQNK----SNKMANTQKE--EIEQQKAIIQ------KSFISER 2536
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAlrdlESRLGDLKKErdELEAQLRELErkieelEAQIEKK 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2537 ELLLKRQKAVEDEKKKLQKQFEDEVKKAEALKDEQERQRKLMEEEKKKLQAIMD------AAVKKQKEAEADMKNKQTEM 2610
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnmLAIQEYEEVLKRLDELKEKR 995
|
890 900
....*....|....*....|...
gi 736215636 2611 EVLEKKRLDQEKQLGAENQKLRE 2633
Cdd:TIGR02169 996 AKLEEERKAILERIEEYEKKKRE 1018
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1458-2005 |
2.24e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.47 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1458 DAEQQKQNIQHELHHLKSLSEQEIKSKsQQLEHALVSHTKIEEEIHTIriqlemtikqkktaESELQQLRDKAAEAEKLR 1537
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETR-DEADEVLEEHEERREELETL--------------EAEIEDLRETIAETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1538 KAAQEDAERLRKQVAEETQKKKNAEDELKRkSEAEKEAAKQKQKALD---------------DLQKFKMQAEEAERRMKQ 1602
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGL-DDADAEAVEARREELEdrdeelrdrleecrvAAQAHNEEAESLREDADD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1603 AEEEklrqikvveevaqksaATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETW 1682
Cdd:PRK02224 354 LEER----------------AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1683 RQKANEAlrlrlqAEEEAQKKSKTQEEAER-QKVEAERDAKKRAKAEDaALKQKDNAEkELEKQRTFAEQVAQQKLSAEQ 1761
Cdd:PRK02224 418 REERDEL------REREAELEATLRTARERvEEAEALLEAGKCPECGQ-PVEGSPHVE-TIEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1762 ECIRLKADFDHAEqqrglldnELQRLKKEVSATEKQRKLLEEELAKVRSEmdsllkmkteaekktmsntekskqlLESEA 1841
Cdd:PRK02224 490 EVEEVEERLERAE--------DLVEAEDRIERLEERREDLEELIAERRET-------------------------IEEKR 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1842 LKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAeKILKEKLAAINEA----TRLRTE-AEIALKAKEAENERLKR 1916
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV-AELNSKLAELKERieslERIRTLlAAIADAEDEIERLREKR 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1917 KAEDEayqrklLEDQAAQHKHDIQEKIIHLKSSSDSEMVrqktiveETLRQKKI--------VEEEIHIIRINFEKASKG 1988
Cdd:PRK02224 616 EALAE------LNDERRERLAEKRERKRELEAEFDEARI-------EEAREDKEraeeyleqVEEKLDELREERDDLQAE 682
|
570
....*....|....*..
gi 736215636 1989 KSDLENELKKLKVIAEE 2005
Cdd:PRK02224 683 IGAVENELEELEELRER 699
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1458-1871 |
2.28e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 79.81 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1458 DAEQQKQNIQHELHHLKSLsEQEIKSKSQQLEHALVSHTKIEEEIHTIR--IQLEMTIKQKKTAESELQQLRDKAAEAEK 1535
Cdd:COG4717 75 ELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1536 LRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVE 1615
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1616 EVAQKSAATQ-----------------LQSHSMSFNVKASKLEESLKKEQGTV----LQLQEEAEQLRKQQEEANKAREQ 1674
Cdd:COG4717 234 NELEAAALEErlkearlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLallfLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1675 ---AEKELETWRQK-----------ANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAK-KRAKAED-----AALKQ 1734
Cdd:COG4717 314 eelEEEELEELLAAlglppdlspeeLLELLDRIEELQELLREAEELEEELQLEELEQEIAALlAEAGVEDeeelrAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1735 KDNAEKELEKQRTFAEQVAQQKLSAEQEcirlkadfdHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDS 1814
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEEL---------LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 1815 LLKMKTEAEKktmsnteksKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEE 1871
Cdd:COG4717 465 LEEDGELAEL---------LQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1414-1860 |
2.41e-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: 80.40 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1414 QAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQHELHHLKSLSEQEIKSKSQQLEHA-- 1491
Cdd:TIGR00618 437 QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNpa 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1492 -----------------LVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVaEE 1554
Cdd:TIGR00618 517 rqdidnpgpltrrmqrgEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT-VR 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1555 TQKKKNAEDELKRKSEAEKEAAK-QKQKALDDLQKF-----KMQAEEAERRMKQAEEEKLRQikvvEEVAQKSAATQLQS 1628
Cdd:TIGR00618 596 LQDLTEKLSEAEDMLACEQHALLrKLQPEQDLQDVRlhlqqCSQELALKLTALHALQLTLTQ----ERVREHALSIRVLP 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1629 HSmsfnvKASKLEESLKKEQGTVLQLQEEAEQLRKQQEeanKAREQAEKELETWR-----QKANEALRLRLQAEEEAQKK 1703
Cdd:TIGR00618 672 KE-----LLASRQLALQKMQSEKEQLTYWKEMLAQCQT---LLRELETHIEEYDRefneiENASSSLGSDLAAREDALNQ 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1704 S-KTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELE-----KQRTFAEQVAQQKLSAEQecIRLKAdfDHAEQQR 1777
Cdd:TIGR00618 744 SlKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAaeiqfFNRLREEDTHLLKTLEAE--IGQEI--PSDEDIL 819
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1778 GLLDNELQrlkKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSV 1857
Cdd:TIGR00618 820 NLQCETLV---QEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKF 896
|
...
gi 736215636 1858 AEE 1860
Cdd:TIGR00618 897 LHE 899
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2306-2629 |
3.52e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2306 AEEAGKMKSLAEEAARLsvEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKL 2385
Cdd:COG1196 209 AEKAERYRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2386 LEDKQQIQQRLDKETEgfQKSLEAERKRQLEvsAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQste 2465
Cdd:COG1196 287 QAEEYELLAELARLEQ--DIARLEERRRELE--ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE--- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2466 tvVQKLETQRLQSTREADGLKEAIADLekereklkkeaeelqnksnkmantQKEEIEQQKAII-----QKSFISERELLL 2540
Cdd:COG1196 360 --LAEAEEALLEAEAELAEAEEELEEL------------------------AEELLEALRAAAelaaqLEELEEAEEALL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2541 KRQKAVEDEKKKLQKQFEDEVKKAEALKDEQERQRKLMEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEKKRLDQ 2620
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
....*....
gi 736215636 2621 EKQLGAENQ 2629
Cdd:COG1196 494 LLLLEAEAD 502
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
177-272 |
1.27e-13 |
|
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: 70.08 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 177 LLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAErDLGVTRLLDPED-VD 255
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 736215636 256 VLHPDEKSIITYVSSLY 272
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
658-848 |
1.34e-13 |
|
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: 72.86 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 658 QLHAFVIAATKELMWLNEKEEEEVNYDWSERNTNMTAKKDNYSGLMRDLELREKKVNVVQATGDKLLRDGHPARKTVEAF 737
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 738 TGALQTQWSWLLQLCCCVETHLKENTAYYQFFSDVKEAEDKIKKMQDTMKRKYTCDrsvTVTRLEDLLQDATDDKEQLAE 817
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|.
gi 736215636 818 FQTHLEGLKRRAKTIIQLRPRNPATAIKGKQ 848
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1292-2182 |
1.73e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 77.52 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1292 LREQLAEEKKLLEEIEKNKDKIDSCQKNAKayiDSVKDYELQILTYKAL----QDPMASPLKKPKMDCASDNIIQEyvtl 1367
Cdd:pfam01576 192 LEERLKKEEKGRQELEKAKRKLEGESTDLQ---EQIAELQAQIAELRAQlakkEEELQAALARLEEETAQKNNALK---- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1368 rtRYSELMTLtsqyikfITETQRRLEDDEKASEKLKEEERKKMAEIQA---ELDKQKQIAEAQAKSVIKAEQEAQELKlK 1444
Cdd:pfam01576 265 --KIRELEAQ-------ISELQEDLESERAARNKAEKQRRDLGEELEAlktELEDTLDTTAAQQELRSKREQEVTELK-K 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1445 MKEEASKRQDVAVDAEQQKQNIQhelhhLKSLSEQ-----EIKSKSQQLEHALVSHTK-IEEEIHTIRIQLEMTIKQKKT 1518
Cdd:pfam01576 335 ALEEETRSHEAQLQEMRQKHTQA-----LEELTEQleqakRNKANLEKAKQALESENAeLQAELRTLQQAKQDSEHKRKK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1519 AESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAER 1598
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLST 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1599 RMKQAEEEK--LRQIKVVEEVAQKSAATQLQSHSMSFNVKASKLEE---SLKKEQGTVLQLQEEAEQLRKQQEEANKARE 1673
Cdd:pfam01576 490 RLRQLEDERnsLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEdagTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1674 QAEKELETWRQKANEAL------RLRLQAEEEAQKK------------SKTQEEAERQKVEA-ERDAK--KRAKAEDAAL 1732
Cdd:pfam01576 570 KLEKTKNRLQQELDDLLvdldhqRQLVSNLEKKQKKfdqmlaeekaisARYAEERDRAEAEArEKETRalSLARALEEAL 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1733 KQKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEM 1812
Cdd:pfam01576 650 EAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQF 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1813 DSLLKMKTEAekktmsNTEKSKQLLesealkmKQLADEATRLrsvaEEAKKQRQTAeeEAARQRAEAEkiLKEKLAAINE 1892
Cdd:pfam01576 730 ERDLQARDEQ------GEEKRRQLV-------KQVRELEAEL----EDERKQRAQA--VAAKKKLELD--LKELEAQIDA 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1893 ATRLRTEAEIALKakeaenerlKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSS-DSEMVRQKTIVEETLRQKKIV 1971
Cdd:pfam01576 789 ANKGREEAVKQLK---------KLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNlEAELLQLQEDLAASERARRQA 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1972 EEEIHIIRINFEKASKGKSDLENELKKLKV----IAEETQKSKLKAEAEAEKLKKLAaeEEKKRKESEEKVKRITAAEEE 2047
Cdd:pfam01576 860 QQERDELADEIASGASGKSALQDEKRRLEAriaqLEEELEEEQSNTELLNDRLRKST--LQVEQLTTELAAERSTSQKSE 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2048 AARQCKAAQEEVARLEKKADEANKQKEKAEKeaekqvIVAKEA--AQKCSSAEQKAQEVLSKNKEDSLAQQKMKE---EF 2122
Cdd:pfam01576 938 SARQQLERQNKELKAKLQEMEGTVKSKFKSS------IAALEAkiAQLEEQLEQESRERQAANKLVRRTEKKLKEvllQV 1011
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2123 ENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAeeeAAKQAKAQKDAEKLKKAAE 2182
Cdd:pfam01576 1012 EDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRA---NAARRKLQRELDDATESNE 1068
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1831-2665 |
1.87e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 77.52 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1831 EKSKQLLESEALKMKQLADEATRlrSVAEEAKKQRQTAEEEAarqraeaekILKEKLAAINEATRLRTEAEIALKAKEAE 1910
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAES--ELKELEKKHQQLCEEKN---------ALQEQLQAETELCAEAEEMRARLAARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1911 NERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSSDSE-MVRQKTIVEETLRQKKI--VEEEIHIIRINFEKASK 1987
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEeAARQKLQLEKVTTEAKIkkLEEDILLLEDQNSKLSK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1988 GKSDLENELKKLKV-IAEETQKSK----LKAEAEA------EKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQ 2056
Cdd:pfam01576 153 ERKLLEERISEFTSnLAEEEEKAKslskLKNKHEAmisdleERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2057 EEVARLEKKADEANKQKEKaekeaekqviVAKEAAQKcSSAEQKAQEVLSKNKEdslaqqkMKEEFENAkrlaqaaekak 2136
Cdd:pfam01576 233 ELRAQLAKKEEELQAALAR----------LEEETAQK-NNALKKIRELEAQISE-------LQEDLESE----------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2137 ekaekeaallRQKAAEAEKQKKSAEEE---------------AAKQ---AKAQKDAEKLKKAAEEEASKRAAAEAEALKQ 2198
Cdd:pfam01576 284 ----------RAARNKAEKQRRDLGEElealkteledtldttAAQQelrSKREQEVTELKKALEEETRSHEAQLQEMRQK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2199 KKQADAEMAKhkkEADQALKLKSQVEK--------------ELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQ 2264
Cdd:pfam01576 354 HTQALEELTE---QLEQAKRNKANLEKakqalesenaelqaELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2265 VEDELAKVRIQMDELLKLKLKIEEQNRSLMKK------DKDKTQKVLAEEAGKMKSLAEEAARLsvEAEETARQRQIAES 2338
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKNIKLSKDvsslesQLQDTQELLQEETRQKLNLSTRLRQL--EDERNSLQEQLEEE 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2339 nlAEQRALAEKMLKEKMQAIQEatkLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKsLEAERKRqleVS 2418
Cdd:pfam01576 509 --EEAKRNVERQLSTLQAQLSD---MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDK-LEKTKNR---LQ 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2419 AEAETLRLKVKELSDAQSKAENEAKKFKKQADEAK---ARLKDtEKQSTETVVQKLETQRLQSTREADGLKEAIADLEKE 2495
Cdd:pfam01576 580 QELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKaisARYAE-ERDRAEAEAREKETRALSLARALEEALEAKEELERT 658
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2496 REKLKKEAEELQN-------------KSNKMANTQKEEIEQQKAIIQKSFIS-------------------ERElLLKRQ 2543
Cdd:pfam01576 659 NKQLRAEMEDLVSskddvgknvheleRSKRALEQQVEEMKTQLEELEDELQAtedaklrlevnmqalkaqfERD-LQARD 737
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2544 KAVEDEKKKLQKQfedeVKKAEALKDEQERQR-------KLMEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEME----V 2612
Cdd:pfam01576 738 EQGEEKRRQLVKQ----VRELEAELEDERKQRaqavaakKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKdlqrE 813
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 2613 LEKKRLDQEKQLgAENQKLREKLQCLEGASKQS----ATKQVASKTIEVQTDVVSEE 2665
Cdd:pfam01576 814 LEEARASRDEIL-AQSKESEKKLKNLEAELLQLqedlAASERARRQAQQERDELADE 869
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1496-1888 |
2.01e-13 |
|
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: 76.98 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1496 TKIEEEIHTIRIQLEMTIKQ-KKTAESELQQLRDKAaEAEKLRKAAQE-DA--ERLRKQVAEETQKKKNAEdelKRKSEA 1571
Cdd:NF033838 76 KSLDKRKHTQNVALNKKLSDiKTEYLYELNVLKEKS-EAELTSKTKKElDAafEQFKKDTLEPGKKVAEAT---KKVEEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1572 EKEAAKQKQKALDD-----LQKFKMQAEEAERRMKQAEEEKLRQikvveevaqksaatqlqshsmsfNVKASKLEESLKK 1646
Cdd:NF033838 152 EKKAKDQKEEDRRNyptntYKTLELEIAESDVEVKKAELELVKE-----------------------EAKEPRDEEKIKQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1647 EQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALrlrlqAEEEAQKKSKTQEEAERQKVEAERDAKKR-A 1725
Cdd:NF033838 209 AKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKN-----VATSEQDKPKRRAKRGVLGEPATPDKKENdA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1726 KAEDAALKQKDNAEKELEKQRTFAEqvAQQKLSAEQEcirlKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEEL 1805
Cdd:NF033838 284 KSSDSSVGEETLPSPSLKPEKKVAE--AEKKVEEAKK----KAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELEL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1806 AKvrsemdsllkmkteAEKKTMSNTEKSKQLLESEALKMKqladEATRLrsvaEEAKKQRQTAEEEAARQRAEAEKIlKE 1885
Cdd:NF033838 358 VK--------------EEAKEPRNEEKIKQAKAKVESKKA----EATRL----EKIKTDRKKAEEEAKRKAAEEDKV-KE 414
|
...
gi 736215636 1886 KLA 1888
Cdd:NF033838 415 KPA 417
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3772-3810 |
2.22e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.58 E-value: 2.22e-13
10 20 30
....*....|....*....|....*....|....*....
gi 736215636 3772 LLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPELHDKL 3810
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1072-1923 |
2.77e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 77.03 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1072 AEQMKVQSELEGLKKDLNSITEQTEEVlasQQQISSAPMLRSELDVTLRKMDhvyglSSIYLDKLKTIDVVIRNTKEAEA 1151
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISEL---EKRLEEIEQLLEELNKKIKDLG-----EEEQLRVKEKIGELEAEIASLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1152 ALKTYESRLLDV-NKVPENEKEVEEQRSQLKSMRAEVEADQVIFDRLQDELrrastindkmtrihSERDAEMEHYRQLVS 1230
Cdd:TIGR02169 309 SIAEKERELEDAeERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY--------------AELKEELEDLRAELE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1231 SLLERWQVVFAQMDMRQRELDLLGRHMNSYNVSYEWLIHWLGEARKRQEKIQAvpigGSKALREQLAEEKKLLEEIEknk 1310
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA----AIAGIEAKINELEEEKEDKA--- 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1311 DKIDSCQKNAKAYIDSVKDYELQILTYKALQDPMASPLKKPKMDC----ASDNIIQEYVTLRTRYSELMT--------LT 1378
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELaeaeAQARASEERVRGGRAVEEVLKasiqgvhgTV 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1379 SQYIKFITETQRRLEDDEKASEKLKEEERKKMAEIQAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVD 1458
Cdd:TIGR02169 528 AQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1459 AEQQKQNIQHELHHLKSLSEQEIKSKSQQLEHALVShtkIEEEIhtiriqLE----MT---------IKQKKTAESELQQ 1525
Cdd:TIGR02169 608 FDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRMVT---LEGEL------FEksgaMTggsraprggILFSRSEPAELQR 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1526 LRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSeaekeaaKQKQKALDDLQKFKMQAEEAERRMKQAEE 1605
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE-------KEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1606 EKLRQIKVVEEVAQKSAATQLQSHsmsfnvkasKLEESLKKEQGTVlqLQEEAEQLRKQQEEANKAREQAEKELETWRQK 1685
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLH---------KLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1686 ANEALRLRLQAEEEAQKKSKTQEEAERQKVEAER---DAKKRAKAEDAALKQKDNAEKELEKQRtfaeqvaqqklsaeqe 1762
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKeieNLNGKKEELEEELEELEAALRDLESRL---------------- 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1763 cIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEkktmsntEKSKQLLESEAL 1842
Cdd:TIGR02169 885 -GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-------EIPEEELSLEDV 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1843 KMKQLADEAtRLRSVAEEAKKQRQTAEEEAARQRAEAEKilKEKLAAINEATRLRTEaeialkakeaENERLKRKAEDEA 1922
Cdd:TIGR02169 957 QAELQRVEE-EIRALEPVNMLAIQEYEEVLKRLDELKEK--RAKLEEERKAILERIE----------EYEKKKREVFMEA 1023
|
.
gi 736215636 1923 Y 1923
Cdd:TIGR02169 1024 F 1024
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
75-154 |
3.34e-13 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 68.77 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 75 HITDLYEDLRDGHNLISLLEVLSGETLPREKGRM----RFHKLQNVQIALDFLKHRQV----KLVNIRNDDIADGNPKLT 146
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 736215636 147 LGLIWTII 154
Cdd:cd21223 105 LALLWRII 112
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1506-1777 |
3.65e-13 |
|
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: 74.11 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1506 RIQLEMTiKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEEtQKKKNAEDELKRKSEAEKEAAKQKQKALDD 1585
Cdd:TIGR02794 54 RIQQQKK-PAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAE-KAAKQAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1586 lqkfKMQAEEAERRMKQAEEeklrqikvveevAQKSAAtqlqshsmsfnvkasklEESLKKEQgtvLQLQEEAEQLRKQQ 1665
Cdd:TIGR02794 132 ----AKAKAEAEAERKAKEE------------AAKQAE-----------------EEAKAKAA---AEAKKKAEEAKKKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1666 EEANKAREQAEKeletwRQKANEAlrlrlqAEEEAQKKSKTQEEAERqKVEAERDAKKRAKAEDAALKQKDNAEKELEKQ 1745
Cdd:TIGR02794 176 EAEAKAKAEAEA-----KAKAEEA------KAKAEAAKAKAAAEAAA-KAEAEAAAAAAAEAERKADEAELGDIFGLASG 243
|
250 260 270
....*....|....*....|....*....|..
gi 736215636 1746 RTFAEQVAQQKLSAEQECIRLKADFDHAEQQR 1777
Cdd:TIGR02794 244 SNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
172-272 |
4.02e-13 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 68.95 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAErDLGVTRLLDP 251
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 736215636 252 ED-VDVLHPDEKSIITYVSSLY 272
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1387-1668 |
4.17e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 75.93 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1387 ETQRRLEDDEKASeklkeeerkkmaeiQAELDKQKQIAEAQAKSVIKAEQEAQELKL---KMKEEASKRQDVAVDAEQQK 1463
Cdd:pfam17380 313 ERRRKLEEAEKAR--------------QAEMDRQAAIYAEQERMAMERERELERIRQeerKRELERIRQEEIAMEISRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1464 qniqhELHHLKSLSEQEIKSKSQQLEHAlvSHTKIEEEIHTIRIQLEMT------IKQKKTAESELQQLRD-KAAEAEKL 1536
Cdd:pfam17380 379 -----ELERLQMERQQKNERVRQELEAA--RKVKILEEERQRKIQQQKVemeqirAEQEEARQREVRRLEEeRAREMERV 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1537 RKAAQE-----------DAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEE 1605
Cdd:pfam17380 452 RLEEQErqqqverlrqqEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYE 531
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736215636 1606 EKLRQIKVVEEVAQKSAAT--QLQSHSMSFNVKASKLeESLKKEQGTVLQLQeEAEQLRKQQEEA 1668
Cdd:pfam17380 532 EERRREAEEERRKQQEMEErrRIQEQMRKATEERSRL-EAMEREREMMRQIV-ESEKARAEYEAT 594
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1412-2021 |
4.22e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 76.31 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1412 EIQAELDKQKQIAEAQA----KSVIKAEQEAQELKLK---MKEEASKRQDVAVDAEQQKQNIQHELHHLKSLSEQEIKSK 1484
Cdd:pfam15921 89 DLQRRLNESNELHEKQKfylrQSVIDLQTKLQEMQMErdaMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1485 SQQLEH---ALVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQL--RDKAAEAEKLRKAAQEDAERLRKQVAEetqkkk 1559
Cdd:pfam15921 169 NTQIEQlrkMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILRELDTEISYLKGRIFP------ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1560 nAEDELKR-KSEAEkeaakqkqkalddlQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQ--KSAATQLQSHsMSFNVK 1636
Cdd:pfam15921 243 -VEDQLEAlKSESQ--------------NKIELLLQQHQDRIEQLISEHEVEITGLTEKASsaRSQANSIQSQ-LEIIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1637 ASKLEESLKKEQgtVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEAL-RLRLQAEEEAQKKSKTQEEAER--- 1712
Cdd:pfam15921 307 QARNQNSMYMRQ--LSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELtEARTERDQFSQESGNLDDQLQKlla 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1713 ------QKVEAERDAKKRAKAEDAALK-QKDNAEKELEKQRTFAEQVAQQKLSAEQECIrlkadfDHAEQQRGLLDNELQ 1785
Cdd:pfam15921 385 dlhkreKELSLEKEQNKRLWDRDTGNSiTIDHLRRELDDRNMEVQRLEALLKAMKSECQ------GQMERQMAAIQGKNE 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1786 RLKKeVSATEKQRKLLEEELAKVRSEMDSlLKMKTEAEKKTMSNTEKSkqlLESEALKMKQLADEATRLRSVA------- 1858
Cdd:pfam15921 459 SLEK-VSSLTAQLESTKEMLRKVVEELTA-KKMTLESSERTVSDLTAS---LQEKERAIEATNAEITKLRSRVdlklqel 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1859 -----EEAKKQRQTAEEEAAR-QRAEAEKILKEKLAAINEATRL-----RTEAEIALKAKEAENERLKRKAEDEAYqrKL 1927
Cdd:pfam15921 534 qhlknEGDHLRNVQTECEALKlQMAEKDKVIEILRQQIENMTQLvgqhgRTAGAMQVEKAQLEKEINDRRLELQEF--KI 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1928 LEDQAAQHKHDIQEKIihlkSSSDSEMVRQKTIVEETLRQKKIVEEEIHIIrinFEKASKGKSDLENELKKLKVIAEETQ 2007
Cdd:pfam15921 612 LKDKKDAKIRELEARV----SDLELEKVKLVNAGSERLRAVKDIKQERDQL---LNEVKTSRNELNSLSEDYEVLKRNFR 684
|
650
....*....|....
gi 736215636 2008 KSKLKAEAEAEKLK 2021
Cdd:pfam15921 685 NKSEEMETTTNKLK 698
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
59-160 |
4.40e-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: 68.42 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 59 KTFTKWVNKhlMKSQRHITDLYEDLRDGHNLISLLEVL-------SGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLV 131
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 736215636 132 NIRNDDIADGNPKLTLGLIWTIILHFQIS 160
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
50-156 |
6.26e-13 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 68.08 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 50 ADERDrvqKKTFTKWVNKHLMKSQrhITDLYEDLRDGhnlISLLEVL--------SGETLPREKGRMRFHKLQNVQIALD 121
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVLdkiqpgcvNWKKVNKPKPLNKFKKVENCNYAVD 72
|
90 100 110
....*....|....*....|....*....|....*
gi 736215636 122 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 156
Cdd:cd21219 73 LAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2117-2627 |
7.56e-13 |
|
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: 75.14 E-value: 7.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2117 KMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSaeeeaakqakaqkdaekLKKAAEEEASKraaaeAEAL 2196
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKD-----------------LTFLLEESRDK-----ANQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2197 KQKKQADAEMAKhkkeadQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVR--- 2273
Cdd:pfam05483 274 EEKTKLQDENLK------ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKaah 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2274 -IQMDELLKLKLKIEEQNRSlmkkdkdkTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRAL---AEK 2349
Cdd:pfam05483 348 sFVVTEFEATTCSLEELLRT--------EQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIlaeDEK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2350 MLKEKMQAIQEATKLKAEAQELQKQKdQAQEKAKKLLEDKQQI----QQRLDKETEGFQKSLEAERKRQLEVSAEAETLR 2425
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLL-QAREKEIHDLEIQLTAiktsEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2426 LKVKELSDAQSKAENEAKKF-------KKQADEAKARLKDTEKQST------ETVVQKLETQRLQSTREADGLKEAIADL 2492
Cdd:pfam05483 499 LENKELTQEASDMTLELKKHqediincKKQEERMLKQIENLEEKEMnlrdelESVREEFIQKGDEVKCKLDKSEENARSI 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2493 EKEREKLKKEAEELQNKSNKM------ANTQKEEIEQQKAIIQKSFISERelllKRQKAVEDEKKKLQKQFEDEVKKAEA 2566
Cdd:pfam05483 579 EYEVLKKEKQMKILENKCNNLkkqienKNKNIEELHQENKALKKKGSAEN----KQLNAYEIKVNKLELELASAKQKFEE 654
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 2567 LKDEQERQ---RKLMEE----EKKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEKKRLDQEKQLGAE 2627
Cdd:pfam05483 655 IIDNYQKEiedKKISEEklleEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEE 722
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1147-1890 |
7.98e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 7.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1147 KEAEAALKTYESRLLDVNKVPENEKEVEEQRSQLKSMRAEVEADQVIFDRLQDELRRASTINDKMTRIHSERDAEMEHYR 1226
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1227 QLVSSLLERWQvvfAQMDMRQRELDLLGRHMNSYNVSYEWLIHWLGEARKRQEKIQAvpigGSKALREQLAEEKKLLEEI 1306
Cdd:TIGR02168 319 EELEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES----RLEELEEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1307 EKNKDKIDSCQKNAKAYIDSVKDYELQILTYKALQDPMASPLKKPKMDCASDNIIQEYVTLRTRYSELMT---LTSQYIK 1383
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEaleELREELE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1384 FITETQRRLEDDEKASEKLKEEERKKMAEIQAELDKQKQIAEAQAK---------SVIKAEQE---AQELKLkmkeeASK 1451
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGyeaAIEAAL-----GGR 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1452 RQDVAV-DAEQQKQNIQhelhHLKslseQEIKSKSQQLEHALVSHTKIEEEihtiriqlemTIKQKKTAESELQQLRDKA 1530
Cdd:TIGR02168 547 LQAVVVeNLNAAKKAIA----FLK----QNELGRVTFLPLDSIKGTEIQGN----------DREILKNIEGFLGVAKDLV 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1531 AEAEKLRKAAQ------------EDAERLRKQVAEE---------------------------TQKKKNAEDELKRKSEA 1571
Cdd:TIGR02168 609 KFDPKLRKALSyllggvlvvddlDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1572 EKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIkvveevaqksaatqlqshsmsfnvkaSKLEESLKKEQGTV 1651
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI--------------------------SALRKDLARLEAEV 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1652 LQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQkKSKTQEEAERQKVEAERDAKKRAKAEDAA 1731
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE-QLKEELKALREALDELRAELTLLNEEAAN 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1732 LKQK-DNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRS 1810
Cdd:TIGR02168 822 LRERlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1811 EMDSLLKMKTEAEKKTMSNTEKSKQL-LESEALKMkQLADEATRLRS----VAEEAKKQRQTAEEEAARQRAEAEKiLKE 1885
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLeLRLEGLEV-RIDNLQERLSEeyslTLEEAEALENKIEDDEEEARRRLKR-LEN 979
|
....*
gi 736215636 1886 KLAAI 1890
Cdd:TIGR02168 980 KIKEL 984
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2097-2491 |
1.41e-12 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 74.26 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2097 AEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEK 2176
Cdd:COG5281 24 AAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADALAAALAEDAAAAAAAAEAALAALA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2177 LKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKELTMVKL-RLDETDKQKALLDEELQRVKGEV 2255
Cdd:COG5281 104 AAALALAAAALAEAALAAAAAAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAALaAAAAAAAAAAAAAAAAAALAAAS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2256 NDAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQI 2335
Cdd:COG5281 184 AAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAASAAAQALAALAAAAAAAALALAA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2336 AE-SNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQ 2414
Cdd:COG5281 264 AAeLALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAAAQALRAAAQALAALAQRALAAAA 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 2415 LEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTETVVQKLETQRLQSTREADGLKEAIAD 2491
Cdd:COG5281 344 LAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWAAGAKAALAEYADSATNVAAQVAQAATSAFSGLTDALAG 420
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1528-1745 |
1.58e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.87 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1528 DKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEK 1607
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1608 LRQIKVVEEVAQKSAATQLQShSMSFNVKASKLEESLKKE---QGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQ 1684
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQP-PLALLLSPEDFLDAVRRLqylKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736215636 1685 kanealrlrLQAEEEAQKKSKTQEEAERQKVEAErdAKKRAKAEDAALKQKDNAEKELEKQ 1745
Cdd:COG4942 179 ---------LLAELEEERAALEALKAERQKLLAR--LEKELAELAAELAELQQEAEELEAL 228
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2302-2621 |
1.88e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 74.00 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2302 QKVLAEEAGKMKSLAEEAARLSVEAEETARQ----RQIAESNLAEQRALaekmlkEKMQAIQeatklkAEAQELQKQKDQ 2377
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREverrRKLEEAEKARQAEM------DRQAAIY------AEQERMAMERER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2378 AQEKAKklLEDKQQIQQRLDKEtegfQKSLEAERKRQLE-VSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARL 2456
Cdd:pfam17380 349 ELERIR--QEERKRELERIRQE----EIAMEISRMRELErLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2457 KDTEKQSTETvvQKLETQRLQSTREADgLKEAIADLEKEREKLKKEAEELQNKSNKMANTQKEEIEQQKAIIQKSFISER 2536
Cdd:pfam17380 423 EQIRAEQEEA--RQREVRRLEEERARE-MERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2537 ELLLKRQKAVEDEKKK--LQKQFEDEVK----KAEALKDEQERQRKLMEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEM 2610
Cdd:pfam17380 500 ELEERKQAMIEEERKRklLEKEMEERQKaiyeEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMR 579
|
330
....*....|.
gi 736215636 2611 EVLEKKRLDQE 2621
Cdd:pfam17380 580 QIVESEKARAE 590
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1429-2257 |
2.09e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 73.99 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1429 KSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNI---------QHELHHLKSLSEQEIKSkSQQLEHALVSHTKIE 1499
Cdd:pfam05483 9 KSFNKCTEDDFEFPFAKSNLSKNGENIDSDPAFQKLNFlpmleqvanSGDCHYQEGLKDSDFEN-SEGLSRLYSKLYKEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1500 EEIHTIRIQLEMTIKQKktaESELQQLRdKAAEAEklRKAAQE---DAERLRKQVAEETQKKKNAEDELKRKSEAEKEAA 1576
Cdd:pfam05483 88 EKIKKWKVSIEAELKQK---ENKLQENR-KIIEAQ--RKAIQElqfENEKVSLKLEEEIQENKDLIKENNATRHLCNLLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1577 KQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQSHsmsFNVKA-----SKLEESLKKEqgtV 1651
Cdd:pfam05483 162 ETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMH---FKLKEdhekiQHLEEEYKKE---I 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1652 LQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANE-ALRLRLQAE---EEAQKKSKTQEEAERQKVEAERD-AKKRAK 1726
Cdd:pfam05483 236 NDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQlEEKTKLQDEnlkELIEKKDHLTKELEDIKMSLQRSmSTQKAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1727 AEDAALKQKDNAEKELEKQrTFAEQVAQQKLSAEQECIRLKADFDHAEQqrgLLDNELQRLKKevsaTEKQRKLLEEELA 1806
Cdd:pfam05483 316 EEDLQIATKTICQLTEEKE-AQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEK----NEDQLKIITMELQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1807 KVRSEMDSLLKMKT--EAEKKTMSNTEKSKQLLESEALKMKQLADEatrLRSVAEEAKKQRQTAEEEAARQRAEAEKILK 1884
Cdd:pfam05483 388 KKSSELEEMTKFKNnkEVELEELKKILAEDEKLLDEKKQFEKIAEE---LKGKEQELIFLLQAREKEIHDLEIQLTAIKT 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1885 EKLAAINEATRLRTEAEialkakeaeNERLKRKAEDEAYQRKLLEDQaaqhkhdiqeKIIHLKSSSDSEMVRQKtivEET 1964
Cdd:pfam05483 465 SEEHYLKEVEDLKTELE---------KEKLKNIELTAHCDKLLLENK----------ELTQEASDMTLELKKHQ---EDI 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1965 LRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKVIAEETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAA 2044
Cdd:pfam05483 523 INCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2045 EEEAARQCKAAQEEVARLEKKADEANKQKEKAEkeaekqvIVAKEAAQKCSSAEQKAQEVLSKNKED----SLAQQKMKE 2120
Cdd:pfam05483 603 IENKNKNIEELHQENKALKKKGSAENKQLNAYE-------IKVNKLELELASAKQKFEEIIDNYQKEiedkKISEEKLLE 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2121 EFENAKRLAQAAEKAkekaekeaallrQKAAEAEKQKKSAEEEAAkqakAQKDAEKLKKAAEEEaskraaaeaealkqkk 2200
Cdd:pfam05483 676 EVEKAKAIADEAVKL------------QKEIDKRCQHKIAEMVAL----MEKHKHQYDKIIEER---------------- 723
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 2201 qaDAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVND 2257
Cdd:pfam05483 724 --DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1523-1743 |
2.18e-12 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 72.53 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1523 LQQLRDKAAEAEKLR-KAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDlQKfkmQAEEAERrmK 1601
Cdd:PRK09510 67 QQQQQKSAKRAEEQRkKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALK-QK---QAEEAAA--K 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1602 QAEEEKLRQikvveEVAQKSAATQlqshsmsfnvkASKLEESLKKeqgtvlqlQEEAEQLRKQQEEANKAREQAEKELET 1681
Cdd:PRK09510 141 AAAAAKAKA-----EAEAKRAAAA-----------AKKAAAEAKK--------KAEAEAAKKAAAEAKKKAEAEAAAKAA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736215636 1682 WRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELE 1743
Cdd:PRK09510 197 AEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2120-2632 |
2.18e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2120 EEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKaqkdaeKLKKAAEEEASKRAaaEAEALKQK 2199
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLR------EINEISSELPELRE--ELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2200 KQadaEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDaVKQKAQVEDELAKVRIQMDEL 2279
Cdd:PRK03918 230 VK---ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE-LKELKEKAEEYIKLSEFYEEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2280 LKLKLKIE-------EQNRSLMKKDKDKTQKVlaEEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALaekmlk 2352
Cdd:PRK03918 306 LDELREIEkrlsrleEEINGIEERIKELEEKE--ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERL------ 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2353 EKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERK-----RQLEVSAEAETLRLK 2427
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2428 VKELSDAqskaENEAKKFKKQADEAKARLKDTEKQstetvvqKLETQRLQSTRE-ADGLKEAIADLEKEREKLKKEAEEL 2506
Cdd:PRK03918 458 TAELKRI----EKELKEIEEKERKLRKELRELEKV-------LKKESELIKLKElAEQLKELEEKLKKYNLEELEKKAEE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2507 QNKSNKMANTQKEEIEQQKAIIQK--SFISERELLLKRQKAVEDEKKKLQKQFE-------DEVKKA------------E 2565
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKleELKKKLAELEKKLDELEEELAELLKELEelgfesvEELEERlkelepfyneylE 606
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 2566 ALKDEQERQRKlmEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEKKrLDQEKQLGAENQKLR 2632
Cdd:PRK03918 607 LKDAEKELERE--EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK-YSEEEYEELREEYLE 670
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3439-3477 |
2.27e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.89 E-value: 2.27e-12
10 20 30
....*....|....*....|....*....|....*....
gi 736215636 3439 LLEAQAGTGFITDPVKNQKYSVDDAVKVGVVGPELHEKL 3477
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
172-272 |
2.32e-12 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 66.59 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAErDLGVTRLLDP 251
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 736215636 252 ED-VDVLHPDEKSIITYVSSLY 272
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1712-2431 |
2.61e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 73.85 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1712 RQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAEQECIRlkadfdHAEQQRGLLDNELQRLKKEV 1791
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLR------EALQQTQQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1792 SATEKQRKLLEEELAKVRsEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALkmkqladeatrlrsvaEEAKKQRQTAEEE 1871
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIE-ELRAQEAVLEETQERINRARKAAPLAAHIKAV----------------TQIEQQAQRIHTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1872 AARQRAEAEKILKEKLAAINEATRLRtEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAA--QHKHDIQEKIIHLKSS 1949
Cdd:TIGR00618 316 LQSKMRSRAKLLMKRAAHVKQQSSIE-EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltQHIHTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1950 S-------DSEMVRQKTIVEETLRQKKIVEEEIHI---IRINFEKASKGKSDLENELKKLKVIAEETQKSKLKAEAEAEK 2019
Cdd:TIGR00618 395 LqslckelDILQREQATIDTRTSAFRDLQGQLAHAkkqQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2020 LKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKA----AQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEA---AQ 2092
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGScihpNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHqltSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2093 KCSSAEQKAQEVLSKNKEDSLAQ--QKMKEEFENakrLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKA 2170
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQcdNRSKEDIPN---LQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2171 QKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQR 2250
Cdd:TIGR00618 632 LHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELET 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2251 VKGEVNDAVKQKAQVEDEL-AKVRIQMDELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEaARLSVEAEET 2329
Cdd:TIGR00618 712 HIEEYDREFNEIENASSSLgSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAEL-SHLAAEIQFF 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2330 ARQRQIAESNLAEQRALAEKMLKEKMQA--------IQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETE 2401
Cdd:TIGR00618 791 NRLREEDTHLLKTLEAEIGQEIPSDEDIlnlqcetlVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
730 740 750
....*....|....*....|....*....|
gi 736215636 2402 GFQKSLEAERKRQLEVSAEAETLRLKVKEL 2431
Cdd:TIGR00618 871 IIQLSDKLNGINQIKIQFDGDALIKFLHEI 900
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2185-2426 |
2.78e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.10 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2185 ASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQ 2264
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2265 VEDELAKVRIQMDELLKLKLKIEEQNRS---LMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQiaesNLA 2341
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA----ELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2342 EQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEA 2421
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 736215636 2422 ETLRL 2426
Cdd:COG4942 251 LKGKL 255
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1411-2025 |
2.98e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.56 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1411 AEIQAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQdvavdaeQQKQNIQHELHHLKSLSEQEIKSKSQQLEH 1490
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-------LRVKEKIGELEAEIASLERSIAEKERELED 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1491 ALVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSE 1570
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1571 AEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQK-SAATQlqshsmsfnvKASKLEESLKKEQG 1649
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEiKKQEW----------KLEQLAADLSKYEQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1650 TVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRL-----------------QAEEEAQKKSKTQEEAER 1712
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEvlkasiqgvhgtvaqlgSVGERYATAIEVAAGNRL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1713 QK--VEAERDAK------KRAKAEDAA---LKQKDNAEKELEKQRT-----FAEQVA---QQKLSAEQECIRLKADFDHA 1773
Cdd:TIGR02169 550 NNvvVEDDAVAKeaiellKRRKAGRATflpLNKMRDERRDLSILSEdgvigFAVDLVefdPKYEPAFKYVFGDTLVVEDI 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1774 EQQRGLLDN------------------------------------ELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLK 1817
Cdd:TIGR02169 630 EAARRLMGKyrmvtlegelfeksgamtggsraprggilfsrsepaELQRLRERLEGLKRELSSLQSELRRIENRLDELSQ 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1818 MKTEAEKKTmSNTEKSKQLLESEALKMKQ-LADEATRLRSVAEE---AKKQRQTAEEEAARQRAEAEKiLKEKLAAInEA 1893
Cdd:TIGR02169 710 ELSDASRKI-GEIEKEIEQLEQEEEKLKErLEELEEDLSSLEQEienVKSELKELEARIEELEEDLHK-LEEALNDL-EA 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1894 TRLRTEAEI------ALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSSDSemvRQKTIvEETLRQ 1967
Cdd:TIGR02169 787 RLSHSRIPEiqaelsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS---IEKEI-ENLNGK 862
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 1968 KKIVEEEIHIIRINFEKASKGKSDLENELKKLKVIAEETQKSKLKAEAEAEKLKKLAA 2025
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1439-1998 |
3.31e-12 |
|
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: 72.75 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1439 QELKlKMKEEASKRQDVAVDAEQQKQNIQHELHHLKSLSEqeiksksqQLEHALvshTKIEEEihtiriqlEMTIKQkkt 1518
Cdd:pfam05701 42 LELE-KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIE--------ELKLNL---ERAQTE--------EAQAKQ--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1519 aESELQQLRDKAAE---AEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSE------AEKEAAKQKqkalddlqkf 1589
Cdd:pfam05701 99 -DSELAKLRVEEMEqgiADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKeyaslvSERDIAIKR---------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1590 kmqAEEAERRMKQAEeeklrqiKVVEEVAQKSAATQ--LQS-HSMSFNVKASKLEESLKKEQGTvLQLQEEAEQLrkqQE 1666
Cdd:pfam05701 168 ---AEEAVSASKEIE-------KTVEELTIELIATKesLESaHAAHLEAEEHRIGAALAREQDK-LNWEKELKQA---EE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1667 EANKAREQ--AEKELETwRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEaerdaKKRAKAEDAALkqkDNAEKELEK 1744
Cdd:pfam05701 234 ELQRLNQQllSAKDLKS-KLETASALLLDLKAELAAYMESKLKEEADGEGNE-----KKTSTSIQAAL---ASAKKELEE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1745 QRTFAEqvaqqKLSAEQECIRLKAdfdhaeqqrGLLDNELQRLKKEVSATEKQRKL-------LEEELAKVRSEMdSLLK 1817
Cdd:pfam05701 305 VKANIE-----KAKDEVNCLRVAA---------ASLRSELEKEKAELASLRQREGMasiavssLEAELNRTKSEI-ALVQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1818 MKTEAEKKTMSNTEKskqllesealKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLR 1897
Cdd:pfam05701 370 AKEKEAREKMVELPK----------QLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1898 TEAEIALKAKEA--ENERLKRKAEDEAYQRKL---------LEDQAAQHKHDIQEKII----HLKSSSDSEmVRQKTIVE 1962
Cdd:pfam05701 440 ASEKLALAAIKAlqESESSAESTNQEDSPRGVtlsleeyyeLSKRAHEAEELANKRVAeavsQIEEAKESE-LRSLEKLE 518
|
570 580 590
....*....|....*....|....*....|....*.
gi 736215636 1963 ETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKK 1998
Cdd:pfam05701 519 EVNREMEERKEALKIALEKAEKAKEGKLAAEQELRK 554
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1348-1943 |
4.49e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1348 LKKPKMDCASDNIIQEYVTLRTRYSELMTLTSQ----------YIKFITETQRRLEDDEKASEKLKEEERKKMAEIQAEL 1417
Cdd:COG4913 218 LEEPDTFEAADALVEHFDDLERAHEALEDAREQiellepirelAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1418 DK-QKQIAEAQAKsviKAEQEAQELKLKMKEEASKRQDVAVDAeQQKQNIQHELHHLKSlSEQEIKSKSQQLEHAL---- 1492
Cdd:COG4913 298 EElRAELARLEAE---LERLEARLDALREELDELEAQIRGNGG-DRLEQLEREIERLER-ELEERERRRARLEALLaalg 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1493 VSHTKIEEEIHTIRIQLEMtikQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAE 1572
Cdd:COG4913 373 LPLPASAEEFAALRAEAAA---LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1573 KEAAKQKQKALD---DLqkfkMQAEEAERRMKQAEEEKLRQIK---VVEEVAQKSAATQLQSHSMSFNVKASKLEESLKK 1646
Cdd:COG4913 450 AEALGLDEAELPfvgEL----IEVRPEEERWRGAIERVLGGFAltlLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1647 EQGTVLQ------------------LQEE------------AEQLRKQQeeanKA----------REQAEKELETWRQKA 1686
Cdd:COG4913 526 PERPRLDpdslagkldfkphpfrawLEAElgrrfdyvcvdsPEELRRHP----RAitragqvkgnGTRHEKDDRRRIRSR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1687 ------NEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAE 1760
Cdd:COG4913 602 yvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1761 QEcirlKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEkktmsntEKSKQLLESE 1840
Cdd:COG4913 682 AS----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE-------DLARLELRAL 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1841 ALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKE--------------KLAAINEATRLRTE-AEIALK 1905
Cdd:COG4913 751 LEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldaDLESLPEYLALLDRlEEDGLP 830
|
650 660 670
....*....|....*....|....*....|....*...
gi 736215636 1906 AKEAENERLKRKAEDEayQRKLLEDQAAQHKHDIQEKI 1943
Cdd:COG4913 831 EYEERFKELLNENSIE--FVADLLSKLRRAIREIKERI 866
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1960-2555 |
4.52e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1960 IVEETLRQKKIVEEEIHIIRinFEKASKGKSDLENELKKL-----KVIAEETQKSKLKAEAEAEKLKKLAAEEEKKRKES 2034
Cdd:PRK03918 140 ILESDESREKVVRQILGLDD--YENAYKNLGEVIKEIKRRierleKFIKRTENIEELIKEKEKELEEVLREINEISSELP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2035 EEKVKRitAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEvLSKNKEDSLA 2114
Cdd:PRK03918 218 ELREEL--EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE-LKELKEKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2115 QQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEE-EASKRAAAEA 2193
Cdd:PRK03918 295 YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2194 EALKqKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDE----- 2268
Cdd:PRK03918 375 ERLK-KRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkel 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2269 LAKVRIQMDELLKLKLKIEEQNRSLmKKDKDKTQKVLAEEAG--KMKSLAEEAARLSVEAEETARQRqiAESNLAEQRAL 2346
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKL-RKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEE--LEKKAEEYEKL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2347 AEKMLKEKMQ------AIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAE 2420
Cdd:PRK03918 531 KEKLIKLKGEikslkkELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2421 AETLRLKVKELSDAQS---KAENEAKKFKKQADEAKARLKDTEKQSTETVVQKLETQRLQSTREADGLKEAIADLEKERE 2497
Cdd:PRK03918 611 EKELEREEKELKKLEEeldKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 2498 KLKKEAEELQNksnkmantQKEEIEQQKaiiqksfiSERELLLKRQKAVEDEKKKLQK 2555
Cdd:PRK03918 691 EIKKTLEKLKE--------ELEEREKAK--------KELEKLEKALERVEELREKVKK 732
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1424-1878 |
4.92e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.77 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1424 AEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQhELhhlkslsEQEIKSKSQQLEHALVSHTKIEEEIH 1503
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE-EL-------EEEIEELRERFGDAPVDLGNAEDFLE 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1504 TIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQ--------EDAERlrkqvAEETQKKKNAEDELkrksEAEKEA 1575
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvEGSPH-----VETIEEDRERVEEL----EAELED 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1576 AKQKQKALDDLQKFKMQAEEAERRMkqaeeEKLRQikvveevaqksaatqlqshsmsfnvKASKLEESLKKEQGTVLQLQ 1655
Cdd:PRK02224 487 LEEEVEEVEERLERAEDLVEAEDRI-----ERLEE-------------------------RREDLEELIAERRETIEEKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1656 EEAEQLRKQQEEankareqAEKELETWRQKANEAlrlRLQAEEEAQKKSKTqeEAERQKVEAERDAKKRAKAEDAALKQK 1735
Cdd:PRK02224 537 ERAEELRERAAE-------LEAEAEEKREAAAEA---EEEAEEAREEVAEL--NSKLAELKERIESLERIRTLLAAIADA 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1736 DNAEKEL-EKQRTFAEQVAQ--QKLSAEQECIR-LKADFDHAeqqrglldnelqrlkkEVSATEKQRKLLEEELAKVRSE 1811
Cdd:PRK02224 605 EDEIERLrEKREALAELNDErrERLAEKRERKReLEAEFDEA----------------RIEEAREDKERAEEYLEQVEEK 668
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 1812 MDSLLKMKTEAEKKtMSNTEKSKQLLESEALKMKQLADEATRLRSVAEEAkkqrQTAEEEAARQRAE 1878
Cdd:PRK02224 669 LDELREERDDLQAE-IGAVENELEELEELRERREALENRVEALEALYDEA----EELESMYGDLRAE 730
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4361-4399 |
5.00e-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: 5.00e-12
10 20 30
....*....|....*....|....*....|....*....
gi 736215636 4361 LLEAQACTGGIIDPNTGEKFTVTDAMNKGLVDKVMVDRI 4399
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
172-269 |
5.08e-12 |
|
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: 65.10 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGyqgLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSN-QENLEQAFSVAERDLGVTRLLD 250
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 736215636 251 PEDVDVLHPDEKSIITYVS 269
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1652-2615 |
5.84e-12 |
|
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: 72.77 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1652 LQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEaLRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAA 1731
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACE-IRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1732 LKQKDNAEKELEKQrtfaeQVAQQKLSAEQECIRLKADFDHAEQQRGLLDN----------ELQRLKKEVSATEKQRKLL 1801
Cdd:TIGR00606 264 IMKLDNEIKALKSR-----KKQMEKDNSELELKMEKVFQGTDEQLNDLYHNhqrtvrekerELVDCQRELEKLNKERRLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1802 EEELAKVRSEMDSL-LKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSvAEEAKKQRQTAEEEAARQRAeAE 1880
Cdd:TIGR00606 339 NQEKTELLVEQGRLqLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKN-FHTLVIERQEDEAKTAAQLC-AD 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1881 KILKEKLAAiNEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSSDSEMVRQKTI 1960
Cdd:TIGR00606 417 LQSKERLKQ-EQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1961 VEETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKVIaEETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKVKR 2040
Cdd:TIGR00606 496 TETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQM-EMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQ 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2041 ITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAekqvivaKEAAQKCSSAEQKAQEVLSKNKEDSlAQQKMKE 2120
Cdd:TIGR00606 575 LEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNEL-------ESKEEQLSSYEDKLFDVCGSQDEES-DLERLKE 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2121 EFENAKRlaqaaekakekaeKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAeKLKKAAEEEASKRAAAEAEALKQKK 2200
Cdd:TIGR00606 647 EIEKSSK-------------QRAMLAGATAVYSQFITQLTDENQSCCPVCQRVF-QTEAELQEFISDLQSKLRLAPDKLK 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2201 QADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQV--EDELAKV------ 2272
Cdd:TIGR00606 713 STESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVcltdvt 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2273 ---RIQMdELLKLKLKIEEQNRSLMKKDKDKTQKVL-------AEEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAE 2342
Cdd:TIGR00606 793 imeRFQM-ELKDVERKIAQQAAKLQGSDLDRTVQQVnqekqekQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKS 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2343 QRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRldkETEGFQKSLEAERKRQLEVSAEAE 2422
Cdd:TIGR00606 872 EKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE---KEELISSKETSNKKAQDKVNDIKE 948
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2423 TLRLKVKELSDAQSKAENEAKKFKKQAD----EAKARLKDTEKQSTE------TVVQKLETQRLQSTREADGLKEAIADL 2492
Cdd:TIGR00606 949 KVKNIHGYMKDIENKIQDGKDDYLKQKEtelnTVNAQLEECEKHQEKinedmrLMRQDIDTQKIQERWLQDNLTLRKREN 1028
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2493 EKEREKLKKEAEELQnkSNKMANTQKEEIEQQKAIIQKSFISERELLLKRQKAVEDEKKKLQKQFedevkKAEALKDEQE 2572
Cdd:TIGR00606 1029 ELKEVEEELKQHLKE--MGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL-----REPQFRDAEE 1101
|
970 980 990 1000
....*....|....*....|....*....|....*....|...
gi 736215636 2573 RQRKLMEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEK 2615
Cdd:TIGR00606 1102 KYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINK 1144
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2781-2818 |
7.18e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 7.18e-12
10 20 30
....*....|....*....|....*....|....*...
gi 736215636 2781 LLEAQAASGYIVDPVKNKLLSVDEAVKCELIGPELHDR 2818
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1481-2068 |
7.73e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.41 E-value: 7.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1481 IKSKSQQLEHALVSHTKIEE--EIHTIRIQLEMTI--KQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQ 1556
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERyqALLKEKREYEGYEllKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1557 KKKNAEDELKRKSEAEKEAAKQKQKALD-DLQKFKMQAEEAERRMKQAEEEklRQIKVVEEVAQKSAATQLQSHSMSFNV 1635
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERSIAEKERELEDAEER--LAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1636 KASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAeRQKV 1715
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL-NAAI 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1716 EAERDAKKRAKAEdaalkqKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATE 1795
Cdd:TIGR02169 430 AGIEAKINELEEE------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1796 K-------QRKLLEE----------ELAKVRSEM---------------------------------------------- 1812
Cdd:TIGR02169 504 ErvrggraVEEVLKAsiqgvhgtvaQLGSVGERYataievaagnrlnnvvveddavakeaiellkrrkagratflplnkm 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1813 --------------------------------------DSLLKMKTEAEKKTM----------------------SNTEK 1832
Cdd:TIGR02169 584 rderrdlsilsedgvigfavdlvefdpkyepafkyvfgDTLVVEDIEAARRLMgkyrmvtlegelfeksgamtggSRAPR 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1833 SKQL-------------------------LESEALKMKQLADEATRLRSVAE----EAKKQRQTAEEEAARQRAEAE--- 1880
Cdd:TIGR02169 664 GGILfsrsepaelqrlrerleglkrelssLQSELRRIENRLDELSQELSDASrkigEIEKEIEQLEQEEEKLKERLEele 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1881 ---KILKEKLAAiNEATRLRTEAEIA-----LKAKEAENERLKRKAEDEAYQ--RKLLEDQAAQHKhDIQEKIIHL---- 1946
Cdd:TIGR02169 744 edlSSLEQEIEN-VKSELKELEARIEeleedLHKLEEALNDLEARLSHSRIPeiQAELSKLEEEVS-RIEARLREIeqkl 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1947 ------KSSSDSEMVRQKTIVEETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLkviaeETQKSKLKAEAEAEKL 2020
Cdd:TIGR02169 822 nrltleKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL-----ESRLGDLKKERDELEA 896
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 736215636 2021 KKLAAEEEKKRKESEEKVKRITAAEEEAARQckAAQEEVARLEKKADE 2068
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLE--ALEEELSEIEDPKGE 942
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2340-2668 |
8.45e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 8.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2340 LAEQRALAEKmlkekmqaiqeATKLKAEAQELQkqkdqAQEKAKKLlEDKQQIQQRLDKETEgfqkSLEAERKRQL---- 2415
Cdd:COG1196 205 LERQAEKAER-----------YRELKEELKELE-----AELLLLKL-RELEAELEELEAELE----ELEAELEELEaela 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2416 EVSAEAETLRLKVKELSD---AQSKAENEAKKFKKQADEAKARLKDTEKQSTETvVQKLETQRLQSTREADGLKEAIADL 2492
Cdd:COG1196 264 ELEAELEELRLELEELELeleEAQAEEYELLAELARLEQDIARLEERRRELEER-LEELEEELAELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2493 EKEREKLKKEAEELQNKSNKMANTQKEEIEQQKAIIQKSFISERELLLKRQKAVEDEKKklQKQFEDEVKKAEALKDEQE 2572
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ--LEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2573 RQRKLMEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEKKRLDQEKQLGAENQKLREKLQCLEGASKQSATKQVAS 2652
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
330
....*....|....*.
gi 736215636 2653 KTIEVQTDVVSEEQLV 2668
Cdd:COG1196 501 ADYEGFLEGVKAALLL 516
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1366-1922 |
1.07e-11 |
|
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: 71.32 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1366 TLRTRYSELMTLTSQYIKFITETQRRLEDDEKASEKLKEEERKKMAEIQAELDkqkqiAEAQAKSVIKAEQEAQELKLKM 1445
Cdd:pfam07111 52 SLELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELD-----ALAVAEKAGQAEAEGLRAALAG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1446 KEEASKRQDvavdaeqqkQNIQHELHHLKSLSEQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTikqkktAESELQQ 1525
Cdd:pfam07111 127 AEMVRKNLE---------EGSQRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETK------RAGEAKQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1526 LRDKAAEAEKLRK---AAQED-------AERLRKQVAEETQKKKNAED-ELKRKSEAekEAAKQKQKALDDLQK----FK 1590
Cdd:pfam07111 192 LAEAQKEAELLRKqlsKTQEEleaqvtlVESLRKYVGEQVPPEVHSQTwELERQELL--DTMQHLQEDRADLQAtvelLQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1591 MQAEEAERRMKQAEEEKLRQIK---VVEEVAQKSAATQLQS-----HSMSFNVKASKLE--ESLKKEQGTVLQLQEEAEQ 1660
Cdd:pfam07111 270 VRVQSLTHMLALQEEELTRKIQpsdSLEPEFPKKCRSLLNRwrekvFALMVQLKAQDLEhrDSVKQLRGQVAELQEQVTS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1661 LRKQQEEANKAREQAEKELETWRQKAnEALRLRLQAEEEAQKKSKTQ----EEAERQKVEAERDAKKR-----AKAEDAA 1731
Cdd:pfam07111 350 QSQEQAILQRALQDKAAEVEVERMSA-KGLQMELSRAQEARRRQQQQtasaEEQLKFVVNAMSSTQIWlettmTRVEQAV 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1732 LK------------QKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKAD----FDHAEQQRGLLDNELQR----LKKEV 1791
Cdd:pfam07111 429 ARipslsnrlsyavRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADlsleLEQLREERNRLDAELQLsahlIQQEV 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1792 SATEKQRKLLEEELAKVRSEMDSLLkmkteaeKKTMSNTEKSKQLLESEALKMKQLADEATRLRsvaEEAKKQRQTAEEE 1871
Cdd:pfam07111 509 GRAREQGEAERQQLSEVAQQLEQEL-------QRAQESLASVGQQLEVARQGQQESTEEAASLR---QELTQQQEIYGQA 578
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736215636 1872 AARQRAEAEKILKEKLA----AINEATRLRTEAEIALK------AKEAENERLKRKAEDEA 1922
Cdd:pfam07111 579 LQEKVAEVETRLREQLSdtkrRLNEARREQAKAVVSLRqiqhraTQEKERNQELRRLQDEA 639
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
52-151 |
1.40e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 64.37 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 52 ERDRvQKKTFTKWVNKhlMKSQRHITDLYEDLRDGHNLISLLE-VLSGE-------TLPREKGRMRFHKLQNVQIALDFL 123
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDkVIPGSvnwkkvnKAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 736215636 124 KHRQVKLVNIRNDDIADGNPKLTLGLIW 151
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2231-2667 |
1.54e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.95 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2231 KLRLDETDKQKALLDEeLQRVKGEVNDAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQNRSLMK-KDKDKTQKVLAEEA 2309
Cdd:COG4717 67 ELNLKELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2310 GKMKSLAEEAARLsveaEETARQRQIAESNLAE-QRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLED 2388
Cdd:COG4717 146 ERLEELEERLEEL----RELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2389 KQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKK------------FKKQADEAKARL 2456
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2457 KDTEKQSTETVVQKLETQRLQSTREADGLKEAIADLEKEREKLKKEAEELQNKSNKMANTQ---KEEIEQQKAIIQKSFI 2533
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElqlEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2534 SERELLLKRQKAVEDEKKKLQKQFEDEVKKAEALKDEQERQRKL----MEEEKKKLQAIMDAAVKKQKEAEADMKNKQTE 2609
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeeeLEEELEELEEELEELEEELEELREELAELEAE 461
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 2610 MEVLEKKRLDQEKQlgaenQKLREKLQCLEGASKQSATKQVASKTIEVQTDVVSEEQL 2667
Cdd:COG4717 462 LEQLEEDGELAELL-----QELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1750-2458 |
1.55e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 70.91 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1750 EQVAQQKLSAEQECIRlKADFDHAEQqrglLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMkTEAEKKTMSN 1829
Cdd:pfam05483 51 EQVANSGDCHYQEGLK-DSDFENSEG----LSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKI-IEAQRKAIQE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1830 ----TEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEiALK 1905
Cdd:pfam05483 125 lqfeNEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFE-ELR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1906 AkEAENERL----KRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSSDSEMVRQKT-IVEETLRQKKIVEEEIHIIRI 1980
Cdd:pfam05483 204 V-QAENARLemhfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTfLLEESRDKANQLEEKTKLQDE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1981 NFEKASKGKSDLENELKKLKVIAEETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQ---E 2057
Cdd:pfam05483 283 NLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTcslE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2058 EVARLEKKADEANKQKEKaekeaekqvIVAKEAAQKCSSAEQKAQevLSKNKEDSLAQ--------QKMKEEFENAKRLA 2129
Cdd:pfam05483 363 ELLRTEQQRLEKNEDQLK---------IITMELQKKSSELEEMTK--FKNNKEVELEElkkilaedEKLLDEKKQFEKIA 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2130 QAAEKAKEKAEKEAALLRQKAAEAEKQ---KKSAEEEAAKQAKAQK---DAEKLKKAAEEEASKRAAAEAEALKQK---- 2199
Cdd:pfam05483 432 EELKGKEQELIFLLQAREKEIHDLEIQltaIKTSEEHYLKEVEDLKtelEKEKLKNIELTAHCDKLLLENKELTQEasdm 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2200 ----KQADAEMAKHKKEADQALK-------LKSQVEKELTMVKLRL-DETDKQKALLD---EELQRVKGEVNDAVKQKAQ 2264
Cdd:pfam05483 512 tlelKKHQEDIINCKKQEERMLKqienleeKEMNLRDELESVREEFiQKGDEVKCKLDkseENARSIEYEVLKKEKQMKI 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2265 VEDELAKVRIQMDELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMK-SLAEEAARLSVEAEETARQRQIAESNLAEQ 2343
Cdd:pfam05483 592 LENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKlELELASAKQKFEEIIDNYQKEIEDKKISEE 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2344 RALAEkmlkekmqaIQEATKLKAEAQELQKQKD-QAQEKAKKLLEDKQQIQQRLDKETE------GFQKSLEAERKrQLE 2416
Cdd:pfam05483 672 KLLEE---------VEKAKAIADEAVKLQKEIDkRCQHKIAEMVALMEKHKHQYDKIIEerdselGLYKNKEQEQS-SAK 741
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 736215636 2417 VSAEAETLRLKVKELS-DAQSKAENEAK-KFKKQADEAKARLKD 2458
Cdd:pfam05483 742 AALEIELSNIKAELLSlKKQLEIEKEEKeKLKMEAKENTAILKD 785
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2146-2639 |
1.64e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2146 LRQKAAEAEKQKKSAEEEAAkQAKAQKDAEKLKKAAEEEaSKRAAAEAEALKQKKQADAEMAKHKKE--ADQALKLKSQV 2223
Cdd:PRK02224 211 LESELAELDEEIERYEEQRE-QARETRDEADEVLEEHEE-RREELETLEAEIEDLRETIAETEREREelAEEVRDLRERL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2224 EKELTMVKLRLDETDkqkaLLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELlklklkiEEQNRSLMKKDKDktqk 2303
Cdd:PRK02224 289 EELEEERDDLLAEAG----LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAH-------NEEAESLREDADD---- 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2304 vLAEEAgkmKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAK 2383
Cdd:PRK02224 354 -LEERA---EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2384 KLLEDKQQIQQRLDK-----------------ETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAEnEAKKFK 2446
Cdd:PRK02224 430 ELEATLRTARERVEEaealleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2447 KQADEAKARLKDTEK---QSTETVVQKLEtqRLQSTREADGLKEAIADLEKEREKLKKEAEELQNKSNKMANTQKEEIEQ 2523
Cdd:PRK02224 509 DRIERLEERREDLEEliaERRETIEEKRE--RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2524 QKAIIQKSfiseRELLLKRQKAVED-----EKKKLQKQFEDEVKkaEALKDEQERQRKLmeEEKKKLQAIMDAAVKKQkE 2598
Cdd:PRK02224 587 RIESLERI----RTLLAAIADAEDEierlrEKREALAELNDERR--ERLAEKRERKREL--EAEFDEARIEEAREDKE-R 657
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 736215636 2599 AEADMKNKQTEMEVLEKKRLDQEKQLGA------ENQKLREKLQCLE 2639
Cdd:PRK02224 658 AEEYLEQVEEKLDELREERDDLQAEIGAveneleELEELRERREALE 704
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
174-273 |
2.17e-11 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 63.13 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 174 KEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDmgKVYRQSN-----QENLEQAFSVAER-DLGVTR 247
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIP--KINKKPKspfkkRENINLFLNACKKlGLPELD 78
|
90 100
....*....|....*....|....*.
gi 736215636 248 LLDPEDVdVLHPDEKSIITYVSSLYD 273
Cdd:cd00014 79 LFEPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1149-1826 |
2.49e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1149 AEAALKTYESRLLDVNKVPENEKEVEEQRSQLKSMRAEVEADQVIFDRLQDELRRAstindkmtriHSERDAEMEHYRQL 1228
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----------LEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1229 VSSLLERWQVVFAQMDMRQRELDllgrhmnsynvsyewlihwlgEARKRQEKIQAVpiggSKALREQLAEEKKLLEEIEK 1308
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRR---------------------ELEERLEELEEE----LAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1309 NKDKIDSCQKNAKAYIDSVKDYELQILTykalqdpmasplkkpkmdcASDNIIQEYVTLRTRYSELMTLTSQYIKFITET 1388
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEA-------------------ELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1389 QRRLEDDEKASEKLKEEErkkmAEIQAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQH 1468
Cdd:COG1196 406 EEAEEALLERLERLEEEL----EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1469 ELhhlksLSEQEIKSKSQQLEHALVSHtkiEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEklrkAAQEDAERLR 1548
Cdd:COG1196 482 LL-----EELAEAAARLLLLLEAEADY---EGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA----LEAALAAALQ 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1549 KQVAEETQKKKNAEDELKRKSEAEKEA-AKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQ 1627
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFlPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1628 SHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELetwrqkanEALRLRLQAEEEAQKKSKTQ 1707
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL--------EELAERLAEEELELEEALLA 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1708 EEAERQKVEAERDAKKRAKAEDAALKQkdnaEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRglldnELQRL 1787
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEE----QLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER-----ELERL 772
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 736215636 1788 KKEVSA--------------TEKQRKLLEEELAKVRSEMDSLLKM--KTEAEKKT 1826
Cdd:COG1196 773 EREIEAlgpvnllaieeyeeLEERYDFLSEQREDLEEARETLEEAieEIDRETRE 827
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1556-1762 |
3.03e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 68.68 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1556 QKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEaerrmKQAEEEklrQIKVVEEVAQKSAATQlqshsmsfnv 1635
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKE-----RLAAQE---QKKQAEEAAKQAALKQ---------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1636 kasKLEESLKKEQGTVLQLQEEAEQLRkQQEEANKAREQAEKELETWRQKANEAlRLRLQAEEEAQKKSKTQEEAERQ-- 1713
Cdd:PRK09510 132 ---KQAEEAAAKAAAAAKAKAEAEAKR-AAAAAKKAAAEAKKKAEAEAAKKAAA-EAKKKAEAEAAAKAAAEAKKKAEae 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 736215636 1714 -KVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAEQE 1762
Cdd:PRK09510 207 aKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2045-2230 |
3.31e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 68.68 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2045 EEEAARQCKAAQEEVARLEKKADEANKQKEKaekeaekqvivAKEAAQKCSSAEQKAQEVLSKNKEDslAQQKMKEEfen 2124
Cdd:PRK09510 89 AEELQQKQAAEQERLKQLEKERLAAQEQKKQ-----------AEEAAKQAALKQKQAEEAAAKAAAA--AKAKAEAE--- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2125 AKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAK---QAKAQKDAEKLKKAAeEEASKRAAAEAEALKQKKQ 2201
Cdd:PRK09510 153 AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKaaaEAKKKAEAEAKKKAA-AEAKKKAAAEAKAAAAKAA 231
|
170 180
....*....|....*....|....*....
gi 736215636 2202 ADAEmAKHKKEADQALKLKSQVEKELTMV 2230
Cdd:PRK09510 232 AEAK-AAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1717-1934 |
4.56e-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: 68.25 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1717 AERDAKKRAKAEDAALKQK-DNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATE 1795
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1796 KQRKLLEEELAKVrseMDSLLKMKTEAEKKTMSNTEKSKQLLESEAL---KMKQLADEATRLRSVAEEAKKQRQTAEEEA 1872
Cdd:COG4942 97 AELEAQKEELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYlkyLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736215636 1873 ARQ---RAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQ 1934
Cdd:COG4942 174 AELealLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
563-752 |
6.96e-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: 65.16 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 563 MRYIQDLLGWVEENQRRVDDGQWGSDLPTVESQLGSHRGLHQSVEEFHSKIQRAKADESQI---SPASKGAYRDYLGKLE 639
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 640 LQYGKLLNASKARLHSLD---QLHAFVIAATKELMWLNEKEEEEVNYDWSERNTNMTAKKDNYSGLMRDLELREKKVNVV 716
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 736215636 717 QATGDKLLRDGHP-ARKTVEAFTGALQTQWSWLLQLC 752
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1678-2440 |
6.98e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.10 E-value: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1678 ELETWRQKAN--EALRLRLQAEEEAQKKSKTQEeAERQKVEAERDAKKRakaedaalkqkdnaekelEKQRTFAEQVAQQ 1755
Cdd:pfam12128 242 EFTKLQQEFNtlESAELRLSHLHFGYKSDETLI-ASRQEERQETSAELN------------------QLLRTLDDQWKEK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1756 KLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEvsaTEKQRKLLEEELAKVRSEMdsllkmkteaekktmSNTEKSKQ 1835
Cdd:pfam12128 303 RDELNGELSAADAAVAKDRSELEALEDQHGAFLDA---DIETAAADQEQLPSWQSEL---------------ENLEERLK 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1836 LLESEAlkmkqladeatrlRSVAEEAKKQRQTAEEEAARQRAEaekiLKEKLAAINEA-TRLRTEAEIALKAKEAEnerl 1914
Cdd:pfam12128 365 ALTGKH-------------QDVTAKYNRRRSKIKEQNNRDIAG----IKDKLAKIREArDRQLAVAEDDLQALESE---- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1915 krkaedeayqrklLEDQAAQHKHDIQEKIIHLKSSSDSEMVR--QKTIVEETLRQKKIVEEEIHIIRINFEKASKGKSDL 1992
Cdd:pfam12128 424 -------------LREQLEAGKLEFNEEEYRLKSRLGELKLRlnQATATPELLLQLENFDERIERAREEQEAANAEVERL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1993 ENELKKLKVIAEETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKA---AQEEVAR--LEKKAD 2067
Cdd:pfam12128 491 QSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGkviSPELLHRtdLDPEVW 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2068 EANKQKEKAEKEAEKQVivakEAAQKCSSA--EQKAQEVLSKNKEDSLAQQKMKEEFEnaKRLAQAAEKAKEKAEKEAAL 2145
Cdd:pfam12128 571 DGSVGGELNLYGVKLDL----KRIDVPEWAasEEELRERLDKAEEALQSAREKQAAAE--EQLVQANGELEKASREETFA 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2146 LRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEK 2225
Cdd:pfam12128 645 RTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVE 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2226 EltmvklrldETDKQKALLDEELQrvKGEVNDAVKQKA---QVEDELAKVRIQMDELLKLKLKIEEQNRSLMKKDKDKtQ 2302
Cdd:pfam12128 725 G---------ALDAQLALLKAAIA--ARRSGAKAELKAletWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRR-Q 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2303 KVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKA 2382
Cdd:pfam12128 793 EVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL 872
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 2383 KKLledkqqiqqRLDKETEGFQKSLeAERKRQLevsaeaETLRLKVKELS-DAQSKAEN 2440
Cdd:pfam12128 873 ATL---------KEDANSEQAQGSI-GERLAQL------EDLKLKRDYLSeSVKKYVEH 915
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
49-157 |
1.02e-10 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 61.83 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 49 CADERDRVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLP----REKGRMRFHKLQNVQIALDFLK 124
Cdd:cd21222 9 EAPEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELME 88
|
90 100 110
....*....|....*....|....*....|...
gi 736215636 125 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 157
Cdd:cd21222 89 DAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2210-2600 |
1.08e-10 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 68.12 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2210 KKEADQALKLKSQVEKELTMVKLRLDET-DKQKALLDEELQRVKGE-VNDAVKQKAQVEDEL-AKVRIQMDELLKlklKI 2286
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRkHTQNVALNKKLSDIKTEyLYELNVLKEKSEAELtSKTKKELDAAFE---QF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2287 EEQNRSLMKKDKDKTQKVlAEEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRAlaekmlkekmqaiqEATKLKA 2366
Cdd:NF033838 131 KKDTLEPGKKVAEATKKV-EEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKA--------------ELELVKE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2367 EAQELQKQKDQAQEKAKklLEDKQQIQQRLDKetegfqksLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFK 2446
Cdd:NF033838 196 EAKEPRDEEKIKQAKAK--VESKKAEATRLEK--------IKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2447 KQADEAKARLKDTEKQSTETVVQKLETQRLQSTREADGLKEAIADLEKEREKLKKEAEELQNKSNKMANTQKE---EIEQ 2523
Cdd:NF033838 266 KRGVLGEPATPDKKENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKTlelEIAE 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 2524 QKAIIQKSfisERELLLKRQKAVEDEKKKLQKQFEDEVKKAEALKDEQ-ERQRKLMEEEKKKLQAIMDAAvkKQKEAE 2600
Cdd:NF033838 346 SDVKVKEA---ELELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLEKiKTDRKKAEEEAKRKAAEEDKV--KEKPAE 418
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3184-3222 |
1.26e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.88 E-value: 1.26e-10
10 20 30
....*....|....*....|....*....|....*....
gi 736215636 3184 LLEAQLSTGGIIDPINSYRIPHDLACKRGYFDEEIDKTL 3222
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1592-1962 |
1.58e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 68.06 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1592 QAEEAERRM----KQAEEEKLRQIKVVEEVAQKSAA-----TQLQSHSMSFN--VKASKLEESLKKEQGTVLQLQEEAEQ 1660
Cdd:COG3096 286 RALELRRELfgarRQLAEEQYRLVEMARELEELSAResdleQDYQAASDHLNlvQTALRQQEKIERYQEDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1661 LRKQQEEANKAREQAEKELETWRQKANEaLRLRL----QAEEEAQkkskTQEEAERQKVEAERDAKKRAKAEDAALkqkD 1736
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEAAEEEVDS-LKSQLadyqQALDVQQ----TRAIQYQQAVQALEKARALCGLPDLTP---E 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1737 NAEKELEKQRTFAEQVAQQKLSAEQeciRL------KADFDHAEQQrglldneLQRLKKEVS---ATEKQRKLLEE--EL 1805
Cdd:COG3096 438 NAEDYLAAFRAKEQQATEEVLELEQ---KLsvadaaRRQFEKAYEL-------VCKIAGEVErsqAWQTARELLRRyrSQ 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1806 AKVRSEMDSLLKMKTEAEKKtMSNTEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAAR---QRAEAEKI 1882
Cdd:COG3096 508 QALAQRLQQLRAQLAELEQR-LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEaveQRSELRQQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1883 LKEKLAAINE--------------ATRLRTEAEIALKAKEAENERLKRKAEDEAyQRKLLEDQAAQHKHDIQEKIIHLKS 1948
Cdd:COG3096 587 LEQLRARIKElaarapawlaaqdaLERLREQSGEALADSQEVTAAMQQLLERER-EATVERDELAARKQALESQIERLSQ 665
|
410
....*....|....
gi 736215636 1949 SSDSEMVRQKTIVE 1962
Cdd:COG3096 666 PGGAEDPRLLALAE 679
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1521-1919 |
1.67e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 68.06 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1521 SELQQLRDKAAEAEKLRKAAqedaerlRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFK---MQAEEAE 1597
Cdd:COG3096 278 NERRELSERALELRRELFGA-------RRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQtalRQQEKIE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1598 RRMKQAEE--EKLR-QIKVVEEVAQKSAATQLQSHSMSFNVKASK-----LEESLKKEQGTVLQLQEEAEQLRKQQ---E 1666
Cdd:COG3096 351 RYQEDLEEltERLEeQEEVVEEAAEQLAEAEARLEAAEEEVDSLKsqladYQQALDVQQTRAIQYQQAVQALEKARalcG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1667 EANKAREQAEKELETWRQKANEALRLRLQAEeeaQKKS-----KTQEEAERQKVEAERDAKKRAKAEDAAlkqkdnaeKE 1741
Cdd:COG3096 431 LPDLTPENAEDYLAAFRAKEQQATEEVLELE---QKLSvadaaRRQFEKAYELVCKIAGEVERSQAWQTA--------RE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1742 LEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEkqrkLLEEELAKVRSEMDSLLKMKTE 1821
Cdd:COG3096 500 LLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE----ELEELLAELEAQLEELEEQAAE 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1822 AEKKTMSNTEKSKQL------LESEALKMKQLADEATRLRSVAEEAKKQRQtaEEEAARQR-AEAE---KILKEKLAAIN 1891
Cdd:COG3096 576 AVEQRSELRQQLEQLrarikeLAARAPAWLAAQDALERLREQSGEALADSQ--EVTAAMQQlLEREreaTVERDELAARK 653
|
410 420
....*....|....*....|....*...
gi 736215636 1892 EatRLRTEAEIALKAKEAENERLKRKAE 1919
Cdd:COG3096 654 Q--ALESQIERLSQPGGAEDPRLLALAE 679
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2857-2895 |
1.67e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.49 E-value: 1.67e-10
10 20 30
....*....|....*....|....*....|....*....
gi 736215636 2857 FLDVQLATGGIVDPINSHRVQLQTAYKQGQFDADMNKKL 2895
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1390-1811 |
2.30e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1390 RRLEDDEKASEKLKEEERKKMAEIQAELDKQKQIAEAQAksvikAEQEAQELKLKMKEEASKRQDvavdAEQQKQNIQHE 1469
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-----LYQELEALEAELAELPERLEE----LEERLEELREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1470 LHHLKSLsEQEIKSKSQQLEHALVSHT-KIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEklrkaaqEDAERLR 1548
Cdd:COG4717 162 EEELEEL-EAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE-------EELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1549 KQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQK--------------FKMQAEEAERRMKQAEEEKLRQIKVV 1614
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1615 EEVAQKSAATQLQSHSMSFNVKASKLEESLKKEQgtvlQLQEEAEQLRKQQEEAnkAREQAEKELETWRQKAN----EAL 1690
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIE----ELQELLREAEELEEEL--QLEELEQEIAALLAEAGvedeEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1691 RLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAED-----AALKQKDNAEKELEKQRTFAEQvAQQKLSAEQECIR 1765
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeeleEELEELEEELEELEEELEELRE-ELAELEAELEQLE 466
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 736215636 1766 LKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSE 1811
Cdd:COG4717 467 EDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
174-269 |
2.43e-10 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 60.48 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 174 KEKLLLWSQRMVEGyqgLRCDNFTTGWRDGKLFNAIIHKHRPTLI-DMGKVYRQSNQENLEQAFSVAERDLGVTRLLDPE 252
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 736215636 253 DVDVLHPDEKSIITYVS 269
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2146-2650 |
3.47e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2146 LRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKK--AAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQV 2223
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGskRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2224 EKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQNRSLMKKDKdkTQK 2303
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--LER 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2304 VLAEEAGKMKslaEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLK------------------ 2365
Cdd:PRK03918 377 LKKRLTGLTP---EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkel 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2366 -----AEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVsaeaetlRLKVKELSDAQSKAEn 2440
Cdd:PRK03918 454 leeytAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEE-------KLKKYNLEELEKKAE- 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2441 EAKKFKKQADEAKARLKDTEKQSTEtvVQKLETQRLQSTREADGLKEAIADLEKEREKLKKeaeelqnKSNKMANTQKEE 2520
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEK--LEELKKKLAELEKKLDELEEELAELLKELEELGF-------ESVEELEERLKE 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2521 IEQ--QKAIIQKSFISERELLLKRQKAVEDEKKKLQKQFEDEVKKAEALKDE-QERQRKLMEEEKKK------------- 2584
Cdd:PRK03918 597 LEPfyNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKElEELEKKYSEEEYEElreeylelsrela 676
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 2585 -LQAIMDAAVKKQKEAEADMKNKQTEMEVLEKKRLDQEK--QLGAENQKLREKLQCLEGASKQSATKQV 2650
Cdd:PRK03918 677 gLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKleKALERVEELREKVKKYKALLKERALSKV 745
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
58-154 |
3.54e-10 |
|
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: 60.28 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 58 KKTFTKWVNKHLMKSQ---------RHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDFL 123
Cdd:cd21217 3 KEAFVEHINSLLADDPdlkhllpidPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 736215636 124 KHRQVKLVNIRNDDIADGNPKLTLGLIWTII 154
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1989-2636 |
3.63e-10 |
|
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: 66.92 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1989 KSDLENELKKLKVIAEETQKS------KLKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAA-----QE 2057
Cdd:TIGR00618 221 KQVLEKELKHLREALQQTQQShayltqKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAplaahIK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2058 EVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQ-EVLSKNKEDSLAQQK-----MKEEFENAKRLAQA 2131
Cdd:TIGR00618 301 AVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRlLQTLHSQEIHIRDAHevatsIREISCQQHTLTQH 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2132 AEKAKEKAEKEAALLRQKAAEAEK-QKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAK-H 2209
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDIlQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKiH 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2210 KKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVndavkQKAQVEDELAKVRIQMDELLKLKLKIEEQ 2289
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL-----CGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2290 NRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQiaesnlaeqralaekmlkekmQAIQEATKLKAEAQ 2369
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDN---------------------RSKEDIPNLQNITV 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2370 ELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQA 2449
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEL 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2450 DEAKARLKDTEKQSTETVVQKLET--QRLQSTREadglkeaiadlekeREKLKKEAEELQNKSNKMANTQKEEIEQQKAI 2527
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMlaQCQTLLRE--------------LETHIEEYDREFNEIENASSSLGSDLAAREDA 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2528 IQKSFiserelllkrqkavedekKKLQKQFeDEVKKAEALKDEQERQRKLMEEEK-KKLQAIMDAAVKKQKEAEADMKNK 2606
Cdd:TIGR00618 741 LNQSL------------------KELMHQA-RTVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLL 801
|
650 660 670
....*....|....*....|....*....|
gi 736215636 2607 QTEMEVLEKKRLDQEKQLGAENQKLREKLQ 2636
Cdd:TIGR00618 802 KTLEAEIGQEIPSDEDILNLQCETLVQEEE 831
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1961-2665 |
3.76e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1961 VEETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKviaeetqksklKAEAEAEKLKKLAAEEEKKRKESEEKVKR 2040
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLR-----------REREKAERYQALLKEKREYEGYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2041 ITAAEEEAA-RQCKAAQEEVARLEKKADEankqkekaekeaekqviVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMK 2119
Cdd:TIGR02169 234 ALERQKEAIeRQLASLEEELEKLTEEISE-----------------LEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2120 EEFENAKRLAQaaekakekaekeaallRQKAAEAEKQKKSAEEEAAKQA---KAQKDAEKLKKAAEEEASKRAAAEAEAL 2196
Cdd:TIGR02169 297 GELEAEIASLE----------------RSIAEKERELEDAEERLAKLEAeidKLLAEIEELEREIEEERKRRDKLTEEYA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2197 KQKKQAD---AEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVR 2273
Cdd:TIGR02169 361 ELKEELEdlrAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2274 IQMDElLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRAlAEKMLKE 2353
Cdd:TIGR02169 441 EEKED-KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA-VEEVLKA 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2354 KMQAI------------QEATKLK------------------AEAQELQKQK-------------------------DQA 2378
Cdd:TIGR02169 519 SIQGVhgtvaqlgsvgeRYATAIEvaagnrlnnvvveddavaKEAIELLKRRkagratflplnkmrderrdlsilseDGV 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2379 QEKAKKLLEDKQQIQ-------------QRLDK-------------ETEGFQKS---------LEAERKRQLEVSAEAET 2423
Cdd:TIGR02169 599 IGFAVDLVEFDPKYEpafkyvfgdtlvvEDIEAarrlmgkyrmvtlEGELFEKSgamtggsraPRGGILFSRSEPAELQR 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2424 LRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEK-------------QSTETVVQKLEtqrlQSTREADGLKEAIA 2490
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRkigeiekeieqleQEEEKLKERLE----ELEEDLSSLEQEIE 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2491 DLEKEREKLKKEAEELQNKSNKMantqKEEIEQQKAIIQKSFISERELLLkrqKAVEDEKKKLQKQFED----------E 2560
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKL----EEALNDLEARLSHSRIPEIQAEL---SKLEEEVSRIEARLREieqklnrltlE 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2561 VKKAEALKDEQERQRKLMEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEKKRLDQEKQLGAENQKLREKLQCLEG 2640
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
810 820
....*....|....*....|....*
gi 736215636 2641 ASKQSATKQVASKTIEVQTDVVSEE 2665
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2233-2452 |
4.41e-10 |
|
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: 65.17 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2233 RLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELLKlKLKIEEQNRSLMKKDKDKTQKVLAEEAGKM 2312
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-RIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2313 KSLAEEAARLSVEAEETARQRQIA---ESNLAEQRALAEKMLKEKMQAIQE-ATKLKAEAQELQKQKDQAQEKAKKL--- 2385
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAALRAELEAERAELeal 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 2386 LEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEA 2452
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1593-1936 |
5.07e-10 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 65.66 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1593 AEEAER-RMKQAEEEKLRQIKVVEEVAQKSAATQLQSHSMSFNVKASKLEE--SLKKEQGTVLQLQEEAEQLRKQQEEAn 1669
Cdd:pfam02029 4 EEEAAReRRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGqgGLDEEEAFLDRTAKREERRQKRLQEA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1670 karEQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEE-AERQKVEAERDAKKRAKAEDaalkqKDNAEKELEKQRtf 1748
Cdd:pfam02029 83 ---LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEkRDSRLGRYKEEETEIREKEY-----QENKWSTEVRQA-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1749 AEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQrLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMS 1828
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKK-VKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1829 NTEKSKQllESEALKMKQLADEATRLR---SVAEEAKKQRQTaEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALK 1905
Cdd:pfam02029 232 QSQEREE--EAEVFLEAEQKLEELRRRrqeKESEEFEKLRQK-QQEAELELEELKKKREERRKLLEEEEQRRKQEEAERK 308
|
330 340 350
....*....|....*....|....*....|....*..
gi 736215636 1906 AKEAENERL------KRKAEDEAYQRKLLEDQAAQHK 1936
Cdd:pfam02029 309 LREEEEKRRmkeeieRRRAEAAEKRQKLPEDSSSEGK 345
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3848-3886 |
5.29e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 57.34 E-value: 5.29e-10
10 20 30
....*....|....*....|....*....|....*....
gi 736215636 3848 VLEAQNATGGFIDPEYYFRLPTDVAMQRGYINKETLDRI 3886
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2297-2635 |
6.40e-10 |
|
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: 66.15 E-value: 6.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2297 DKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQI---------AESNLAEQRALAEK--MLKEKMQAIQEATKLK 2365
Cdd:pfam02463 150 MKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELiidleelklQELKLKEQAKKALEyyQLKEKLELEEEYLLYL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2366 AEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSL----------EAERKRQLEVSAEAETLRLKVKELSDAQ 2435
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLkenkeeekekKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2436 SKAENEAKKFKKQADEAKARLKDTEKQSTETVVQKLETQRLQSTREADglKEAIADLEKEREKLKKEAEELQNKSNKMAN 2515
Cdd:pfam02463 310 VDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEE--EEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2516 TQKEEIEQQKAIIQKSfISERELLLKRQKAVEDEKKKLQKQFEDEVKKAEALKDEQERQRKLMEEEKKKLQAIMDAAVKK 2595
Cdd:pfam02463 388 SAAKLKEEELELKSEE-EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE 466
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 736215636 2596 QKEAEADMKNKQTEMEVLEKKRLDQEKQLGAENQKLREKL 2635
Cdd:pfam02463 467 LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKAR 506
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2040-2401 |
8.05e-10 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 64.92 E-value: 8.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2040 RITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKcssaeqkaQEVLSKNKEDSlaQQKMK 2119
Cdd:pfam07888 63 RYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE--------KDALLAQRAAH--EARIR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2120 EEFENAKRLAQAAEKAKEKAEKEAAllRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQK 2199
Cdd:pfam07888 133 ELEEDIKTLTQRVLERETELERMKE--RAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2200 KQADAEMAKHK-KEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQ-------RVKGEVNDAVKQKAQVEDELAK 2271
Cdd:pfam07888 211 LQDTITTLTQKlTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSsmaaqrdRTQAELHQARLQAAQLTLQLAD 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2272 VRIQMDELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAArlsveaeetarQRQIAESNLAEQRALAEKML 2351
Cdd:pfam07888 291 ASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERM-----------EREKLEVELGREKDCNRVQL 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 736215636 2352 KEKMQAIQEatkLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETE 2401
Cdd:pfam07888 360 SESRRELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
174-274 |
8.33e-10 |
|
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: 58.90 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 174 KEKLLLWSQRMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQAFSVAERDLGVTRLLDPED 253
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 736215636 254 VdVLHPDEKSIITYVSSLYDA 274
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1410-1865 |
8.77e-10 |
|
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: 65.16 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1410 MAEIQAELDKQKQIAEAQAKSVIKA----------EQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQhELHHLKSLSEQ 1479
Cdd:pfam07111 206 LSKTQEELEAQVTLVESLRKYVGEQvppevhsqtwELERQELLDTMQHLQEDRADLQATVELLQVRVQ-SLTHMLALQEE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1480 EIKSKSQQLEHALVSHTK--------IEEEIHTIRIQLEM-------TIKQKKTAESELQQ---------------LRDK 1529
Cdd:pfam07111 285 ELTRKIQPSDSLEPEFPKkcrsllnrWREKVFALMVQLKAqdlehrdSVKQLRGQVAELQEqvtsqsqeqailqraLQDK 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1530 AAEAEKLR---KAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEe 1606
Cdd:pfam07111 365 AAEVEVERmsaKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVR- 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1607 KLRQIKVVeeVAQKSAATQLQSHSMSFNVKASKLEESLKKEqgtVLQLQEEAEQLRKQ--------QEEANKAREQAEKE 1678
Cdd:pfam07111 444 KVHTIKGL--MARKVALAQLRQESCPPPPPAPPVDADLSLE---LEQLREERNRLDAElqlsahliQQEVGRAREQGEAE 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1679 letwRQKANEALRlrlQAEEEAQkksKTQEEAER--QKVEAERDAKKRAKAEDAALKQkdnaekELEKQRTFAEQVAQQK 1756
Cdd:pfam07111 519 ----RQQLSEVAQ---QLEQELQ---RAQESLASvgQQLEVARQGQQESTEEAASLRQ------ELTQQQEIYGQALQEK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1757 LsAEQEcIRLKADFdhAEQQRGLLDNELQRLKKEVSATEKQRKLLEEelaKVRSEmdSLLKMKTEAEKKTMSNTEKSKQL 1836
Cdd:pfam07111 583 V-AEVE-TRLREQL--SDTKRRLNEARREQAKAVVSLRQIQHRATQE---KERNQ--ELRRLQDEARKEEGQRLARRVQE 653
|
490 500
....*....|....*....|....*....
gi 736215636 1837 LESEalkmKQLADEATRLRSVAEEAKKQR 1865
Cdd:pfam07111 654 LERD----KNLMLATLQQEGLLSRYKQQR 678
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2004-2214 |
9.11e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.06 E-value: 9.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2004 EETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLE----KKADEANKQkekaeke 2079
Cdd:PRK09510 68 QQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAalkqKQAEEAAAK------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2080 aekqvivAKEAAQKCSSAEQKAQEVLSKNKEdslAQQKMKEEFENAKRLAQAAEKAKEKAEKeaallrQKAAEAEKQKks 2159
Cdd:PRK09510 141 -------AAAAAKAKAEAEAKRAAAAAKKAA---AEAKKKAEAEAAKKAAAEAKKKAEAEAA------AKAAAEAKKK-- 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 2160 AEEEAAKQA----KAQKDAEKLKKAAEEEASKRAAAEAEAlKQKKQADAEMAKHKKEAD 2214
Cdd:PRK09510 203 AEAEAKKKAaaeaKKKAAAEAKAAAAKAAAEAKAAAEKAA-AAKAAEKAAAAKAAAEVD 260
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2101-2658 |
9.14e-10 |
|
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: 65.15 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2101 AQEVLSKNKEDSLAQQKMKEEFENAKRLAqaaekakekaekeaalLRQKAAEAEKQKksAEEEAAKQAKAQKDAEKLKKA 2180
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARI----------------ELEKKASALKRQ--LDRESDRNQELQKRIRLLEKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2181 aEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQAL----KLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKgEVN 2256
Cdd:pfam05557 64 -EAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLadarEVISCLKNELSELRRQIQRAELELQSTNSELEELQ-ERL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2257 DAVKQKAQ-VEDELAKVRIQMDELLKLKLKIEEQNRSLMKKDKDKTQ-KVLAEEAGKMKSLAEEAARLSVEAE---ETAR 2331
Cdd:pfam05557 142 DLLKAKASeAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvKNSKSELARIPELEKELERLREHNKhlnENIE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2332 QRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLledkqqiqqrldKETEGFQKSLEAER 2411
Cdd:pfam05557 222 NKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNL------------RSPEDLSRRIEQLQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2412 KRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQstetvVQKLETQRLQSTREADGLKEAIA- 2490
Cdd:pfam05557 290 QREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKAL-----VRRLQRRVLLLTKERDGYRAILEs 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2491 -DLEKEREKLKKEAEELQNKSNKMANTQKEEIEQQKAIIQKSfisERELLLKRQKAVEDE----KKKLQKQFEDEVKKAE 2565
Cdd:pfam05557 365 yDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVA---EEELGGYKQQAQTLErelqALRQQESLADPSYSKE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2566 ALK------DEQERQRKLMEEEKKKLQAIMdaaVKKQKEAEADMKN------KQTEMEVLEKKRLDQEKQLGAENQKLRE 2633
Cdd:pfam05557 442 EVDslrrklETLELERQRLREQKNELEMEL---ERRCLQGDYDPKKtkvlhlSMNPAAEAYQQRKNQLEKLQAEIERLKR 518
|
570 580
....*....|....*....|....*
gi 736215636 2634 KLQCLEGASKQSATKQVASKTIEVQ 2658
Cdd:pfam05557 519 LLKKLEDDLEQVLRLPETTSTMNFK 543
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1479-1839 |
9.84e-10 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 64.50 E-value: 9.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1479 QEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLR-KAAQEDAERLRKQVAEETQK 1557
Cdd:pfam02029 17 EERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRqKRLQEALERQKEFDPTIADE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1558 KKNAEDELKRKSEAEKEAAKQKQKalDDLQKFKMQAEEAERRMKQAEEEKLRQ-IKVVEEVAQKSAATQLQSHSMSfnvK 1636
Cdd:pfam02029 97 KESVAERKENNEEEENSSWEKEEK--RDSRLGRYKEEETEIREKEYQENKWSTeVRQAEEEGEEEEDKSEEAEEVP---T 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1637 ASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEeeaqkkSKTQEEAERQKVE 1716
Cdd:pfam02029 172 ENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ------SQEREEEAEVFLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1717 AERdakkraKAEDAALKQKDNAEKELEKQRtfaeqvaQQKLSAEQECIRLKAdfdHAEQQRGLLDNELQRLKKEvsatEK 1796
Cdd:pfam02029 246 AEQ------KLEELRRRRQEKESEEFEKLR-------QKQQEAELELEELKK---KREERRKLLEEEEQRRKQE----EA 305
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 736215636 1797 QRKLLEEELAKvrsemdsllKMKTEAEKKTMSNTEKSKQLLES 1839
Cdd:pfam02029 306 ERKLREEEEKR---------RMKEEIERRRAEAAEKRQKLPED 339
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
59-153 |
1.06e-09 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 58.50 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 59 KTFTKWVNKHLMKS--QRHITDLYEDLRDGHNLISLLEVLSGETL------PREKGRMrfhkLQNVQIALDFLKHRQVKL 130
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 736215636 131 VNIRNDDIADGNPKLTLGLIWTI 153
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1307-1942 |
1.14e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.74 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1307 EKNKDKI--------------DSCQKNA--------------KAYIDSVKDYELQILTYKALQDPmasplkkpkmdcASD 1358
Cdd:pfam05483 141 QENKDLIkennatrhlcnllkETCARSAektkkyeyereetrQVYMDLNNNIEKMILAFEELRVQ------------AEN 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1359 NIIQEYVTLRTRYSELMTLTSQYIKFITETQRRLEddekaseklkeeerKKMAEIQAELDKQKQIAEAQAKSVIKAEQEA 1438
Cdd:pfam05483 209 ARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVS--------------LLLIQITEKENKMKDLTFLLEESRDKANQLE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1439 QELKLK---MKEEASKRQDVAVDAEQQKQNIQHELHHLKSLSE-------------QEIKSKSQQLEHALVSHT------ 1496
Cdd:pfam05483 275 EKTKLQdenLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEdlqiatkticqltEEKEAQMEELNKAKAAHSfvvtef 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1497 -----KIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEetqkKKNAEDELKRKSEA 1571
Cdd:pfam05483 355 eattcSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE----DEKLLDEKKQFEKI 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1572 EKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQSHSMSFNVKASKLEESLKKEQGTV 1651
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASD 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1652 LQLqeeaeQLRKQQEEANKAREQAEKELEtwrqkanealrlRLQAEEEAQKKSKTQEEAERQKVEAERDAKKrakaedaa 1731
Cdd:pfam05483 511 MTL-----ELKKHQEDIINCKKQEERMLK------------QIENLEEKEMNLRDELESVREEFIQKGDEVK-------- 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1732 lKQKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSE 1811
Cdd:pfam05483 566 -CKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1812 MDSL---LKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAEEaKKQRQTAEEEA--ARQRAEAEKILKEK 1886
Cdd:pfam05483 645 LASAkqkFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDK-RCQHKIAEMVAlmEKHKHQYDKIIEER 723
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736215636 1887 LAAI-------NEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEK 1942
Cdd:pfam05483 724 DSELglyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1526-1901 |
1.24e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.98 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1526 LRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKN-------AEDELKRKSEAEKeAAKQKQKALDDLQKFKMQAEEAER 1598
Cdd:PRK04863 291 LRRELYTSRRQLAAEQYRLVEMARELAELNEAESDleqdyqaASDHLNLVQTALR-QQEKIERYQADLEELEERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1599 RMKQAEEEKL-RQIKVVE-EVAQKSAATQLQSHSMSFNV---------KASKLEESLKKEQG----TVLQLQEEAEQLRK 1663
Cdd:PRK04863 370 VVEEADEQQEeNEARAEAaEEEVDELKSQLADYQQALDVqqtraiqyqQAVQALERAKQLCGlpdlTADNAEDWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1664 QQEEANKAREQAEKEL---ETWRQKANEALRL--RLQAE---EEAQKKSK-TQEEAERQKVEAERDAKKRAKAedAALKQ 1734
Cdd:PRK04863 450 KEQEATEELLSLEQKLsvaQAAHSQFEQAYQLvrKIAGEvsrSEAWDVAReLLRRLREQRHLAEQLQQLRMRL--SELEQ 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1735 KDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADfdhAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDS 1814
Cdd:PRK04863 528 RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE---LEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPA 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1815 LLKMKTEAEKKTmsntEKSKQLLESEALKMKQLADEATRLRSvaeeakkQRQTAEEEAARQRAEAEKILKEKLAAINEAT 1894
Cdd:PRK04863 605 WLAAQDALARLR----EQSGEEFEDSQDVTEYMQQLLERERE-------LTVERDELAARKQALDEEIERLSQPGGSEDP 673
|
....*..
gi 736215636 1895 RLRTEAE 1901
Cdd:PRK04863 674 RLNALAE 680
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1444-2025 |
1.33e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 64.92 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1444 KMKEEASKRQDVAVDAEQQKQNIQHELHHLKSlSEQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKKTAESEL 1523
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNIDYLEEKLKS-SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1524 QQLRDKAAEAEKLRKAAQEDAERLrKQVAEETQKKKNAEDELKRkseAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQA 1603
Cdd:PRK01156 242 NELSSLEDMKNRYESEIKTAESDL-SMELEKNNYYKELEERHMK---IINDPVYKNRNYINDYFKYKNDIENKKQILSNI 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1604 EEeklrQIKVVEEVAQKsaATQLQSHSMSFNVKASKLEEsLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWR 1683
Cdd:PRK01156 318 DA----EINKYHAIIKK--LSVLQKDYNDYIKKKSRYDD-LNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1684 QKANEALRLrlqAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEkqrtfaeqvaqqKLSAEQEC 1763
Cdd:PRK01156 391 AFISEILKI---QEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNME------------MLNGQSVC 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1764 IRLKADF--DHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKvrsemdsLLKMKTEAEKKTMSNTEKSKQLLESEA 1841
Cdd:PRK01156 456 PVCGTTLgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVD-------LKKRKEYLESEEINKSINEYNKIESAR 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1842 LKMKQLADEATRLRSV---AEEAKKQRQTAEEEAARQRAEA----------------EKILKEKLAAINEATRLRTEAEI 1902
Cdd:PRK01156 529 ADLEDIKIKINELKDKhdkYEEIKNRYKSLKLEDLDSKRTSwlnalavislidietnRSRSNEIKKQLNDLESRLQEIEI 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1903 ALKAKEAENERLKRKAEDEAY----QRKLLEDQAAQhKHDIQEKIIHLKSSSDSEMVRQKTIVEETLRQKKIvEEEIHII 1978
Cdd:PRK01156 609 GFPDDKSYIDKSIREIENEANnlnnKYNEIQENKIL-IEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDI-EDNLKKS 686
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 736215636 1979 RINFEKASKGKSDLENELKKLKVIAEETQKSKLKAEAEAEKLKKLAA 2025
Cdd:PRK01156 687 RKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1549-2002 |
1.63e-09 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 64.69 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1549 KQVAEETQKKKNAedelkrKSEAEKEAAKQKQKALDDLQkfkmQAEEAERRMKQAEeeklrqiKVVEEVAQKSAATQLQS 1628
Cdd:PRK10929 26 KQITQELEQAKAA------KTPAQAEIVEALQSALNWLE----ERKGSLERAKQYQ-------QVIDNFPKLSAELRQQL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1629 HSMSFNVKASKLEESLKKEQGTVLQLQEE-AEQLRKQQEEANKAREQAEkELETWRQKANEALRLRLQAEEEAQKKSKTQ 1707
Cdd:PRK10929 89 NNERDEPRSVPPNMSTDALEQEILQVSSQlLEKSRQAQQEQDRAREISD-SLSQLPQQQTEARRQLNEIERRLQTLGTPN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1708 EEAERQKVEAerdakkrAKAEDAALKQKDNaekELEkqrtfaeqVAQqkLSA--EQECIRLKADFDHAEQQRglLDNELQ 1785
Cdd:PRK10929 168 TPLAQAQLTA-------LQAESAALKALVD---ELE--------LAQ--LSAnnRQELARLRSELAKKRSQQ--LDAYLQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1786 RLKKEVSATEKQrkllEEELAKVRSEMDSllkmkteaekktmsntEKSKQLLESealkmkqLADEATRLRSVAEEAKKQR 1865
Cdd:PRK10929 226 ALRNQLNSQRQR----EAERALESTELLA----------------EQSGDLPKS-------IVAQFKINRELSQALNQQA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1866 QTAEEEAARQRAEAEKIL--KEKLAAINEATRLRTEAEIALKAKEAENERLkrkAEDEAYQRklLEDQAAQ------HKH 1937
Cdd:PRK10929 279 QRMDLIASQQRQAASQTLqvRQALNTLREQSQWLGVSNALGEALRAQVARL---PEMPKPQQ--LDTEMAQlrvqrlRYE 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736215636 1938 DIQEKIIHLKSSsdsemvRQKTIVEETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKVI 2002
Cdd:PRK10929 354 DLLNKQPQLRQI------RQADGQPLTAEQNRILDAQLRTQRELLNSLLSGGDTLILELTKLKVA 412
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1642-2025 |
1.75e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1642 ESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKAnEALRLRLQAEEEAQKKSKTQEEAERQKVEAERdA 1721
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL-EKLEKLLQLLPLYQELEALEAELAELPERLEE-L 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1722 KKRAKAEDAALKQKDNAEKEL-EKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKL 1800
Cdd:COG4717 152 EERLEELRELEEELEELEAELaELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1801 LEEE---------------LAKVRSEMDSLLKMKTEAEKKT-----------------MSNTEKSKQLLESEALKMKQLA 1848
Cdd:COG4717 232 LENEleaaaleerlkearlLLLIAAALLALLGLGGSLLSLIltiagvlflvlgllallFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1849 DEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEA--YQRK 1926
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1927 LLEDQAAQHKHDIQEKIIHLKSSSDSEMVRQKTIVEETLRQK-KIVEEEIHIIRINFEKASKGKSDLENELKKL------ 1999
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLeedgel 471
|
410 420
....*....|....*....|....*...
gi 736215636 2000 --KVIAEETQKSKLKAEAEAEKLKKLAA 2025
Cdd:COG4717 472 aeLLQELEELKAELRELAEEWAALKLAL 499
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4359-4393 |
2.04e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 55.57 E-value: 2.04e-09
10 20 30
....*....|....*....|....*....|....*
gi 736215636 4359 QRLLEAQACTGGIIDPNTGEKFTVTDAMNKGLVDK 4393
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDP 35
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3515-3549 |
2.10e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 55.41 E-value: 2.10e-09
10 20 30
....*....|....*....|....*....|....*
gi 736215636 3515 LLEAQFSTGGIIDPVSSHRVPNDVAIQRGYCSKQM 3549
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPET 35
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2201-2455 |
2.20e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 62.93 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2201 QADAEMAKHKKEADQALKLKSQVEKEltmvklrLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELL 2280
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAE-------LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2281 KlklKIEEQNRSLMKKDKDKTQKVLAEEAgkmKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMlKEKMQAIQE 2360
Cdd:COG3883 86 E---ELGERARALYRSGGSVSYLDVLLGS---ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKK-AELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2361 ATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAEN 2440
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
250
....*....|....*
gi 736215636 2441 EAKKFKKQADEAKAR 2455
Cdd:COG3883 239 AAAAAASAAGAGAAG 253
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4015-4053 |
2.50e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 55.41 E-value: 2.50e-09
10 20 30
....*....|....*....|....*....|....*....
gi 736215636 4015 LLEAQAATGYVIDPIKNLKLNVTEAVKMSVVGPEFKDKL 4053
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4437-4475 |
2.84e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 55.03 E-value: 2.84e-09
10 20 30
....*....|....*....|....*....|....*....
gi 736215636 4437 FLEVQYLTGGLIEPDATSRVSIDEAVKKGSLDARTAQKL 4475
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2409-2669 |
2.94e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2409 AERKRQLEVSA---EAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQStETVVQKLETQRLQSTREADGL 2485
Cdd:COG1196 212 AERYRELKEELkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL-EELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2486 KEAIADLEKEREKLKKEAEELQNKSNKMANTQKEEIEQQKAIIQKSfiSERELLLKRQKAVEDEKKKLQKQFEDEVKKAE 2565
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE--EELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2566 ALKDEQERQRKLMEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEKKRLDQEKQLGAENQKLREKLQCLEGASKQS 2645
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260
....*....|....*....|....
gi 736215636 2646 ATKQVASKTIEVQTDVVSEEQLVT 2669
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEA 472
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1538-1778 |
3.74e-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: 61.79 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1538 KAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKfKMQAEEAERRMKQAEEEKLRQIKVVEEV 1617
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQ-RAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1618 AQKSAATQLQshsmsfnvkaskleeslkkeqgtvlqlQEEAEQLRKQQEEAnkareqaEKeletwrqkanealrlrlQAE 1697
Cdd:TIGR02794 125 KAKQAAEAKA---------------------------KAEAEAERKAKEEA-------AK-----------------QAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1698 EEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQR 1777
Cdd:TIGR02794 154 EEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAE 233
|
.
gi 736215636 1778 G 1778
Cdd:TIGR02794 234 L 234
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2146-2482 |
3.86e-09 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 62.85 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2146 LRQKAAEAEKQKKSAEEEA------AKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHK--------- 2210
Cdd:pfam09731 97 VSSEVAEEEKEATKDAAEAkaqlpkSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKeasdtaeis 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2211 --KEADQALKLKSQVEKEL--TMVKLRLDETDKQKALLDEELQRVKGEVN--DAVKQKAQVEDELAKVriqMDELLKLKL 2284
Cdd:pfam09731 177 reKATDSALQKAEALAEKLkeVINLAKQSEEEAAPPLLDAAPETPPKLPEhlDNVEEKVEKAQSLAKL---VDQYKELVA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2285 KIEEQNRSLMKKDKDKTQKVLAEeaGKMKSLAEEAARL-SVEAEETARQRQIAESNLAEQRAlAEKMLKEkmqaiQEATK 2363
Cdd:pfam09731 254 SERIVFQQELVSIFPDIIPVLKE--DNLLSNDDLNSLIaHAHREIDQLSKKLAELKKREEKH-IERALEK-----QKEEL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2364 LKAEAQELQKQKDqaqekakKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLK-----------VKELS 2432
Cdd:pfam09731 326 DKLAEELSARLEE-------VRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKdvlveqeielqREFLQ 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 736215636 2433 DAQSKAENEAKKFKKQADEAKARLKDTEKQST---ETVVQKLETQRLQSTREA 2482
Cdd:pfam09731 399 DIKEKVEEERAGRLLKLNELLANLKGLEKATSshsEVEDENRKAQQLWLAVEA 451
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1474-2024 |
3.99e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.12 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1474 KSLSEQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEM-------TIKQKKTAESELQQLRDKAAEAEKlrKAAQEDAER 1546
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKlnnkyndLKKQKEELENELNLLEKEKLNIQK--NIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1547 LRKQ-----VAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEklrQIKVVEEVAQKs 1621
Cdd:TIGR04523 197 LKLElllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE---QNKIKKQLSEK- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1622 aatqlQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQ-----LRKQQEEANKAREQAEKELETWRQKANEalrlrLQA 1696
Cdd:TIGR04523 273 -----QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISQNNKIISQ-----LNE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1697 EEEAQKKSKTQEEAERQKVEAErdakkrakaedaaLKQKDNAEKELEKQRtfaEQVAQQKLSAEQECIRLKADFDHAEQQ 1776
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRE-------------LEEKQNEIEKLKKEN---QSYKQEIKNLESQINDLESKIQNQEKL 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1777 RGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKtmsnTEKSKQLLESEALKMKQLADEATRLRS 1856
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI----IKNLDNTRESLETQLKVLSRSINKIKQ 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1857 VAEEAKKQRQTAEEE------AARQRAEAEKILKEKLAAINEATRlRTEAEIALKAKEAENERLKRKAEDEAYQRKLLED 1930
Cdd:TIGR04523 483 NLEQKQKELKSKEKElkklneEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISDLEDELNKDDFELKKENLEK 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1931 QaaqhKHDIQEKIIHLKSSSDSEMVRQKTIvEETLRQKkivEEEIHIIRINFEKASKGKSDLENELKKLKVIAEETQKSK 2010
Cdd:TIGR04523 562 E----IDEKNKEIEELKQTQKSLKKKQEEK-QELIDQK---EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
570
....*....|....
gi 736215636 2011 LKAEAEAEKLKKLA 2024
Cdd:TIGR04523 634 KNIKSKKNKLKQEV 647
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2343-2634 |
4.06e-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: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2343 QRALAEKMLKEKMQAIqEATKLKAEAQELQKQkdqaQEKAKKLLEDKQQIQQRLDKetegfQKSLEAERKR-QLEVSAEA 2421
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKEEKARE----VERRRKLEEAEKARQAEMDR-----QAAIYAEQERmAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2422 ETLRLKVKELSDAQSKAENEAKKFKKQADeaKARLKDTEKQSTETVVQKLETQRLQSTREADGLKEAIADLEKEREKLKK 2501
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAMEISRMRE--LERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2502 EAEELQNKSNKMANTQKEEIEQQkaiiqksfiseRELLLKRQKAVEdekkKLQKQFEDEVKKAEALKDEQERQRKLMEEE 2581
Cdd:pfam17380 429 QEEARQREVRRLEEERAREMERV-----------RLEEQERQQQVE----RLRQQEEERKRKKLELEKEKRDRKRAEEQR 493
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 736215636 2582 KKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEKKRLDQEKQLGAENQKLREK 2634
Cdd:pfam17380 494 RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQ 546
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1655-1881 |
4.16e-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: 62.09 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1655 QEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQ 1734
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1735 KDNAEKELEKQRTFAEQVAQQK-----LSAE--QECIR----LKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEE 1803
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPplallLSPEdfLDAVRrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 1804 ELAKVRSEMDSLLKMKTEaEKKTMSNTEKSKQLLESEAlkmKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEK 1881
Cdd:COG4942 179 LLAELEEERAALEALKAE-RQKLLARLEKELAELAAEL---AELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2147-2384 |
4.50e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 63.04 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2147 RQKAAEA-----EKQKKSAEEEAAKQAKAQKDAEKLKKA---------AEEEASKRAAAEAEALKQKKQADAEMAKHKKE 2212
Cdd:PRK05035 445 KKKAEEAkarfeARQARLEREKAAREARHKKAAEARAAKdkdavaaalARVKAKKAAATQPIVIKAGARPDNSAVIAARE 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2213 ADQALKLKSQVEKELTmvklrlDETDKQKALLDEELQRVKGevndavkQKAQVEDELAKVRiqmDELLKLKLKIEEQnrs 2292
Cdd:PRK05035 525 ARKAQARARQAEKQAA------AAADPKKAAVAAAIARAKA-------KKAAQQAANAEAE---EEVDPKKAAVAAA--- 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2293 lMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQR-QIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQEL 2371
Cdd:PRK05035 586 -IARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKaKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQ 664
|
250
....*....|...
gi 736215636 2372 QKQKDQAQEKAKK 2384
Cdd:PRK05035 665 ANAEPEEAEDPKK 677
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2233-2639 |
4.93e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2233 RLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQNRSLMKKDKDKtQKVLAEEAGKM 2312
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK-RKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2313 KSLAEEAARLSVEAEETARQRQIAESNLA--EQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEdkq 2390
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE--- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2391 qiqqrLDKETEGFQKSLEAERKRQlevsaeaetlrlkvkelsdaqsKAENEAKKFKKQADEAKARLKDTEKQSTETVVQK 2470
Cdd:PRK03918 343 -----LKKKLKELEKRLEELEERH----------------------ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2471 LETQRLQSTREADGLKEAIADLEKEREKLKKEAEELQNKSNKMANTQKEEIEQQKAIIQKSFISERELLLKRQKAVEDEK 2550
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2551 KKLQKQFEdEVKKAEALKDEQERQRKLMEEEK---KKLQAIMDAAVKKQKEAEADMKNK----QTEMEVLeKKRLDQEKQ 2623
Cdd:PRK03918 476 RKLRKELR-ELEKVLKKESELIKLKELAEQLKeleEKLKKYNLEELEKKAEEYEKLKEKliklKGEIKSL-KKELEKLEE 553
|
410
....*....|....*.
gi 736215636 2624 LGAENQKLREKLQCLE 2639
Cdd:PRK03918 554 LKKKLAELEKKLDELE 569
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2086-2257 |
5.34e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 61.75 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2086 VAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAE-KQKKSAEEEA 2164
Cdd:PRK09510 84 KEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEaKRAAAAAKKA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2165 AKQAKAQKDAEKLKKA-------AEEEASKRAAAEAE--ALKQKKQADAEMAKHKKEADQALKlksqVEKELTMVKLRLD 2235
Cdd:PRK09510 164 AAEAKKKAEAEAAKKAaaeakkkAEAEAAAKAAAEAKkkAEAEAKKKAAAEAKKKAAAEAKAA----AAKAAAEAKAAAE 239
|
170 180
....*....|....*....|..
gi 736215636 2236 ETDKQKALLDEELQRVKGEVND 2257
Cdd:PRK09510 240 KAAAAKAAEKAAAAKAAAEVDD 261
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1309-2000 |
5.37e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 62.73 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1309 NKDKIDSCQKNAKAYIDSVKDYELQILTYKALQDPMASPLKKPKmdcasDNIIQEYVTLRTRYSELMTLTSQYIKFITET 1388
Cdd:TIGR04523 94 NKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENK-----KNIDKFLTEIKKKEKELEKLNNKYNDLKKQK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1389 QrRLEDDEKASEKLKEEERKKMAEIQAELDKQKQIAeaqakSVIKA-EQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQ 1467
Cdd:TIGR04523 169 E-ELENELNLLEKEKLNIQKNIDKIKNKLLKLELLL-----SNLKKkIQKNKSLESQISELKKQNNQLKDNIEKKQQEIN 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1468 HElhhlkslsEQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRdkaAEAEKLRKAAQEDaerL 1547
Cdd:TIGR04523 243 EK--------TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK---SEISDLNNQKEQD---W 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1548 RKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQ--KSAATQ 1625
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQsyKQEIKN 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1626 LQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWrqkanealrlrlqaeeeaqKKSK 1705
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL-------------------TNQD 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1706 TQEEAERQKVEAERDAKKrakaedaalKQKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKadfdhaeQQRGLLDNELQ 1785
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLE---------TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN-------EEKKELEEKVK 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1786 RLKKEVSATEKQRKLLEEELAKVRSEMDSLlkmktEAEKKTMsNTEKSKQLLESEALKMKQladEATRLRSVAEEAKKQR 1865
Cdd:TIGR04523 514 DLTKKISSLKEKIEKLESEKKEKESKISDL-----EDELNKD-DFELKKENLEKEIDEKNK---EIEELKQTQKSLKKKQ 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1866 QTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIAlkakEAENERL----------KRKAEDEAYQRKLLEDQAAQH 1935
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA----KKENEKLssiiknikskKNKLKQEVKQIKETIKEIRNK 660
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736215636 1936 KHDIQEKIIHLKSSSDSEMVRQKTIVEET-LRQKKIVEEEIHIirINFEKASKGKSDLENELKKLK 2000
Cdd:TIGR04523 661 WPEIIKKIKESKTKIDDIIELMKDWLKELsLHYKKYITRMIRI--KDLPKLEEKYKEIEKELKKLD 724
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1477-1726 |
6.69e-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: 61.32 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1477 SEQEIKSKSQQLEhalvshtKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQ 1556
Cdd:COG4942 18 QADAAAEAEAELE-------QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1557 KKKNAEDELKRKSE--AEKEAAKQKQKALDDLqKFKMQAEEAErrmkqaeeEKLRQIKVVEEV--AQKSAATQLQSHSMS 1632
Cdd:COG4942 91 EIAELRAELEAQKEelAELLRALYRLGRQPPL-ALLLSPEDFL--------DAVRRLQYLKYLapARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1633 FNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEalrLRLQAEEEAQKKSKTQEEAER 1712
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE---LQQEAEELEALIARLEAEAAA 238
|
250
....*....|....
gi 736215636 1713 QKVEAERDAKKRAK 1726
Cdd:COG4942 239 AAERTPAAGFAALK 252
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2175-2641 |
6.91e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.44 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2175 EKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGE 2254
Cdd:pfam15921 285 EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2255 VNDAVKQKAQVEDELAKVRIQMDELLKlKLKIE-EQNRSLMKKDKDKTQKVlaeeagkmkslaeeaARLSVEAEETARQR 2333
Cdd:pfam15921 365 RDQFSQESGNLDDQLQKLLADLHKREK-ELSLEkEQNKRLWDRDTGNSITI---------------DHLRRELDDRNMEV 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2334 QIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLED---KQQIQQRLDKETEGFQKSLEaE 2410
Cdd:pfam15921 429 QRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEltaKKMTLESSERTVSDLTASLQ-E 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2411 RKRQLEVS-AEAETLR----LKVKELSDAQskaeNEAKKFKKQADEAKA-RLKDTEKQST-ETVVQKLE--TQRL-QSTR 2480
Cdd:pfam15921 508 KERAIEATnAEITKLRsrvdLKLQELQHLK----NEGDHLRNVQTECEAlKLQMAEKDKViEILRQQIEnmTQLVgQHGR 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2481 EADGLKeaiadlekereklkkeaeELQNKSNKMANTQKEEIEQQKAIIQKSFISERElLLKRQKAVEDEKKKLQKQFEDE 2560
Cdd:pfam15921 584 TAGAMQ------------------VEKAQLEKEINDRRLELQEFKILKDKKDAKIRE-LEARVSDLELEKVKLVNAGSER 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2561 VKKAEALKdeQERQRKLmeEEKKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEKKRLDQEKQLGAENQKLREKLQCLEG 2640
Cdd:pfam15921 645 LRAVKDIK--QERDQLL--NEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG 720
|
.
gi 736215636 2641 A 2641
Cdd:pfam15921 721 S 721
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
57-156 |
7.24e-09 |
|
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: 56.36 E-value: 7.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 57 QKKTFTKWVNKHLMKSqrHITDLYEDLRDGHNLISLLEVLSGETLPREKG-----RMRFHKLQNVQIALDFLKHRQVKLV 131
Cdd:cd21299 5 EERCFRLWINSLGIDT--YVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 736215636 132 NIRNDDIADGNPKLTLGLIWTIILH 156
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2092-2425 |
7.74e-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: 62.06 E-value: 7.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2092 QKCSSAEQKAQEVLSKNKED---SLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAE---AEKQKKSAE---- 2161
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEkarEVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELErirQEERKRELErirq 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2162 EEAAKQAKAQKDAEKLKKAAE----------EEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQV---EKELT 2228
Cdd:pfam17380 368 EEIAMEISRMRELERLQMERQqknervrqelEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRleeERARE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2229 MVKLRLDETDKQkalldEELQRVKgevndavkqkaQVEDELAKVRIQMDELLKLKLKIEEQNRSLMKKDKdktqkvlaeE 2308
Cdd:pfam17380 448 MERVRLEEQERQ-----QQVERLR-----------QQEEERKRKKLELEKEKRDRKRAEEQRRKILEKEL---------E 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2309 AGKMKSLAEEAARLSVEAEETARQRQIAESnlaEQRALAEKMLKEKmqaiqeatklkaeaQELQKQKdQAQEKAKKLLED 2388
Cdd:pfam17380 503 ERKQAMIEEERKRKLLEKEMEERQKAIYEE---ERRREAEEERRKQ--------------QEMEERR-RIQEQMRKATEE 564
|
330 340 350
....*....|....*....|....*....|....*...
gi 736215636 2389 KQQIQQrLDKETEGFQKSLEAERKRQ-LEVSAEAETLR 2425
Cdd:pfam17380 565 RSRLEA-MEREREMMRQIVESEKARAeYEATTPITTIK 601
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1491-1948 |
7.88e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 7.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1491 ALVSH----TKIEEEIHTIRIQLEM---------TIKQKKTAESELQQLRDKAA--EAEKLRKAAQEDAERLRKQVAEET 1555
Cdd:COG4913 229 ALVEHfddlERAHEALEDAREQIELlepirelaeRYAAARERLAELEYLRAALRlwFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1556 QKKKNAEDELKRKSEAEKEAAKQKQKA----LDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAAtqlqshsm 1631
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE-------- 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1632 SFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKAN----EALRLRLQAEEEAQKKS--- 1704
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEael 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1705 ---------KTQEE-----AER----------------------------------QKVEAERDAKKRAKAEDAALKQK- 1735
Cdd:COG4913 461 pfvgelievRPEEErwrgaIERvlggfaltllvppehyaaalrwvnrlhlrgrlvyERVRTGLPDPERPRLDPDSLAGKl 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1736 --------DNAEKELEKQRTFA-----EQVAQQKLSAEQECI------RLKADFDHAEQQRGLL--DNE--LQRLKKEVS 1792
Cdd:COG4913 541 dfkphpfrAWLEAELGRRFDYVcvdspEELRRHPRAITRAGQvkgngtRHEKDDRRRIRSRYVLgfDNRakLAALEAELA 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1793 ATEKQRKLLEEELAKVRSEMDSLLKMKTEAEK-KTMSNTEKSKQLLESE-ALKMKQLA------DEATRLRSVAEEAKKQ 1864
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRlAEYSWDEIDVASAEREiAELEAELErldassDDLAALEEQLEELEAE 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1865 RQTAEEEAARQRAEAEKILKEklaaINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKII 1944
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERID 776
|
....
gi 736215636 1945 HLKS 1948
Cdd:COG4913 777 ALRA 780
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1519-1761 |
7.88e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 61.89 E-value: 7.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1519 AESELQQLRDKAAEAE--KLRKAAQEdaERLRKQVAEETQKKKNAEDELKRKSEAEKEAA----KQKQKALDDLQKFKMQ 1592
Cdd:PRK05035 434 AKAEIRAIEQEKKKAEeaKARFEARQ--ARLEREKAAREARHKKAAEARAAKDKDAVAAAlarvKAKKAAATQPIVIKAG 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1593 AEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQSHSMSFNVKASKLEeslKKEQGTVLQLQEEAEQLRKQQEEANKAR 1672
Cdd:PRK05035 512 ARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAK---KAAQQAANAEAEEEVDPKKAAVAAAIAR 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1673 EQAEK--------------ELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNA 1738
Cdd:PRK05035 589 AKAKKaaqqaasaepeeqvAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAE 668
|
250 260
....*....|....*....|....*..
gi 736215636 1739 EKELEKQR--TFAEQVA--QQKLSAEQ 1761
Cdd:PRK05035 669 PEEAEDPKkaAVAAAIAraKAKKAAQQ 695
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1802-2428 |
8.05e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1802 EEELAKVRSEmdslLKMKTEAEKKTMSNTEKSKQLLesealkmKQLADEATR-LRSVAEEAKKQRQTAEE-EAARQRAEA 1879
Cdd:PRK03918 164 YKNLGEVIKE----IKRRIERLEKFIKRTENIEELI-------KEKEKELEEvLREINEISSELPELREElEKLEKEVKE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1880 EKILKEKLAAINEATRLRTEAEIALKAK--EAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKsssdSEMVRQ 1957
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKirELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFY----EEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1958 KTIVEETLrqkKIVEEEIHIIRINFEKASKGKSDLENELKKLKVIAEETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEK 2037
Cdd:PRK03918 309 LREIEKRL---SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2038 VKRITAAEEEAARqckaAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSS-----AEQKAQEVLSKNKEDS 2112
Cdd:PRK03918 386 PEKLEKELEELEK----AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVcgrelTEEHRKELLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2113 LAQQKMKEEFENAKR-LAQAAEKAKEKAEKEAALLRQKaaEAEKQKKSAEEEAAKQakaqkDAEKLKKAAEE-----EAS 2186
Cdd:PRK03918 462 KRIEKELKEIEEKERkLRKELRELEKVLKKESELIKLK--ELAEQLKELEEKLKKY-----NLEELEKKAEEyeklkEKL 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2187 KRAAAEAEALKQKKQADAEMAKHKKEADQALKlksQVEKELTMVKLRLDETD-KQKALLDEELQRVKG------EVNDAV 2259
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLEELKKKLAELEKKLD---ELEEELAELLKELEELGfESVEELEERLKELEPfyneylELKDAE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2260 KQKAQVEDELAKVRIQMD----ELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQI 2335
Cdd:PRK03918 612 KELEREEKELKKLEEELDkafeELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREE 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2336 AESNLaeqralaeKMLKEKMQAIQEAtklKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAE---RK 2412
Cdd:PRK03918 692 IKKTL--------EKLKEELEEREKA---KKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASEIFEElteGK 760
|
650
....*....|....*..
gi 736215636 2413 RQ-LEVSAEAETLRLKV 2428
Cdd:PRK03918 761 YSgVRVKAEENKVKLFV 777
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1518-1763 |
8.84e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 8.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1518 TAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAE 1597
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1598 RRMKQAEeeklRQIKVVEEVaqksaatqLQSHSMS-FNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAE 1676
Cdd:COG3883 93 RALYRSG----GSVSYLDVL--------LGSESFSdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1677 KELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQK 1756
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
....*..
gi 736215636 1757 LSAEQEC 1763
Cdd:COG3883 241 AAAASAA 247
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1634-1796 |
9.12e-09 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 61.56 E-value: 9.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1634 NVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKanealrlrLQAEEEAQKKSKTQEE---- 1709
Cdd:pfam05262 202 DLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQK--------QQEAKNLPKPADTSSPkedk 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1710 --AERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKlsaeqecirlkadfdHAEQQRGLLD--NELQ 1785
Cdd:pfam05262 274 qvAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDK---------------ELEAQKKREPvaEDLQ 338
|
170
....*....|.
gi 736215636 1786 RLKKEVSATEK 1796
Cdd:pfam05262 339 KTKPQVEAQPT 349
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1382-1624 |
9.17e-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: 62.06 E-value: 9.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1382 IKFITETQR-RLEDDEKASEKLKEEERKKMAEIQAELDKQKQIAEAQAKSVIKAEQE-AQELKLKMKEEASKRQDVAVDA 1459
Cdd:pfam17380 374 ISRMRELERlQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEeARQREVRRLEEERAREMERVRL 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1460 EQQKQniQHELHHLKSlSEQEIKSKSQQLEHALVSHTKIEEEihtiriqlemtikQKKTAESELQQLRDKAAEAEKLRKA 1539
Cdd:pfam17380 454 EEQER--QQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQ-------------RRKILEKELEERKQAMIEEERKRKL 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1540 AQEDAERLRKQVAEEtQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMkqaeeekLRQIKVVEEVAQ 1619
Cdd:pfam17380 518 LEKEMEERQKAIYEE-ERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREM-------MRQIVESEKARA 589
|
....*
gi 736215636 1620 KSAAT 1624
Cdd:pfam17380 590 EYEAT 594
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1419-1813 |
9.19e-09 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 62.13 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1419 KQKQIAEAQAkSVIKAEQEAQELKLKMkeeASKRQdvavdaeQQKQNIQHeLHHLKSLSEQEIKSKSQQLEHALV----- 1493
Cdd:PRK10246 438 QQKRLAQLQV-AIQNVTQEQTQRNAAL---NEMRQ-------RYKEKTQQ-LADVKTICEQEARIKDLEAQRAQLqagqp 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1494 -------SHTKIEeeihtiriqlemtikQKKTAESELQQLRDKAAEAEKlrKAAQEDAERLRKQVAEETQKKKNAEDELK 1566
Cdd:PRK10246 506 cplcgstSHPAVE---------------AYQALEPGVNQSRLDALEKEV--KKLGEEGAALRGQLDALTKQLQRDESEAQ 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1567 RKSEAEKEAAKQKQKAL----------DDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAAT-QLQSHSMSFNV 1635
Cdd:PRK10246 569 SLRQEEQALTQQWQAVCaslnitlqpqDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQqQIEQRQQQLLT 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1636 KASKLEESLKKEQGTVLQL---QEEAEQLRKQQEEANKAREQ---------------------AEKELETWRQKANEALR 1691
Cdd:PRK10246 649 ALAGYALTLPQEDEEASWLatrQQEAQSWQQRQNELTALQNRiqqltplletlpqsddlphseETVALDNWRQVHEQCLS 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1692 LrlQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAED------AAL----------KQKDNAEKELEKQRTFAEQVAQQ 1755
Cdd:PRK10246 729 L--HSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDdqqaflAALldeetltqleQLKQNLENQRQQAQTLVTQTAQA 806
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736215636 1756 ---KLSAEQECIRLKADFDHAEQQRGLLDNEL-----------QRLKKEVSATEKQRKLLeEELAKVRSEMD 1813
Cdd:PRK10246 807 laqHQQHRPDGLDLTVTVEQIQQELAQLAQQLrenttrqgeirQQLKQDADNRQQQQALM-QQIAQATQQVE 877
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1195-1850 |
9.86e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1195 DRLQDELRRASTINDKMtrihSERDAEMEHYRQLVSSLLERWQVVFAQMDMRQRELDLLGRHMNSYNVSYEWLIHWLGEA 1274
Cdd:PRK03918 179 ERLEKFIKRTENIEELI----KEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1275 RKRQEKIqavpiggsKALREQLAEEKKLLEEIEKNKDKIDSCQKNAKAYIDsvkdyelqiltykalqdpmasplkkpkmd 1354
Cdd:PRK03918 255 RKLEEKI--------RELEERIEELKKEIEELEEKVKELKELKEKAEEYIK----------------------------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1355 casdnIIQEYVTLRTRYSELMTLTSQYIKFITETQRRLEDDEKaseklkeeerkkmaeiqaeldkqkqiAEAQAKSVIKA 1434
Cdd:PRK03918 298 -----LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE--------------------------KEERLEELKKK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1435 EQEAQELKLKMKEEASKRQdvavDAEQQKQNIQHELHHLKSLSEQEIKSKSQQLEHAlvsHTKIEEEIHTI---RIQLEM 1511
Cdd:PRK03918 347 LKELEKRLEELEERHELYE----EAKAKKEELERLKKRLTGLTPEKLEKELEELEKA---KEEIEEEISKItarIGELKK 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1512 TIKQKKTAESELQQLRDKAAEAEklRKAAQEDAERLrkqVAEETQKKKNAEDELKRKSEAEKEAAKQKQKalddLQKFKM 1591
Cdd:PRK03918 420 EIKELKKAIEELKKAKGKCPVCG--RELTEEHRKEL---LEEYTAELKRIEKELKEIEEKERKLRKELRE----LEKVLK 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1592 QAEEAERRMKQAE-----EEKLRQIKVVEEVAQKSAATQLQSHSMSFNVKASKLEESLKKEQGtvlqLQEEAEQLRKQQE 1666
Cdd:PRK03918 491 KESELIKLKELAEqlkelEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLD 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1667 EANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQR 1746
Cdd:PRK03918 567 ELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELR 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1747 TFAEQvAQQKLSAEqecirlkaDFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEK-- 1824
Cdd:PRK03918 647 KELEE-LEKKYSEE--------EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKle 717
|
650 660 670
....*....|....*....|....*....|....
gi 736215636 1825 KTMSNTE-------KSKQLLESEAL-KMKQLADE 1850
Cdd:PRK03918 718 KALERVEelrekvkKYKALLKERALsKVGEIASE 751
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2087-2225 |
1.52e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 59.86 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2087 AKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEfenakRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAK 2166
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQ-----RAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKA 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736215636 2167 QAKA-QKDAEKLKKAAEEEASKRAAAEA--EALKQKKQADAEmAKHKKEADQALKLKSQVEK 2225
Cdd:TIGR02794 137 EAEAeRKAKEEAAKQAEEEAKAKAAAEAkkKAEEAKKKAEAE-AKAKAEAEAKAKAEEAKAK 197
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1424-1678 |
1.69e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1424 AEAQAKSVIKAEQEAQELKLKMKEEASKRQDvavdAEQQKQNIQHELHHLkslsEQEIKSKSQQLEhalvshtKIEEEIH 1503
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAA----LKKEEKALLKQLAAL----ERRIAALARRIR-------ALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1504 TIRIQLEMTIKQKKTAESELQQLRDKAAE-AEKLRKAAQEDAERLRKQVAEETQKKKNAEDeLKRKSEAEKEAAKQKQKA 1582
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1583 LDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEevAQKSAATQLQShsmsfnvkasKLEESLKKEQGTVLQLQEEAEQLR 1662
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALE--ALKAERQKLLA----------RLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*.
gi 736215636 1663 KQQEEANKAREQAEKE 1678
Cdd:COG4942 227 ALIARLEAEAAAAAER 242
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1654-2273 |
1.88e-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: 60.81 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1654 LQEEAEQLRKQQEEANKAREQAEKELETWRqKANEALRLRLQaeeeaqkksKTQEEAERQKVEAERdAKKRAkaedaalk 1733
Cdd:pfam05701 47 VQEEIPEYKKQSEAAEAAKAQVLEELESTK-RLIEELKLNLE---------RAQTEEAQAKQDSEL-AKLRV-------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1734 qkdnaeKELEKQRTFAEQVAqqklsaeqecirlkadfdhAEQQrglLDNELQRLKKEVSatekQRKLLEEELAKVRSEMD 1813
Cdd:pfam05701 108 ------EEMEQGIADEASVA-------------------AKAQ---LEVAKARHAAAVA----ELKSVKEELESLRKEYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1814 SLLKMKTEAEKKTMSNTEKSKQL------LESEALKMKQLADEAtrlRSVAEEAKKQRQTAEEEAARQRAEAEKILKEkl 1887
Cdd:pfam05701 156 SLVSERDIAIKRAEEAVSASKEIektveeLTIELIATKESLESA---HAAHLEAEEHRIGAALAREQDKLNWEKELKQ-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1888 aAINEATRLRTEAEIA--LKAKEAENERL--KRKAEDEAYQRKLLEDQAAQHKHDiqekiihLKSSSDSEMVRQKTivee 1963
Cdd:pfam05701 231 -AEEELQRLNQQLLSAkdLKSKLETASALllDLKAELAAYMESKLKEEADGEGNE-------KKTSTSIQAALASA---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1964 tlrqKKIVEEeihiIRINFEKASkgksdleNELKKLKVIAeetqkSKLKAEAEAEK-----LKKLAAEEEKKRKESEEKV 2038
Cdd:pfam05701 299 ----KKELEE----VKANIEKAK-------DEVNCLRVAA-----ASLRSELEKEKaelasLRQREGMASIAVSSLEAEL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2039 KRITAAEEEAARQCKAAQEEVARLEKKADEAnkqkekaekeaekqvivAKEAAQKCSSAeQKAQEVLsknkedslaqQKM 2118
Cdd:pfam05701 359 NRTKSEIALVQAKEKEAREKMVELPKQLQQA-----------------AQEAEEAKSLA-QAAREEL----------RKA 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2119 KEEFENAKRLAQAAEKAKEKAekeaallrQKAAEAekqKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKR----AAAEAE 2194
Cdd:pfam05701 411 KEEAEQAKAAASTVESRLEAV--------LKEIEA---AKASEKLALAAIKALQESESSAESTNQEDSPRgvtlSLEEYY 479
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 2195 ALkQKKQADAEMAKHKKEADQALKLKSQVEKELTMVKlRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVR 2273
Cdd:pfam05701 480 EL-SKRAHEAEELANKRVAEAVSQIEEAKESELRSLE-KLEEVNREMEERKEALKIALEKAEKAKEGKLAAEQELRKWR 556
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1478-1806 |
2.71e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.74 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1478 EQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLemtikqkKTAESELQQLRDKAAEAEKL-RKAAQEDAERLRKQVAEETQ 1556
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQL-------EQAKEGLSALNRLLPRLNLLaDETLADRVEEIREQLDEAEE 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1557 KKKNAEDELKRKSEAEKEAAK--QKQKALDDLQKFKMQAEEAERRMKQaeeeklrQIKVVEEVAQKSAAtqlqshsmsfn 1634
Cdd:PRK04863 909 AKRFVQQHGNALAQLEPIVSVlqSDPEQFEQLKQDYQQAQQTQRDAKQ-------QAFALTEVVQRRAH----------- 970
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1635 VKASKLEESLKKEQGTVlqlqeeaEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQ- 1713
Cdd:PRK04863 971 FSYEDAAEMLAKNSDLN-------EKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEl 1043
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1714 ---KVEAERDAKKRAKAE----DAALKQKDNAEKELEKQRTFAE---QVAQQKLSAEQECIRLKADFdhAEQQRGLLDNE 1783
Cdd:PRK04863 1044 qdlGVPADSGAEERARARrdelHARLSANRSRRNQLEKQLTFCEaemDNLTKKLRKLERDYHEMREQ--VVNAKAGWCAV 1121
|
330 340
....*....|....*....|...
gi 736215636 1784 LQRLKKevSATEkqRKLLEEELA 1806
Cdd:PRK04863 1122 LRLVKD--NGVE--RRLHRRELA 1140
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1411-1675 |
3.04e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 59.50 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1411 AEIQ-AELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQdvavdaEQQKQNIQhelhhlkslSEQEIKSKSQQLE 1489
Cdd:COG2268 212 TEIAiAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERR------EAETARAE---------AEAAYEIAEANAE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1490 HAlvshtkIEEEIHTIRIQLEMTIKQKKTAESELQQLRD--KAAEAEKLRKAAQEDAErlrkqvAEETQKKKNAEDELKR 1567
Cdd:COG2268 277 RE------VQRQLEIAEREREIELQEKEAEREEAELEADvrKPAEAEKQAAEAEAEAE------AEAIRAKGLAEAEGKR 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1568 kseAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAeeEKLRQIKVVEEVAQKSAATQLQSHSMsfnvkaSKLEESLKKE 1647
Cdd:COG2268 345 ---ALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPL--EKIDKITIIDGGNGGNGAGSAVAEAL------APLLESLLEE 413
|
250 260
....*....|....*....|....*...
gi 736215636 1648 QGtvLQLQEEAEQLRKQQEEANKAREQA 1675
Cdd:COG2268 414 TG--LDLPGLLKGLTGAGAAAPAGEPAE 439
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1655-1840 |
3.38e-08 |
|
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: 59.58 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1655 QEEAEQLRKQQEEANKArEQAEKELETWRQKANEALRLRLQAEEEAQKKsktQEEAERQKVEAERDAKKRAKAEDAALKQ 1734
Cdd:pfam15709 355 REQEEQRRLQQEQLERA-EKMREELELEQQRRFEEIRLRKQRLEEERQR---QEEEERKQRLQLQAAQERARQQQEEFRR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1735 KDNaEKELEKQRTFAEQVAQQKLSAEQECIRLkadfdhAEQQRGLLD-NELQRLkkevsatEKQRKLLEEElAKVRSEMD 1813
Cdd:pfam15709 431 KLQ-ELQRKKQQEEAERAEAEKQRQKELEMQL------AEEQKRLMEmAEEERL-------EYQRQKQEAE-EKARLEAE 495
|
170 180
....*....|....*....|....*..
gi 736215636 1814 SLLKMKTEAEKKTMSNTEKSKQLLESE 1840
Cdd:pfam15709 496 ERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1018-1874 |
3.60e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 60.13 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1018 VPPRAGEQDESVCKTYLTQIKDLRLRL-EGCE--NRTVTRLRQPVdkeplkacalktaeqMKVQSELEGLKKDLNSITEQ 1094
Cdd:pfam15921 68 IAYPGKEHIERVLEEYSHQVKDLQRRLnESNElhEKQKFYLRQSV---------------IDLQTKLQEMQMERDAMADI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1095 TEEVLASQQQissapmLRSELDVTLRKMDHVYGLSSIYLDKLKT-IDVVIRNTKEAEAALKTYESRLLDVNKVpeNEKEV 1173
Cdd:pfam15921 133 RRRESQSQED------LRNQLQNTVHELEAAKCLKEDMLEDSNTqIEQLRKMMLSHEGVLQEIRSILVDFEEA--SGKKI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1174 EEQRS-QLKSMRAEVEADQVIFDRLQDELR----RASTINDKMTRIHSERDAEMEhyrqlvsSLLERWQVVFAQMdMRQR 1248
Cdd:pfam15921 205 YEHDSmSTMHFRSLGSAISKILRELDTEISylkgRIFPVEDQLEALKSESQNKIE-------LLLQQHQDRIEQL-ISEH 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1249 ELDLLGrhmnsynvsyewLIHWLGEARKRQEKIQAVPIGGSKALREQLAEEKKLLEEIEKNKDKIDSCQKNAK-AYIDSV 1327
Cdd:pfam15921 277 EVEITG------------LTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKrMYEDKI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1328 KDYELQILTYKalqdpmaSPLKKPKMDcaSDNIIQEYVTLRTRYSELMTLTSQYIKFIT---ETQRRLEDDEKASEKLKE 1404
Cdd:pfam15921 345 EELEKQLVLAN-------SELTEARTE--RDQFSQESGNLDDQLQKLLADLHKREKELSlekEQNKRLWDRDTGNSITID 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1405 EERKKMAEIQAELDKQKQIAEAQaKSVIKAEQEAQELKLKMKEEA-SKRQDVAVDAEQQKQNIQHELHHLKSL------S 1477
Cdd:pfam15921 416 HLRRELDDRNMEVQRLEALLKAM-KSECQGQMERQMAAIQGKNESlEKVSSLTAQLESTKEMLRKVVEELTAKkmtlesS 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1478 EQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLR-KAAQEDA--ERLRKQVAEE 1554
Cdd:pfam15921 495 ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKviEILRQQIENM 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1555 T----QKKKNAEDELKRKSEAEKEAAKQKQkaldDLQKFKMQAEEAERRMKQAEEE----KLRQIKVVEEVAQKSAATQ- 1625
Cdd:pfam15921 575 TqlvgQHGRTAGAMQVEKAQLEKEINDRRL----ELQEFKILKDKKDAKIRELEARvsdlELEKVKLVNAGSERLRAVKd 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1626 -LQSHSMSFN-VKASKLEESLKKEQGTVLQLQ-----EEAE----QLRKQQEEANKAREQAEKELETWRQKANEALRLRL 1694
Cdd:pfam15921 651 iKQERDQLLNeVKTSRNELNSLSEDYEVLKRNfrnksEEMEtttnKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAM 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1695 QAEEEAQKKsKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNA-EKELEKQRTFAEQVA-------QQKLSAEQECIRL 1766
Cdd:pfam15921 731 GMQKQITAK-RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKlSQELSTVATEKNKMAgelevlrSQERRLKEKVANM 809
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1767 KADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLK---MKTEAEKKTMSN---TEKSKQLLESE 1840
Cdd:pfam15921 810 EVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKprlLQPASFTRTHSNvpsSQSTASFLSHH 889
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 736215636 1841 ALKMKQLADEATR--------LRSVAEEAKKQRQTAEEEAAR 1874
Cdd:pfam15921 890 SRKTNALKEDPTRdlkqllqeLRSVINEEPTVQLSKAEDKGR 931
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1575-1746 |
4.56e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 57.24 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1575 AAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQshsmsfnvkASKLEESLKKEQGTVLQL 1654
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE---------LEDLEKEIKRLELEIEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1655 QEEAEQLRKQQEEANKARE--QAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAAL 1732
Cdd:COG1579 72 EARIKKYEEQLGNVRNNKEyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170
....*....|....
gi 736215636 1733 KQKDNAEKELEKQR 1746
Cdd:COG1579 152 AELEAELEELEAER 165
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1366-1677 |
4.91e-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: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1366 TLRTRYSELMTLTSQYIKFITETQRRLEDDEK---ASEKLKEEERKKMAEIQAELDKQKQIAEAQAKSVIKAEQEAQELK 1442
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKdlaRLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1443 LKMKEEASKRQDVAVDAEQQKQNI---QHELHHLKSL----------SEQEIKSKSQQLEHALVSHTKIEEEIHTIRIQL 1509
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALdelRAELTLLNEEaanlrerlesLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1510 EMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKF 1589
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1590 KMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAAtqlqshsmsfnvkasKLEESLkKEQGTV--------LQLQEEAEQL 1661
Cdd:TIGR02168 942 QERLSEEYSLTLEEAEALENKIEDDEEEARRRLK---------------RLENKI-KELGPVnlaaieeyEELKERYDFL 1005
|
330
....*....|....*.
gi 736215636 1662 RKQQEEANKAREQAEK 1677
Cdd:TIGR02168 1006 TAQKEDLTEAKETLEE 1021
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1410-1757 |
5.32e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 58.39 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1410 MAEIQAELDKQkqIAEAQAksvIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQHELHHLKSLSEQ-EIKSKSQQL 1488
Cdd:pfam13868 17 AAKCNKERDAQ--IAEKKR---IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQiEEREQKRQE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1489 EHALVSHTKIEEEIHTIRIQLE--MTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELK 1566
Cdd:pfam13868 92 EYEEKLQEREQMDEIVERIQEEdqAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1567 RKSEAEKEAAKQKQKAlddlqkfKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAAtqlqshsmsfnvkasKLEESLKK 1646
Cdd:pfam13868 172 EAEREEIEEEKEREIA-------RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQ---------------KEREEAEK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1647 EQGTVLQLQEEAEQLRKQQEEAnKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAK 1726
Cdd:pfam13868 230 KARQRQELQQAREEQIELKERR-LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAA 308
|
330 340 350
....*....|....*....|....*....|.
gi 736215636 1727 AEDAALKQKDNAEKELEKQRTFAEQVAQQKL 1757
Cdd:pfam13868 309 EREEELEEGERLREEEAERRERIEEERQKKL 339
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2404-2627 |
5.57e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2404 QKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQ--STETVVQKLETQRLQSTRE 2481
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQElaALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2482 ADGLKEAIADLEKEREKLKKeaeelQNKSNKMANTQKEEIEQQKAIIQKSFISERELLLKRQKAVEDEKKKLQKQFEDEV 2561
Cdd:COG4942 99 LEAQKEELAELLRALYRLGR-----QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 2562 KKAEALKDEQERQRKLMEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEK--KRLDQEKQLGAE 2627
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAliARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2190-2380 |
6.11e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 6.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2190 AAEAEALKQKKQADA--EMAKHKKEADQALKLKSQVEKELTMVKLRLDETdkQKALLDEELQRVKGEVNDAVKQKAQVED 2267
Cdd:COG4913 239 RAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2268 ELAKVRIQMDELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETArqrQIAESNLAEQRALA 2347
Cdd:COG4913 317 RLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA---EEFAALRAEAAALL 393
|
170 180 190
....*....|....*....|....*....|...
gi 736215636 2348 EKMLKEKMQAIQEATKLKAEAQELQKQKDQAQE 2380
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1035-1711 |
6.83e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.21 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1035 TQIKDLRLRLEGCENRTVTRLRQPVDKEPLKACALK--TAEQMKVQSELEGLKKDLNSITEQTEEVLASQQQISSAPMLR 1112
Cdd:TIGR00618 194 GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKhlREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1113 SELDVtLRKMDHVYGLSSIYLDKLKTIDVVIRNTKEAEAALKTYESRLLDVNKVPENEKEVEEQRSQLKSMRAEVEADQV 1192
Cdd:TIGR00618 274 AQEAV-LEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1193 IFDRLQDELRRASTINDKMTRIHSERDaEMEHYRQLVSSLLERWQVVFAQMDMRQRELDLLGRHMNSYNVSYEWLIHWLG 1272
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKK 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1273 EARKRQEKIQAVPIGGSKALREQLAEEKKLLEEIEKNKDKIDScQKNAKAYIDSVKDYELQILTYKALQDPMASPLKK-- 1350
Cdd:TIGR00618 432 QQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ-LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGsc 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1351 -------------PKMDCASDNIIQEYVTLRTR----YSELMTLTSQyIKFITETQRRLEDDEKASEKLKEEERKKMAEI 1413
Cdd:TIGR00618 511 ihpnparqdidnpGPLTRRMQRGEQTYAQLETSeedvYHQLTSERKQ-RASLKEQMQEIQQSFSILTQCDNRSKEDIPNL 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1414 QAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKrQDVAVDAEQQKQNIQHELHHLKSLSEQEIKsksQQLEHALV 1493
Cdd:TIGR00618 590 QNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDL-QDVRLHLQQCSQELALKLTALHALQLTLTQ---ERVREHAL 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1494 SHTKIEEEIHTIRIQLEmtikqkKTAESELQQLRDKAAEAEKLRKAAQEDAERLrKQVAEETQKKKNAEDELKRKSEAEK 1573
Cdd:TIGR00618 666 SIRVLPKELLASRQLAL------QKMQSEKEQLTYWKEMLAQCQTLLRELETHI-EEYDREFNEIENASSSLGSDLAARE 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1574 EAAKQKQKALDDLQKFKMQAEEaerrmkQAEEEKLRQIKVVEEVAQKSAatQLQSHSMSFNVKASKLEESLKKEQGTVLQ 1653
Cdd:TIGR00618 739 DALNQSLKELMHQARTVLKART------EAHFNNNEEVTAALQTGAELS--HLAAEIQFFNRLREEDTHLLKTLEAEIGQ 810
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1654 LQEEAEQLRK-QQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKK-SKTQEEAE 1711
Cdd:TIGR00618 811 EIPSDEDILNlQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLaQLTQEQAK 870
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1414-1791 |
7.77e-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: 59.08 E-value: 7.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1414 QAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQ----------HELHH-LKSLSEQEIK 1482
Cdd:pfam12128 470 DERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDelelqlfpqaGTLLHfLRKEAPDWEQ 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1483 SKSQQLEHALVSHTKIEEEIHTIRIQLEMT----------IKQKKTAESElQQLRDKAAEAEKLRKAAQEDAERLRKQVA 1552
Cdd:pfam12128 550 SIGKVISPELLHRTDLDPEVWDGSVGGELNlygvkldlkrIDVPEWAASE-EELRERLDKAEEALQSAREKQAAAEEQLV 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1553 ------EETQKK--------KNAEDELKR-----------KSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEK 1607
Cdd:pfam12128 629 qangelEKASREetfartalKNARLDLRRlfdekqsekdkKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQ 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1608 LRQIKVVEEVAQKSAATQLQSHSMSFNVKASKLEESLKKEQG------------------TVLQLQEEAEQLRKQQEEAN 1669
Cdd:pfam12128 709 KREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKaletwykrdlaslgvdpdVIAKLKREIRTLERKIERIA 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1670 KaREQAEKELETWRQK--ANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRT 1747
Cdd:pfam12128 789 V-RRQEVLRYFDWYQEtwLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC 867
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 736215636 1748 FAEQVAQQKLSAEQECIRLKADF--DHAEQQRGLLDNELQRLKKEV 1791
Cdd:pfam12128 868 EMSKLATLKEDANSEQAQGSIGErlAQLEDLKLKRDYLSESVKKYV 913
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1501-1680 |
7.81e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.47 E-value: 7.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1501 EIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQ 1580
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1581 kaLDDLQKfkmQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQlqshsmsfnVKASKLEESLKKEQGtvlQLQEEAEQ 1660
Cdd:COG1579 91 --YEALQK---EIESLKRRISDLEDEILELMERIEELEEELAELE---------AELAELEAELEEKKA---ELDEELAE 153
|
170 180
....*....|....*....|
gi 736215636 1661 LRKQQEEANKAREQAEKELE 1680
Cdd:COG1579 154 LEAELEELEAEREELAAKIP 173
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1635-1846 |
7.85e-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: 57.93 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1635 VKASKLEESLKKEQGTVLQLQEE----AEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEA 1710
Cdd:TIGR02794 38 IQAVLVDPGAVAQQANRIQQQKKpaakKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1711 ERQKVEA-ERDAKKRAKAEDAALKQKdnAEKELEKQrtfAEQVAQQKLSAE----QECIRLKADFDHAEQQrgllDNELQ 1785
Cdd:TIGR02794 118 QKQAEEAkAKQAAEAKAKAEAEAERK--AKEEAAKQ---AEEEAKAKAAAEakkkAEEAKKKAEAEAKAKA----EAEAK 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736215636 1786 RLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQ 1846
Cdd:TIGR02794 189 AKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1684-1944 |
8.65e-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: 57.55 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1684 QKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAErdaKKRAKAEDAALKQKDNAEKELEKQRtfAEQVAQQKLSAEQEC 1763
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAE---KQRAAEQARQKELEQRAAAEKAAKQ--AEQAAKQAEEKQKQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1764 IRLKAdfdhaeqqrglldnelQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKtmsnTEKSKQLLESEAlK 1843
Cdd:TIGR02794 122 EEAKA----------------KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKK----AEEAKKKAEAEA-K 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1844 MKQLADEatrlRSVAEEAKKQRQTAEEEA---ARQRAEAEKILKEKLAAINEATRLRTEAEIAL-KAKEAENERLKRKAE 1919
Cdd:TIGR02794 181 AKAEAEA----KAKAEEAKAKAEAAKAKAaaeAAAKAEAEAAAAAAAEAERKADEAELGDIFGLaSGSNAEKQGGARGAA 256
|
250 260
....*....|....*....|....*
gi 736215636 1920 DEAYQRKLledqAAQHKHDIQEKII 1944
Cdd:TIGR02794 257 AGSEVDKY----AAIIQQAIQQNLY 277
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2197-2643 |
8.66e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.88 E-value: 8.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2197 KQKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQvedelakvriqm 2276
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ------------ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2277 DELLKLKLKIEEQnrslmKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQ 2356
Cdd:TIGR04523 307 DWNKELKSELKNQ-----EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2357 AIQEATKLKAEAQELQKQkdqaqekakklLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQS 2436
Cdd:TIGR04523 382 YKQEIKNLESQINDLESK-----------IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2437 KAENEAKKFKKQADEAKARLKDTEKqSTETVVQKLEtqrlQSTREADglkeaiadlekereklkkeaeeLQNKSNKMANT 2516
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSR-SINKIKQNLE----QKQKELK----------------------SKEKELKKLNE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2517 QKEEIEQQkaiiQKSFISERELLLKRQKAVEDEKKKLQKQFEDevKKAEALKDEQERQRKLMEEEK-------KKLQAIM 2589
Cdd:TIGR04523 504 EKKELEEK----VKDLTKKISSLKEKIEKLESEKKEKESKISD--LEDELNKDDFELKKENLEKEIdeknkeiEELKQTQ 577
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736215636 2590 DAAVKKQKEAEADMKNKQTE-------MEVLEKKRLDQEKQLG---AENQKLREKLQCLEGASK 2643
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEkkdlikeIEEKEKKISSLEKELEkakKENEKLSSIIKNIKSKKN 641
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1381-1920 |
8.76e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.76 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1381 YIKFITETQRRLEDDEKASEKLKEEERKKMAEIQAELDKqKQIAEAQAKSVIKAEQEAQELKLKMKEeaskrqdvavdAE 1460
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDD-YNNLKSALNELSSLEDMKNRYESEIKT-----------AE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1461 QQKQNIQHELHHLKSLSEQEIKSKSQQlehALVSHTKIEEEIHTIRiQLEMTIKQKKTAESELQQLRDkaaeaeKLRKAA 1540
Cdd:PRK01156 263 SDLSMELEKNNYYKELEERHMKIINDP---VYKNRNYINDYFKYKN-DIENKKQILSNIDAEINKYHA------IIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1541 QEDAERlrkqvaEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQ- 1619
Cdd:PRK01156 333 VLQKDY------NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDa 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1620 -KSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQ-----------QEEANKAREQAEKELETWRQKAN 1687
Cdd:PRK01156 407 iKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1688 EALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLK 1767
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1768 -ADFDHAEQQRGLLDNELQR-----LKKEVSATEKQRKLLEEELAKVRSEMDSLLKmKTEAEkktMSNTEKSKQLLESEA 1841
Cdd:PRK01156 567 rTSWLNALAVISLIDIETNRsrsneIKKQLNDLESRLQEIEIGFPDDKSYIDKSIR-EIENE---ANNLNNKYNEIQENK 642
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 1842 LKMKQLADEATRLRSVAEEaKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAED 1920
Cdd:PRK01156 643 ILIEKLRGKIDNYKKQIAE-IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1638-1902 |
9.50e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 58.37 E-value: 9.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1638 SKLEESLKkEQGTVLQLQEEAEQLR-KQQEEANKAREQAE---KELETWRQKANEALRLRLQAEEEAQKKSKtQEEAERQ 1713
Cdd:pfam07888 34 NRLEECLQ-ERAELLQAQEAANRQReKEKERYKRDREQWErqrRELESRVAELKEELRQSREKHEELEEKYK-ELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1714 KVEAERDAKKRAKAEDAALKqkdnaeKELEKQrtfAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSA 1793
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARI------RELEED---IKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1794 TEKQRKLLEEELAKVRSEMdsllkmkteAEKKTmsntekSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEE--E 1871
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSL---------AQRDT------QVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQErlN 247
|
250 260 270
....*....|....*....|....*....|.
gi 736215636 1872 AARQRAEAekiLKEKLAAINeATRLRTEAEI 1902
Cdd:pfam07888 248 ASERKVEG---LGEELSSMA-AQRDRTQAEL 274
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
172-274 |
9.85e-08 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 53.15 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGyqgLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYrQSNQ--ENLEQAFSVAERDLGVTRLL 249
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCPDWESW-DPNQpvQNAREAMQQADDWLGVPQVI 86
|
90 100
....*....|....*....|....*
gi 736215636 250 DPEDVDVLHPDEKSIITYVSSLYDA 274
Cdd:cd21314 87 APEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1410-1732 |
1.03e-07 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 58.19 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1410 MAEIQAELDKQKQIAEAQAKsviKAEQEAQELKLKmKEEASKRQDVAVDAEQ--------QKQNIQHELHHLKSL----- 1476
Cdd:pfam03528 13 LEKENAEFYRLKQQLEAEFN---QKRAKFKELYLA-KEEDLKRQNAVLQEAQveldalqnQLALARAEMENIKAVatvse 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1477 -SEQEI--KSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKK--------TAESELQQLRDKAAEA------EKLRKA 1539
Cdd:pfam03528 89 nTKQEAidEVKSQWQEEVASLQAIMKETVREYEVQFHRRLEQERaqwnqyreSAEREIADLRRRLSEGqeeenlEDEMKK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1540 AQEDAERLRKQVAeetqkkknaedelkrksEAEKEAAKQKQKALddlqkfkmqaeEAERRMKQAEEEKLRQIKVVEEvAQ 1619
Cdd:pfam03528 169 AQEDAEKLRSVVM-----------------PMEKEIAALKAKLT-----------EAEDKIKELEASKMKELNHYLE-AE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1620 KSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKE-LETWRQKANEALRLRL---- 1694
Cdd:pfam03528 220 KSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQfLESQRLLMRDMQRMESvlts 299
|
330 340 350
....*....|....*....|....*....|....*....
gi 736215636 1695 -QAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAAL 1732
Cdd:pfam03528 300 eQLRQVEEIKKKDQEEHKRARTHKEKETLKSDREHTVSI 338
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2125-2361 |
1.15e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 57.16 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2125 AKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKsAEEEAAKQAKAQKDAEKLKKAAEEeaskraAAEAEALKQKKqadA 2204
Cdd:TIGR02794 52 ANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRA-AEQARQKELEQRAAAEKAAKQAEQ------AAKQAEEKQKQ---A 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2205 EMAKHKKEADQALKLKSQVEKEltmvklrldetdkqkalLDEELQRvKGEVNDAVKQKAQVEDELAKVRIQMDELLKLKL 2284
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERK-----------------AKEEAAK-QAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKA 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 2285 KIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEA 2361
Cdd:TIGR02794 184 EAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2384-2640 |
1.16e-07 |
|
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: 58.53 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2384 KLLEDKQQIQQRLDKETEGFQK--SLEAERKRQLEvsaeaetlRLKvkelsdAQSKAENEAKKFKKQADEAKARL----- 2456
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRleDILNELERQLK--------SLE------RQAEKAERYKELKAELRELELALlvlrl 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2457 --KDTEKQSTETVVQKLETQRLQSTREADGLKEAIADLEKEREKLKKEAEELQnKSNKMANTQKEEIEQQKAIIQKSfis 2534
Cdd:TIGR02168 235 eeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ-KELYALANEISRLEQQKQILRER--- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2535 eRELLLKRQKAVEDEKKKLQKQFEDEVKKAEALKDEQERQRKLMEEEKKKLqaimDAAVKKQKEAEADMKNKQTEMEVLE 2614
Cdd:TIGR02168 311 -LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL----EELEAELEELESRLEELEEQLETLR 385
|
250 260
....*....|....*....|....*....
gi 736215636 2615 KKRLD---QEKQLGAENQKLREKLQCLEG 2640
Cdd:TIGR02168 386 SKVAQlelQIASLNNEIERLEARLERLED 414
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1515-1745 |
1.19e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 58.04 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1515 QKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQvaEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAE 1594
Cdd:pfam15709 330 QEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQ--EQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1595 EAERRMKQAEEEKLRQikvveevaqksaatqlqshsmsfnvkasKLEESLKKEQgtvlQLQEEaeqlrKQQEEANKAREQ 1674
Cdd:pfam15709 408 RKQRLQLQAAQERARQ----------------------------QQEEFRRKLQ----ELQRK-----KQQEEAERAEAE 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736215636 1675 AEKELETWRQKANEALRLRLQAEEE-AQKKSKTQEEAERQKVEAErdaKKRAKAEDAALKQKDNAEKELEKQ 1745
Cdd:pfam15709 451 KQRQKELEMQLAEEQKRLMEMAEEErLEYQRQKQEAEEKARLEAE---ERRQKEEEAARLALEEAMKQAQEQ 519
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1948-2203 |
1.41e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.12 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1948 SSSDSEMVRQKTIVEETLRQkkiveeeihiirinfEKASKGKSDLENELKKL-KVIAEETQKsklKAEAEAEKLKKLAAE 2026
Cdd:PRK09510 48 SVIDAVMVDPGAVVEQYNRQ---------------QQQQKSAKRAEEQRKKKeQQQAEELQQ---KQAAEQERLKQLEKE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2027 --EEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEV 2104
Cdd:PRK09510 110 rlAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2105 LSKNKEDSLAQQKMKEEFEnakrlaqaaekakekaekeaallrQKAAEAEKQKKSAEeeaaKQAKAQKDAEKLKKAAEEE 2184
Cdd:PRK09510 190 EAAAKAAAEAKKKAEAEAK------------------------KKAAAEAKKKAAAE----AKAAAAKAAAEAKAAAEKA 241
|
250
....*....|....*....
gi 736215636 2185 ASKRAAAEAEALKQKKQAD 2203
Cdd:PRK09510 242 AAAKAAEKAAAAKAAAEVD 260
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1363-2022 |
1.45e-07 |
|
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: 58.16 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1363 EYVTLRTRYSELMTLTSQYIKFITETQRRLEDDEKASEKLKEEERKKMAEIqAELDKQkqiAEAQAKSVIKAEQEAQELK 1442
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI-EELERE---IEEERKRRDKLTEEYAELK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1443 LKMKEEASKRQDVAVDA----------EQQKQNIQHELHHLK---SLSEQEIKSKSQQLEHALVSHTKIEEEIHTIRIQL 1509
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFaetrdelkdyREKLEKLKREINELKrelDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1510 EMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKF 1589
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGV 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1590 K---MQAEEAERRMKQAEE----EKLRQIKVVEEVAQKSAATQLQSHS---MSF----NVKASKLEESLKKEQGTV---L 1652
Cdd:TIGR02169 524 HgtvAQLGSVGERYATAIEvaagNRLNNVVVEDDAVAKEAIELLKRRKagrATFlplnKMRDERRDLSILSEDGVIgfaV 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1653 QLQEEAEQLRKQ----------QEEANKAREQA--------EKEL----------------ETWRQKANEALRLRLQAEE 1698
Cdd:TIGR02169 604 DLVEFDPKYEPAfkyvfgdtlvVEDIEAARRLMgkyrmvtlEGELfeksgamtggsraprgGILFSRSEPAELQRLRERL 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1699 EAQKKSKTQEEAERQKVEAERDAkKRAKAEDA------ALKQKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDH 1772
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDE-LSQELSDAsrkigeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1773 AEQQRGLLDNELQRLKKEVSATEkqRKLLEEELAKVRSEMDSLLKMKTEAEKKTmSNTEKSKQLLESEALKMKQLADEAT 1852
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARL-REIEQKLNRLTLEKEYLEKEIQELQ 839
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1853 RLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQA 1932
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1933 AQHKHDIQEKIIHLKS-----SSDSEMVRQKTIVEETLRQKKIVEEEIHIIR-IN------FEKASKGKSDLENELKKLk 2000
Cdd:TIGR02169 920 SELKAKLEALEEELSEiedpkGEDEEIPEEELSLEDVQAELQRVEEEIRALEpVNmlaiqeYEEVLKRLDELKEKRAKL- 998
|
730 740
....*....|....*....|..
gi 736215636 2001 viaEETQKSKLKAEAEAEKLKK 2022
Cdd:TIGR02169 999 ---EEERKAILERIEEYEKKKR 1017
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
52-159 |
1.47e-07 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 53.47 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 52 ERDRVQKKTFTKWVNKhlMKSQRHITDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 122
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnkvNKPPYPKLGANMK--KLENCNYAVEL 93
|
90 100 110
....*....|....*....|....*....|....*...
gi 736215636 123 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 159
Cdd:cd21331 94 GKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1740-2649 |
1.52e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.13 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1740 KELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLL---DNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLL 1816
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQItskEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1817 KMKTE--AEKKTMSNTEKSKQLLESEALKMKQLADEatRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEAT 1894
Cdd:TIGR00606 266 KLDNEikALKSRKKQMEKDNSELELKMEKVFQGTDE--QLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1895 RLRTE-AEIALKAKEAENERLKRKAEDEAYQRKLlEDQAAQHKHDIQEKIIHLKSSSDSEMVRQKTIVEETLR--QKKIV 1971
Cdd:TIGR00606 344 ELLVEqGRLQLQADRHQEHIRARDSLIQSLATRL-ELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCAdlQSKER 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1972 EEEIHIIRINFEKASKGKSdLENElkklKVIAEETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQ 2051
Cdd:TIGR00606 423 LKQEQADEIRDEKKGLGRT-IELK----KEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2052 CKAAQEEVARLEK--------KADEANKQKEKAEKEAEKQVIVAKEAAQKcssaeqkAQEVLSKNKEDSLAQQKMKEEFE 2123
Cdd:TIGR00606 498 TLKKEVKSLQNEKadldrklrKLDQEMEQLNHHTTTRTQMEMLTKDKMDK-------DEQIRKIKSRHSDELTSLLGYFP 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2124 NAKRLAQAAEKAKEKAEKEAALLRQKAAEAEK----QKKSAEEEAAKQAKAQKDAEKLKKA--AEEEASKRAAAEAEALK 2197
Cdd:TIGR00606 571 NKKQLEDWLHSKSKEINQTRDRLAKLNKELASleqnKNHINNELESKEEQLSSYEDKLFDVcgSQDEESDLERLKEEIEK 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2198 QKKQAdAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQkalLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMD 2277
Cdd:TIGR00606 651 SSKQR-AMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAE---LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRD 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2278 ELLklkLKIEEQNRSLMKKDKDktqkvLAEEAGKMKSLAEEAARL--SVEAEETARQRQIAESNLAEQrALAEKMLKEKM 2355
Cdd:TIGR00606 727 EML---GLAPGRQSIIDLKEKE-----IPELRNKLQKVNRDIQRLknDIEEQETLLGTIMPEEESAKV-CLTDVTIMERF 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2356 QAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEgfqkslEAERKRQLEVSAEAETLRLKVKElsdaq 2435
Cdd:TIGR00606 798 QMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVS------KIELNRKLIQDQQEQIQHLKSKT----- 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2436 skaeNEAKKFKKQADEAKARLKDTEKQSTEtvvqkLETQRLQSTREADGLKEAIADLEKEREKLKKEAEELQNKSNKMAN 2515
Cdd:TIGR00606 867 ----NELKSEKLQIGTNLQRRQQFEEQLVE-----LSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2516 TQKEEIEQQKAIIQKSFISERELllkrQKAVEDEKKKLQKQFEDEVKKAEALKDEQERQRKLMEEEKKKLQAIMDAAVKK 2595
Cdd:TIGR00606 938 KAQDKVNDIKEKVKNIHGYMKDI----ENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQ 1013
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736215636 2596 QKEAEADMKNKQTEMEVLEKKRL----------DQEKQLGAENQKLREKLQCLEGASKQSATKQ 2649
Cdd:TIGR00606 1014 ERWLQDNLTLRKRENELKEVEEElkqhlkemgqMQVLQMKQEHQKLEENIDLIKRNHVLALGRQ 1077
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2040-2276 |
1.63e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.78 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2040 RITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEvlsKNKEDSLAQQKMK 2119
Cdd:TIGR02794 59 KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE---EAKAKQAAEAKAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2120 EEFENAKRLAQAAEKA--KEKAEKEAALLRQKAAEAEKQKKS---AEEEAAKQAK---AQKDAEKLKKAAEEEASKRAAA 2191
Cdd:TIGR02794 136 AEAEAERKAKEEAAKQaeEEAKAKAAAEAKKKAEEAKKKAEAeakAKAEAEAKAKaeeAKAKAEAAKAKAAAEAAAKAEA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2192 EAEAlkqKKQADAEMAKHKKEADQALKLKSQVEKELTmvklrldeTDKQKALLDEELQRVKGEVNDAVKQKAQVEDELA- 2270
Cdd:TIGR02794 216 EAAA---AAAAEAERKADEAELGDIFGLASGSNAEKQ--------GGARGAAAGSEVDKYAAIIQQAIQQNLYDDPSFRg 284
|
....*....
gi 736215636 2271 ---KVRIQM 2276
Cdd:TIGR02794 285 ktcRLRIRL 293
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
167-274 |
1.83e-07 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 52.40 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 167 QSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTGWRDGKLFNAIIHKHRPTLI-DMGKVYRQSNQENLEQAFSVAERDLGV 245
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100 110
....*....|....*....|....*....|.
gi 736215636 246 TRLLDPEDVdvLHPD--EKSIITYVSSLYDA 274
Cdd:cd21313 80 PQVITPEEI--IHPDvdEHSVMTYLSQFPKA 108
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1870-2598 |
1.83e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.81 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1870 EEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLL--EDQAAQHKHDIQEKiihlK 1947
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikENNATRHLCNLLKE----T 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1948 SSSDSEMVRQKTIVEETLRQKKIveeeihiirinfekaskgksDLENELKKLKVIAEEtqkskLKAEAEAEKLKklaaee 2027
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVYM--------------------DLNNNIEKMILAFEE-----LRVQAENARLE------ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2028 ekKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEankqkekAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSK 2107
Cdd:pfam05483 213 --MHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITE-------KENKMKDLTFLLEESRDKANQLEEKTKLQDEN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2108 NKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASK 2187
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2188 RAAAEAEALK----QKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKqkaLLDEELQRVKgeVNDAVKQKA 2263
Cdd:pfam05483 364 LLRTEQQRLEknedQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEK---LLDEKKQFEK--IAEELKGKE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2264 QVEDELAKVRIQMDELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQrqiaesnlaeq 2343
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQE----------- 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2344 ralAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLED----KQQIQQRLDKETEGFQKSLEAERKRQLEVSA 2419
Cdd:pfam05483 508 ---ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDElesvREEFIQKGDEVKCKLDKSEENARSIEYEVLK 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2420 EAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQST-----ETVVQKLETQrLQSTRE-----ADGLKEAI 2489
Cdd:pfam05483 585 KEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKqlnayEIKVNKLELE-LASAKQkfeeiIDNYQKEI 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2490 ADLEKEREKLKKEAEELQNKSNKMANTQKE-------EIEQQKAIIQK------SFISERELLLKRQKAVEDEKKKLQKQ 2556
Cdd:pfam05483 664 EDKKISEEKLLEEVEKAKAIADEAVKLQKEidkrcqhKIAEMVALMEKhkhqydKIIEERDSELGLYKNKEQEQSSAKAA 743
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 736215636 2557 FEDEVK--KAEALKDEQERQRKLMEEEKKKLQAIMDAAVKKQKE 2598
Cdd:pfam05483 744 LEIELSniKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2432-2652 |
1.90e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2432 SDAQSKAENEAKKFKKQADEAKARLKDTEKQstetvVQKLETQRLQSTREADGLKEAIADLEKEREKLKKEAEELQNKSN 2511
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKE-----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2512 KMA---NTQKEEIEQQKAIIQKSFISERELLLKRQKAVEDEKKKLQ------KQFEDEVKKAEALKDEQERQRKLMEEEK 2582
Cdd:COG4942 94 ELRaelEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736215636 2583 KKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEKKRLDQEKQ---LGAENQKLREKLQCLEGASKQSATKQVAS 2652
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAElaeLQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1499-1720 |
2.00e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.39 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1499 EEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKnAEDELKRKSEAEKEaakq 1578
Cdd:TIGR02794 67 QERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK-QAAEAKAKAEAEAE---- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1579 kQKALDDLQKfkmQAEEaERRMKQAEEEKLRQikvvEEVAQKSAAtqlqshsmsfnvKASKLEESLKKEQGTVLQLQEEA 1658
Cdd:TIGR02794 142 -RKAKEEAAK---QAEE-EAKAKAAAEAKKKA----EEAKKKAEA------------EAKAKAEAEAKAKAEEAKAKAEA 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736215636 1659 EQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERD 1720
Cdd:TIGR02794 201 AKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVD 262
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1653-1883 |
2.09e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.74 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1653 QLQEEAEQLRKQQEEANKAREQAEkELETWRQKANEalrlRLQAEEeaQKKSKTQEEAERQKVEAERDAKKRAKAEDAAL 1732
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQE----RLKQLE--KERLAAQEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1733 KQKDNAekelekqrtfaeqvaqqKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQrklleEELAKVRSEM 1812
Cdd:PRK09510 140 KAAAAA-----------------KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKA-----EAEAAAKAAA 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736215636 1813 DSLLKMKTEAEKKTMSNTEKskqllESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKIL 1883
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKK-----KAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2219-2639 |
2.36e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2219 LKSQVE-KELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELLKLKLKIEE--QNRSLMK 2295
Cdd:PRK02224 192 LKAQIEeKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDlrETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2296 KDKDKTQKVLAEEAGKMKSLAEEAARLSVEAE------ETARQRQiaeSNLAEQRALAEKMLKEKMQAIQEATKlkaEAQ 2369
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGlddadaEAVEARR---EELEDRDEELRDRLEECRVAAQAHNE---EAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2370 ELQKQKDQAQEKAKKLLEDKQqiqqRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQA 2449
Cdd:PRK02224 346 SLREDADDLEERAEELREEAA----ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2450 DEAKARLKDTEK--QSTETVVQKLET-----------QRLQSTREADGLKEAiadlekereklkkeaeelqnksnkmaNT 2516
Cdd:PRK02224 422 DELREREAELEAtlRTARERVEEAEAlleagkcpecgQPVEGSPHVETIEED--------------------------RE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2517 QKEEIEQQKAIIQksfiSERELLLKRQKAVEDeKKKLQKQFEDEVKKAEALKDEQERQRKLMEEEKKKLQAIMDAAVKKQ 2596
Cdd:PRK02224 476 RVEELEAELEDLE----EEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 736215636 2597 KEAEADMKNKQTEMEVLEKKRlDQEKQLGAENQKLREKLQCLE 2639
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAR-EEVAELNSKLAELKERIESLE 592
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1516-1758 |
2.38e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 57.10 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1516 KKTAESELQQLRdkaAEAEKLRKAAQEDAERLRKQvaeetqKKKNAEDE-LKRKSEAEKEAaKQKQKALDDLQKFKMQAE 1594
Cdd:PRK12704 26 KKIAEAKIKEAE---EEAKRILEEAKKEAEAIKKE------ALLEAKEEiHKLRNEFEKEL-RERRNELQKLEKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1595 EAERRmkqaEEEKLRqikvveevaqksaatqlqshsmsfnvkasKLEESLKKEQGTVLQLQEEAEqlrKQQEEANKAREQ 1674
Cdd:PRK12704 96 ENLDR----KLELLE-----------------------------KREEELEKKEKELEQKQQELE---KKEEELEELIEE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1675 AEKELEtwrQKANealrlrLQAEE-EAQKKSKTQEEAERQKVEAERDAKKRAKAEdaalkqkdnAEKELEK------QRT 1747
Cdd:PRK12704 140 QLQELE---RISG------LTAEEaKEILLEKVEEEARHEAAVLIKEIEEEAKEE---------ADKKAKEilaqaiQRC 201
|
250
....*....|.
gi 736215636 1748 FAEQVAQQKLS 1758
Cdd:PRK12704 202 AADHVAETTVS 212
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1520-1825 |
2.74e-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: 57.27 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1520 ESELQQLRDKAAEAEKLRKAAQEDAERLRKQVaeetqkkknaedelkrkseaekEAAKQKQKALDDLQKFKM-------- 1591
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQL----------------------DQLKEQLQLLNKLLPQANlladetla 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1592 -QAEEAERRMKQAEEEKL------RQIKVVEEVAQksaatQLQSHSMSFnvkaskleESLKKEqgtVLQLQEEAEQLRKQ 1664
Cdd:COG3096 893 dRLEELREELDAAQEAQAfiqqhgKALAQLEPLVA-----VLQSDPEQF--------EQLQAD---YLQAKEQQRRLKQQ 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1665 --------QEEANKAREQAEKELETwRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEaerdakkRAKAEDAALKQKD 1736
Cdd:COG3096 957 ifalsevvQRRPHFSYEDAVGLLGE-NSDLNEKLRARLEQAEEARREAREQLRQAQAQYS-------QYNQVLASLKSSR 1028
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1737 NAekeleKQRTFAEqvAQQKLSAeqecIRLKADFDHAEQQRGlldnELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLL 1816
Cdd:COG3096 1029 DA-----KQQTLQE--LEQELEE----LGVQADAEAEERARI----RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQ 1093
|
....*....
gi 736215636 1817 KMKTEAEKK 1825
Cdd:COG3096 1094 KRLRKAERD 1102
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4089-4125 |
2.91e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 49.40 E-value: 2.91e-07
10 20 30
....*....|....*....|....*....|....*..
gi 736215636 4089 IRLLEAQIATGGIIDPQESHRLPVEAAYERGLFDEEM 4125
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1654-1825 |
2.98e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1654 LQEEAEQLRKQQEEANKAR----------EQAEKELETWRQ--KANEALRLRLQAEEEAQKKSKTQEEA-----ERQKVE 1716
Cdd:PRK04863 892 LADRVEEIREQLDEAEEAKrfvqqhgnalAQLEPIVSVLQSdpEQFEQLKQDYQQAQQTQRDAKQQAFAltevvQRRAHF 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1717 AERDAKKRAKAEDA---ALKQK-DNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQ------- 1785
Cdd:PRK04863 972 SYEDAAEMLAKNSDlneKLRQRlEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvpad 1051
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 736215636 1786 ------------RLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKK 1825
Cdd:PRK04863 1052 sgaeerararrdELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1386-1735 |
3.32e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 56.41 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1386 TETQRRLEDDEKASeklkeeerkkmaEIQAELDKQKQiaeaqaksviKAEQEAQElklKMKEEASKRQDVAVDAEQQKQN 1465
Cdd:pfam02029 52 PSGQGGLDEEEAFL------------DRTAKREERRQ----------KRLQEALE---RQKEFDPTIADEKESVAERKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1466 IQHElhhLKSLSEQEIKSKSQQLEHalvshtkiEEEihtiriqlEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAE 1545
Cdd:pfam02029 107 NEEE---ENSSWEKEEKRDSRLGRY--------KEE--------ETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1546 RLRKQV-AEETQKKKNAEDELKRKSEaEKEAAKQKQKalddLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAAT 1624
Cdd:pfam02029 168 EVPTENfAKEEVKDEKIKKEKKVKYE-SKVFLDQKRG----HPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1625 QLQShsmsfnvkASKLEESLKKEQGTVlqlQEEAEQLRKQQEEANKAREQAEKELEtWRQKANEALRLRlQAEEEAQKKS 1704
Cdd:pfam02029 243 FLEA--------EQKLEELRRRRQEKE---SEEFEKLRQKQQEAELELEELKKKRE-ERRKLLEEEEQR-RKQEEAERKL 309
|
330 340 350
....*....|....*....|....*....|.
gi 736215636 1705 KTQEEAERQKVEAErdakkRAKAEDAALKQK 1735
Cdd:pfam02029 310 REEEEKRRMKEEIE-----RRRAEAAEKRQK 335
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1701-1888 |
3.60e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 56.32 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1701 QKKSKTQEEAERQKVEAERDAKKRAKaedaalkqkdnaEKELEKQrtfaEQVAQQKLSAEQECIRLKADFDHAEQQrgLL 1780
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKK------------EALLEAK----EEIHKLRNEFEKELRERRNELQKLEKR--LL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1781 DNElQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTmsnTEKSKQLLESEALKmkqlADEATR--LRSVA 1858
Cdd:PRK12704 93 QKE-ENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI---EEQLQELERISGLT----AEEAKEilLEKVE 164
|
170 180 190
....*....|....*....|....*....|....
gi 736215636 1859 EEAKKQR----QTAEEEAarqRAEAEKILKEKLA 1888
Cdd:PRK12704 165 EEARHEAavliKEIEEEA---KEEADKKAKEILA 195
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1411-1767 |
3.84e-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: 56.88 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1411 AEIQAELDKQKQIAEAQAKSvikAEQEAQELKLKMkeeASKRQdvAVDaEQQKQNIQHelhhlkslseqeiksksQQLEH 1490
Cdd:COG3096 367 EEVVEEAAEQLAEAEARLEA---AEEEVDSLKSQL---ADYQQ--ALD-VQQTRAIQY-----------------QQAVQ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1491 ALvshtkieEEIHTIRIQLEMTIKQkktAESELQQLRDKAAEA-EKLRKAAQedaerlRKQVAEETQKKKNAEDELKRK- 1568
Cdd:COG3096 421 AL-------EKARALCGLPDLTPEN---AEDYLAAFRAKEQQAtEEVLELEQ------KLSVADAARRQFEKAYELVCKi 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1569 -SEAEKEAAKQK-QKALDDLQKFKMQAEEAER-RMKQAE-EEKLRQIKVVEEVAQ---KSAATQLQSHSMSFNVKAsKLE 1641
Cdd:COG3096 485 aGEVERSQAWQTaRELLRRYRSQQALAQRLQQlRAQLAElEQRLRQQQNAERLLEefcQRIGQQLDAAEELEELLA-ELE 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1642 ESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRqKANEALRlRLQAEEEAQKKSKTQEEAERQKV-EAERD 1720
Cdd:COG3096 564 AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWL-AAQDALE-RLREQSGEALADSQEVTAAMQQLlERERE 641
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 736215636 1721 AkKRAKAEDAALKQkdnaekELEKQrtfAEQVAQQKLSAEQECIRLK 1767
Cdd:COG3096 642 A-TVERDELAARKQ------ALESQ---IERLSQPGGAEDPRLLALA 678
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1711-2066 |
4.03e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.67 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1711 ERQKVEAERDAK-KRAKAEDAALKQ-KDNAEKELEKQRTFAE-QVAQQKLSAEQECIrlkadfdHAEQQRGLLDN--ELQ 1785
Cdd:pfam17380 279 QHQKAVSERQQQeKFEKMEQERLRQeKEEKAREVERRRKLEEaEKARQAEMDRQAAI-------YAEQERMAMERerELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1786 RLKKEVSATEKQRkLLEEELAKVRSEMDSLLKMKTEAEKKTmsntekskqllesealkmkqladeaTRLRSVAEEAKKQR 1865
Cdd:pfam17380 352 RIRQEERKRELER-IRQEEIAMEISRMRELERLQMERQQKN-------------------------ERVRQELEAARKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1866 QTAEEeaaRQRA-EAEKILKEKLAAINEATRLRtEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKII 1944
Cdd:pfam17380 406 ILEEE---RQRKiQQQKVEMEQIRAEQEEARQR-EVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEK 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1945 HLKSSSDSEMVRQKTIVEE-TLRQKKIVEEEihiirinfekasKGKSDLENELK-KLKVIAEETQKSKLKAEAEAEKLKK 2022
Cdd:pfam17380 482 EKRDRKRAEEQRRKILEKElEERKQAMIEEE------------RKRKLLEKEMEeRQKAIYEEERRREAEEERRKQQEME 549
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 736215636 2023 LAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKA 2066
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1690-2184 |
4.69e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1690 LRLRLQAE-EEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRtfaeqvaqQKLSAEQECIRLKA 1768
Cdd:COG4717 47 LLERLEKEaDELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEL--------EELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1769 DFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLA 1848
Cdd:COG4717 119 EKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1849 DEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRK-- 1926
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1927 ---------LLEDQAAQHKHDIQEKIIHLKSSSDSEMVRQKTIVEETLRQKKIVEEEIHIIRINFEKASKGK---SDLEN 1994
Cdd:COG4717 279 lflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQellREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1995 ELKKLKVIAEETQKSKLKAEAEAEKLKKLAAEEekkrkeseekvkritaaeeEAARQCKAAQEEVARLEKKADEANKQKE 2074
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGVEDEEELRAAL-------------------EQAEEYQELKEELEELEEQLEELLGELE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2075 KAEKEAEKQVIvaKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQaaekakekaekeaalLRQKAAEAE 2154
Cdd:COG4717 420 ELLEALDEEEL--EEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE---------------LLQELEELK 482
|
490 500 510
....*....|....*....|....*....|
gi 736215636 2155 KQKKSAEEEAAKQAKAQKDAEKLKKAAEEE 2184
Cdd:COG4717 483 AELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
54-153 |
4.87e-07 |
|
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: 51.50 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 54 DRVQKKTFTKWVNKHLMKS--QRHITDLYEDLRDGHNLISLLEVLSGETLPREKG--RMRFHKLQNVQIALDFLKHRQVK 129
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 736215636 130 LVNIRNDDIADGNPKLTLGLIWTI 153
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1411-1932 |
5.39e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 56.35 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1411 AEIQAELDKQKQIAEAQaksvikaEQEAQEL-----KLKMKEEASKRQDVAVDAEQQKQNIQHELHHLkSLSEQEIKSK- 1484
Cdd:PRK10246 223 ASLQVLTDEEKQLLTAQ-------QQQQQSLnwltrLDELQQEASRRQQALQQALAAEEKAQPQLAAL-SLAQPARQLRp 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1485 ---SQQLEHALVSHTKIEEEIHTIRIQLEMTI---------KQKKTAESELQQLRDKAAEAEKLRKAAQEDAErLRKQVA 1552
Cdd:PRK10246 295 hweRIQEQSAALAHTRQQIEEVNTRLQSTMALrarirhhaaKQSAELQAQQQSLNTWLAEHDRFRQWNNELAG-WRAQFS 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1553 EETQKKKNaedelKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQikvveevaqksAATQLQSHSMS 1632
Cdd:PRK10246 374 QQTSDREQ-----LRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQHAEQRPLRQ-----------RLVALHGQIVP 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1633 FNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANK--AREQAEKELETwRQKANEALRLRLQ--------------A 1696
Cdd:PRK10246 438 QQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQqlADVKTICEQEA-RIKDLEAQRAQLQagqpcplcgstshpA 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1697 EEEAQKKSKTQEEAERQKVEAErdaKKRAKAEDAALKQKDNAekeLEKQRTFAEQVAQQKLSAEQE--------CIRLKA 1768
Cdd:PRK10246 517 VEAYQALEPGVNQSRLDALEKE---VKKLGEEGAALRGQLDA---LTKQLQRDESEAQSLRQEEQAltqqwqavCASLNI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1769 DFDHAEQQRGLLDNELQRlkkevsatEKQRKLLEEelakvRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESE----ALKM 1844
Cdd:PRK10246 591 TLQPQDDIQPWLDAQEEH--------ERQLRLLSQ-----RHELQGQIAAHNQQIIQYQQQIEQRQQQLLTAlagyALTL 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1845 KQLADEATRLRSVAEEAK--KQRQTaEEEAARQRAEAEKILKEKLAAINEATrlrTEAE--IALKAKEAENERLKRKAED 1920
Cdd:PRK10246 658 PQEDEEASWLATRQQEAQswQQRQN-ELTALQNRIQQLTPLLETLPQSDDLP---HSEEtvALDNWRQVHEQCLSLHSQL 733
|
570
....*....|..
gi 736215636 1921 EAYQRKLLEDQA 1932
Cdd:PRK10246 734 QTLQQQDVLEAQ 745
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1575-1892 |
5.46e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.92 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1575 AAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQshsmsfnvkaskLEESLKKEQGTVLQL 1654
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQ------------IEEREQKRQEEYEEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1655 QEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQ 1734
Cdd:pfam13868 97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAERE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1735 KDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNEL----QRLKKEVSATEKQ-----RKLLEEEL 1805
Cdd:pfam13868 177 EIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEaekkARQRQELQQAREEqielkERRLAEEA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1806 AKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRsvAEEAKKQRQTAEEEAARQRAEAEKILKE 1885
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQR--AAEREEELEEGERLREEEAERRERIEEE 334
|
....*..
gi 736215636 1886 KLAAINE 1892
Cdd:pfam13868 335 RQKKLKE 341
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2167-2462 |
5.54e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.11 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2167 QAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAemAKHKKEADQ-ALKLKSQVEKELTMVKlrldetdKQKALLD 2245
Cdd:PRK05035 433 QAKAEIRAIEQEKKKAEEAKARFEARQARLEREKAARE--ARHKKAAEArAAKDKDAVAAALARVK-------AKKAAAT 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2246 EELQRVKGEVNDAVKQKAQVEDELAKVRIQMDEllklklkiEEQNRSlmkkDKDKTQKVLAEEA-GKMKSLAEEAARLSV 2324
Cdd:PRK05035 504 QPIVIKAGARPDNSAVIAAREARKAQARARQAE--------KQAAAA----ADPKKAAVAAAIArAKAKKAAQQAANAEA 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2325 EAEETARQRQIAEsnlAEQRALAEKmlkekmQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGfq 2404
Cdd:PRK05035 572 EEEVDPKKAAVAA---AIARAKAKK------AAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEP-- 640
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 2405 kslEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQ 2462
Cdd:PRK05035 641 ---VDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4192-4220 |
5.84e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.48 E-value: 5.84e-07
10 20
....*....|....*....|....*....
gi 736215636 4192 IVDPETGKEMSVYEAYQKGLIDHQTYMEL 4220
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1654-2566 |
6.26e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.28 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1654 LQEEAEQLRKQQEEANKAREQAEKELETWRQKANEaLRLRLQaeeEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALK 1733
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVID-LQTKLQ---EMQMERDAMADIRRRESQSQEDLRNQLQNTVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1734 Q-KDNAEKELEKQRTFAEQVAQQKLSAE---QECIRLKADFDHAEQQRGLLDNELQRL--KKEVSATEKQRKLLEEELAK 1807
Cdd:pfam15921 156 AaKCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILRELDTEISY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1808 VRSEM----DSLLKMKTEAEKKT----MSNTEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEA 1879
Cdd:pfam15921 236 LKGRIfpveDQLEALKSESQNKIelllQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1880 EKILKEKLAAINEatrLRTEAeialkaKEAenerlKRKAEDEayqrklledqaaqhkhdiqekiihlksssdsemvrqkt 1959
Cdd:pfam15921 316 MRQLSDLESTVSQ---LRSEL------REA-----KRMYEDK-------------------------------------- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1960 iVEETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLkviAEETQKSKLKAEAEAEKLKKLaaeeekkrkESEEKVK 2039
Cdd:pfam15921 344 -IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKL---LADLHKREKELSLEKEQNKRL---------WDRDTGN 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2040 RITAaeEEAARQCKAAQEEVARLEKkadeankqkekaekeaekqviVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMK 2119
Cdd:pfam15921 411 SITI--DHLRRELDDRNMEVQRLEA---------------------LLKAMKSECQGQMERQMAAIQGKNESLEKVSSLT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2120 EEFENAKRLaqaaekakekaekeaalLRQKAAEAEKQKKSAEEeaakqakAQKDAEKLKKAAEEEASKRAAAEAEALKQK 2199
Cdd:pfam15921 468 AQLESTKEM-----------------LRKVVEELTAKKMTLES-------SERTVSDLTASLQEKERAIEATNAEITKLR 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2200 KQADAEMA--KHKKEADQALKlksQVEKELTMVKLRLDETDKQKALLDEELQRV------KGEVNDAVK-QKAQVEDELA 2270
Cdd:pfam15921 524 SRVDLKLQelQHLKNEGDHLR---NVQTECEALKLQMAEKDKVIEILRQQIENMtqlvgqHGRTAGAMQvEKAQLEKEIN 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2271 KVRIQMDELLKLKLKIEEQNRSLMKKDKD-KTQKVLAEEAGKmkslaeeaarlsveaeetarqrqiaesnlaeqralaek 2349
Cdd:pfam15921 601 DRRLELQEFKILKDKKDAKIRELEARVSDlELEKVKLVNAGS-------------------------------------- 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2350 mlkEKMQAIQEatkLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVK 2429
Cdd:pfam15921 643 ---ERLRAVKD---IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2430 ELSDAQSKAENEAKKFKKQADEAKARLkdtekQSTETVVQKLETQRLQSTREADGLKEaiadlekEREKLKKEAEELQNK 2509
Cdd:pfam15921 717 SMEGSDGHAMKVAMGMQKQITAKRGQI-----DALQSKIQFLEEAMTNANKEKHFLKE-------EKNKLSQELSTVATE 784
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 2510 SNKMANT----------QKEEIEQQKAIIQKSFI--SERELLLKRQkavEDEKKKLQKQFEDEVKKAEA 2566
Cdd:pfam15921 785 KNKMAGElevlrsqerrLKEKVANMEVALDKASLqfAECQDIIQRQ---EQESVRLKLQHTLDVKELQG 850
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1398-1623 |
6.81e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1398 ASEKLKEEERKKMAEIQAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQhELHHLKSLS 1477
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-ELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1478 EQEIKSKSQQLEHALVSHTKIEEeihtiRIQLEMTIKQKKTAESE-----LQQL-RDKAAEAEKLRkAAQEDAERLRKQV 1551
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGR-----QPPLALLLSPEDFLDAVrrlqyLKYLaPARREQAEELR-ADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736215636 1552 AEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAA 1623
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2014-2441 |
7.29e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2014 EAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKAD--EANKQKEKAEKEAEKQVIVAKEAA 2091
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEelEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2092 QKCSSAEQKAQEVLSKNKEdslAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQ 2171
Cdd:COG4717 132 QELEALEAELAELPERLEE---LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2172 KDAEKLKKAAEEEasKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLD---------------- 2235
Cdd:COG4717 209 AELEEELEEAQEE--LEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSliltiagvlflvlgll 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2236 -----ETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRI----QMDELLKLKLKIEEQNRSLMKKDKDKTQKVLA 2306
Cdd:COG4717 287 allflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLppdlSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2307 EEAGKMKSL-------AEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATkLKAEAQELQKQKDQAQ 2379
Cdd:COG4717 367 ELEQEIAALlaeagveDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-LEEELEELEEELEELE 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 2380 EKAKKLLEDKQQIQQRLDK-ETEGFQKSLEAERKRQLEVSAEAE----TLRLKVKELSDAQSKAENE 2441
Cdd:COG4717 446 EELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAeewaALKLALELLEEAREEYREE 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1812-2263 |
7.42e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1812 MDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAEE-AKKQRQTAEEEAARQRAEAEKILKEKLAAI 1890
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1891 NEATRLRTEAEIALKAKEAENERLKRKAED-EAYQRKL--LEDQAAQHKHDIQEKIIHLKSSSDSEMVRQKTIVEETLRQ 1967
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEElRELEEELeeLEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1968 KKIVEEEIHIIRINFEKASKGKSDLENELKKLKvIAEETQKSKLKAEAEAEKLKK-----------------------LA 2024
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEARLLLLIAAALLALlglggsllsliltiagvlflvlgLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2025 AEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEV 2104
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2105 LSKNKEDSL---AQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQakaqkDAEKLKKAA 2181
Cdd:COG4717 367 ELEQEIAALlaeAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE-----ELEELEEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2182 EEEASKRAAAeaealkQKKQADAEMAKHKKEADQALklkSQVEKELTMVKLRLDETDKQ-------KALLDEELQRVKGE 2254
Cdd:COG4717 442 EELEEELEEL------REELAELEAELEQLEEDGEL---AELLQELEELKAELRELAEEwaalklaLELLEEAREEYREE 512
|
....*....
gi 736215636 2255 VNDAVKQKA 2263
Cdd:COG4717 513 RLPPVLERA 521
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1524-1722 |
8.56e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1524 QQLRDKAAEAEKLRKAAQEDAERLRKQVAEetqkkknAEDEL---KRK------SEAEKEAAKQKQKALDDLQKFKMQAE 1594
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEE-------AEAALeefRQKnglvdlSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1595 EAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQ-QEEANKARE 1673
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILA 316
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 736215636 1674 QAEKELETWRQKAnEALRlrlQAEEEAQKKSKTQEEAERQKVEAERDAK 1722
Cdd:COG3206 317 SLEAELEALQARE-ASLQ---AQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2374-2666 |
1.01e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2374 QKDQAQEKAKKLLEDKQQIQQRLDKetegfqksleaerkrqleVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAK 2453
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDA------------------LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2454 ARLKDTEKQSTETVVQKLETQRLQSTRE----ADGLKEAIADlekereklkkeaeelQNKSNKMANTQKEEIEQQKAiiq 2529
Cdd:COG3883 79 AEIEERREELGERARALYRSGGSVSYLDvllgSESFSDFLDR---------------LSALSKIADADADLLEELKA--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2530 ksfiserelllkRQKAVEDEKKKLqkqfEDEVKKAEALKDEQERQRKLMEEEKKKLQAIMDAAVKKQKEAEADMKNKQTE 2609
Cdd:COG3883 141 ------------DKAELEAKKAEL----EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 2610 MEVLEKKRLDQEKQLGAENQKLREKLQCLEGASKQSATKQVASKTIEVQTDVVSEEQ 2666
Cdd:COG3883 205 LAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGS 261
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1635-2228 |
1.48e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1635 VKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAR-EQAEKELETWRQK--ANEALRLRLQAEEEAQKKSKTQEEAE 1711
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAEleELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1712 RQKVEAERDAKKRAKAEDAAlKQKDNAEKELEKQRT----FAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRL 1787
Cdd:COG4913 325 LDELEAQIRGNGGDRLEQLE-REIERLERELEERERrrarLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1788 KKEVSATEKQRKLLEEELAKVRSEMDSLlkmkteaekktmsntEKSKQLLESEALKM-KQLADE----ATRLRSVAEEAk 1862
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASL---------------ERRKSNIPARLLALrDALAEAlgldEAELPFVGELI- 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1863 kqrQTAEEEAARQRAeAEKIL--------------KEKLAAINE---ATRLRTEaeialKAKEAENERLKRKAEDEAYQR 1925
Cdd:COG4913 468 ---EVRPEEERWRGA-IERVLggfaltllvppehyAAALRWVNRlhlRGRLVYE-----RVRTGLPDPERPRLDPDSLAG 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1926 KL-LEDQAAQH--KHDIQEKIIHLKSSSDSE------------MVRQKTiveeTLRQKkiveeeihiirinfekaskgks 1990
Cdd:COG4913 539 KLdFKPHPFRAwlEAELGRRFDYVCVDSPEElrrhpraitragQVKGNG----TRHEK---------------------- 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1991 DLENELKKLKVIAEETQKsKLKA-EAEAEKLkklaaeeekkrkeseekvkriTAAEEEAARQCKAAQEEVARLEKKADEA 2069
Cdd:COG4913 593 DDRRRIRSRYVLGFDNRA-KLAAlEAELAEL---------------------EEELAEAEERLEALEAELDALQERREAL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2070 NKQKEKAEKEaekqvIVAKEAAQKCSSAEQKAQEVLSKNKEdslaqqkmkeeFENAKRLAQAAEKAKEKAEKEAALLRQK 2149
Cdd:COG4913 651 QRLAEYSWDE-----IDVASAEREIAELEAELERLDASSDD-----------LAALEEQLEELEAELEELEEELDELKGE 714
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 2150 AAEAEKQKKSAEEEaakQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKELT 2228
Cdd:COG4913 715 IGRLEKELEQAEEE---LDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELE 790
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1888-2204 |
1.59e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 54.57 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1888 AAINEATRLRTEAEIALKAKEAENERLKR-KAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKsssdsemvRQKTIVEETLR 1966
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLEReKAAREARHKKAAEARAAKDKDAVAAALARVK--------AKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1967 QKKIVEEEihiirinfekaskgKSDLENELKKLKVIAEETQKSKLKAEAEAEKLKKLAAEEEKkrkeseekvkritAAEE 2046
Cdd:PRK05035 508 IKAGARPD--------------NSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIAR-------------AKAK 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2047 EAARQCKAAQEEVARLEKKADEANKQKEKAekeaekqvivAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEfenAK 2126
Cdd:PRK05035 561 KAAQQAANAEAEEEVDPKKAAVAAAIARAK----------AKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAK---AK 627
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 2127 RLAQAAEKAKEKaekeaallrqkAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEA-LKQKKQADA 2204
Cdd:PRK05035 628 KAEQQANAEPEE-----------PVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIArAKAKKAAQQ 695
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1659-1769 |
1.64e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 54.11 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1659 EQLRKQQEEANKAREQAEKELETWRQKANEALRL-RLQAEEEAQKKSKTQEEAERQKVEAERDAK---KRAKAEDAALKQ 1734
Cdd:COG2268 192 RKIAEIIRDARIAEAEAERETEIAIAQANREAEEaELEQEREIETARIAEAEAELAKKKAEERREaetARAEAEAAYEIA 271
|
90 100 110
....*....|....*....|....*....|....*...
gi 736215636 1735 KDNAEKELEKQRTFAEQVAQ---QKLSAEQECIRLKAD 1769
Cdd:COG2268 272 EANAEREVQRQLEIAEREREielQEKEAEREEAELEAD 309
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1836-2070 |
1.72e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1836 LLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLK 1915
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1916 RKAE----DEAYQRKLLEDQ-AAQHKHDIQEKIIHLKSSSD-SEMVRQKTIVEETLRQKKiveEEIHIIRINFEKASKGK 1989
Cdd:COG4942 90 KEIAelraELEAQKEELAELlRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARR---EQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1990 SDLENELKKLKVIAEETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEA 2069
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
.
gi 736215636 2070 N 2070
Cdd:COG4942 247 G 247
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1098-2001 |
1.85e-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: 54.67 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1098 VLASQQQISSAPMlrSELDVTLRKMDHVYGLSSiYLDKLKTIDVVIRNTKEAeaaLKTYESRLLDVNKVPENEKEVeeqR 1177
Cdd:TIGR00606 153 VIFCHQEDSNWPL--SEGKALKQKFDEIFSATR-YIKALETLRQVRQTQGQK---VQEHQMELKYLKQYKEKACEI---R 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1178 SQLKSMRAEVEADQVIFDRLQDELRRAstindkmtrihSERDAEMEHYRQLVSSLLERWQVVFAQMDMRQRELDLLGRHM 1257
Cdd:TIGR00606 224 DQITSKEAQLESSREIVKSYENELDPL-----------KNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKM 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1258 NSYNVSYEWLIHWLGEARKRQEKIQavpigGSKALREQLAEEKKLLEEIEKNKDKIDSCQKNAKAYIDSVKDYElQILTY 1337
Cdd:TIGR00606 293 EKVFQGTDEQLNDLYHNHQRTVREK-----ERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQE-HIRAR 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1338 KALQDPMA--SPLKKPKMDCASDNIIQEYVTLRTRYSElmtltsQYIKFITETQRRLEDDEKASEKLKEEERKKMAEIQA 1415
Cdd:TIGR00606 367 DSLIQSLAtrLELDGFERGPFSERQIKNFHTLVIERQE------DEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGR 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1416 ELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQHELHHLKSLSEQEIKSKSQQLEHALVSH 1495
Cdd:TIGR00606 441 TIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1496 TKIEEEIH---TIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAE 1572
Cdd:TIGR00606 521 DQEMEQLNhhtTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKEL 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1573 KEAAKQKQKALDDLQKFKMQAEEAERRM-----KQAEEEKLRQIKvvEEVaqKSAATQLQSHSMSFNVKASKLEESLKKE 1647
Cdd:TIGR00606 601 ASLEQNKNHINNELESKEEQLSSYEDKLfdvcgSQDEESDLERLK--EEI--EKSSKQRAMLAGATAVYSQFITQLTDEN 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1648 QG----------TVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAER--QKV 1715
Cdd:TIGR00606 677 QSccpvcqrvfqTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNklQKV 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1716 EAERDAKKRAKAEDAALKQKDNAEKELEKQrTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSatE 1795
Cdd:TIGR00606 757 NRDIQRLKNDIEEQETLLGTIMPEEESAKV-CLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQ--E 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1796 KQrklleEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQlLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQ 1875
Cdd:TIGR00606 834 KQ-----HELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE-LKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1876 RAEAEKILKEKlaaineaTRLRTEAEIALKAKEAENerlkRKAEDEAYQRKLLEDQAAQHKHDIQEKIIH----LKSSSD 1951
Cdd:TIGR00606 908 KEQDSPLETFL-------EKDQQEKEELISSKETSN----KKAQDKVNDIKEKVKNIHGYMKDIENKIQDgkddYLKQKE 976
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 736215636 1952 SEMVRQKTIVEETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKV 2001
Cdd:TIGR00606 977 TELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKR 1026
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
176-271 |
1.88e-06 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 50.38 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 176 KLLL-WSQrMVEGYQGLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQ-----------------------EN 231
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 736215636 232 LEQAFSVAER-----------DLG-VTRLLDPEDVDVLHPDEKSIITYVSSL 271
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1657-2200 |
1.89e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 54.25 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1657 EAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQaeeEAQKKSKTQEEAERQKVEAERDAKKRAKAeDAALKQ-- 1734
Cdd:NF033838 56 QKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLS---DIKTEYLYELNVLKEKSEAELTSKTKKEL-DAAFEQfk 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1735 KDNAEKElekqrtfaEQVAQ-QKLSAEQEcirLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVrsemd 1813
Cdd:NF033838 132 KDTLEPG--------KKVAEaTKKVEEAE---KKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKE----- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1814 sllkmkteaEKKTMSNTEKSKQlleSEAlKMKQLADEATRLrsvaEEAKKQRQTAEEEAARQRAEAEKILKEKLAAinea 1893
Cdd:NF033838 196 ---------EAKEPRDEEKIKQ---AKA-KVESKKAEATRL----EKIKTDREKAEEEAKRRADAKLKEAVEKNVA---- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1894 trlrteaeialkakEAENERLKRKAedeayQRKLLEDQAAQHKHDIQEKiihlksSSDSEmVRQKTIVEETLR-QKKIVE 1972
Cdd:NF033838 255 --------------TSEQDKPKRRA-----KRGVLGEPATPDKKENDAK------SSDSS-VGEETLPSPSLKpEKKVAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1973 EEIHIirinfEKASKGKSDLENELKK------LKVIAEETQKSKLKA-EAEAEKLKKlaaeeekkrkeseekvkriTAAE 2045
Cdd:NF033838 309 AEKKV-----EEAKKKAKDQKEEDRRnyptntYKTLELEIAESDVKVkEAELELVKE-------------------EAKE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2046 EEAARQCKAAQEEVarlEKKADEANKqkekaekeaekqvivakeaaqkcssaeqkaqevLSKNKEDslaQQKMKEEfenA 2125
Cdd:NF033838 365 PRNEEKIKQAKAKV---ESKKAEATR---------------------------------LEKIKTD---RKKAEEE---A 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 2126 KRLAQAAEKAKEKAEKeaallRQKAAEAEKQKKSA--EEEAAKQAKAQKDAEklkKAAEEEASKRAAAEAEALKQKK 2200
Cdd:NF033838 403 KRKAAEEDKVKEKPAE-----QPQPAPAPQPEKPApkPEKPAEQPKAEKPAD---QQAEEDYARRSEEEYNRLTQQQ 471
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
1694-1936 |
1.97e-06 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 54.72 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1694 LQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALkQKDNAEkelekQRTFAEQVAQQKLSAEQECirlKADFDHA 1773
Cdd:NF033875 41 VQAAELDTQPGTTTVQPDNPDPQSGSETPKTAVSEEATV-QKDTTS-----QPTKVEEVASEKNGAEQSS---ATPNDTT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1774 EQQRGLLDNELQRLKKEVSATEKQRKLLEE--ELAKVRSEMDSLLKMKTEAEK----KTMSNTEKSKQLL----ESEALK 1843
Cdd:NF033875 112 NAQQPTVGAEKSAQEQPVVSPETTNEPLGQptEVAPAENEANKSTSIPKEFETpdvdKAVDEAKKDPNITvvekPAEDLG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1844 MKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKE--KLAAINEATRLRTEAEIAlkakEAENERLKRKAEDE 1921
Cdd:NF033875 192 NVSSKDLAAKEKEVDQLQKEQAKKIAQQAAELKAKNEKIAKEnaEIAAKNKAEKERYEKEVA----EYNKHKNENGYVNE 267
|
250
....*....|....*
gi 736215636 1922 AYQRKLLEDQAAQHK 1936
Cdd:NF033875 268 AISKNLVFDQSVVTK 282
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1421-1622 |
1.97e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.01 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1421 KQIAEAQAKSvikAEQEAQelklKMKEEASKRqdvavdAEQQKQNI----QHELHHLKSLSEQEIKSKSQQLEhalvsht 1496
Cdd:PRK12704 26 KKIAEAKIKE---AEEEAK----RILEEAKKE------AEAIKKEAlleaKEEIHKLRNEFEKELRERRNELQ------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1497 kieeeihtiriQLEMTIKQKK-TAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEA 1575
Cdd:PRK12704 86 -----------KLEKRLLQKEeNLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 736215636 1576 AKQkqkalddlqkfkMQAEEAErrmKQAEEEKLRQIKVVEEVAQKSA 1622
Cdd:PRK12704 155 AKE------------ILLEKVE---EEARHEAAVLIKEIEEEAKEEA 186
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1458-1907 |
1.99e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 54.44 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1458 DAEQQKQNIQHELHHLKSLSEQEIKSKSQQLEHALVSHTKIEeeihtiriQLEMTIKQKktaESELQQLRDKAAEAEKLR 1537
Cdd:pfam10174 251 DLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKID--------QLKQELSKK---ESELLALQTKLETLTNQN 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1538 KAAQEDAERLRKQVAEETQKK---KNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVV 1614
Cdd:pfam10174 320 SDCKQHIEVLKESLTAKEQRAailQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1615 EEVAQ----------------KSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANkarEQAEKE 1678
Cdd:pfam10174 400 QKKIEnlqeqlrdkdkqlaglKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEEL---ESLKKE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1679 LETWRQKANEalrLRLQAEEEAQKKSKTQEEAERQkveAERDAKK--RAKAEDAALKQKDNAEKELEKQRTFAEQVAqqk 1756
Cdd:pfam10174 477 NKDLKEKVSA---LQPELTEKESSLIDLKEHASSL---ASSGLKKdsKLKSLEIAVEQKKEECSKLENQLKKAHNAE--- 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1757 lsaeqECIRLKADFDhaeqqrglldNELQRLKKEVSatekqrkLLEEELAKVRSEMDSLLKMKTEAEkktMSNTEKSKQL 1836
Cdd:pfam10174 548 -----EAVRTNPEIN----------DRIRLLEQEVA-------RYKEESGKAQAEVERLLGILREVE---NEKNDKDKKI 602
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736215636 1837 LESEALKMKQLADEATRLRSV----AEEAKKQRQTAEEEAARQRAEAEKILKEKLAAI-NEATRLRTEAEiALKAK 1907
Cdd:pfam10174 603 AELESLTLRQMKEQNKKVANIkhgqQEMKKKGAQLLEEARRREDNLADNSQQLQLEELmGALEKTRQELD-ATKAR 677
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1499-1759 |
2.31e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1499 EEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQ 1578
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1579 KQKALDDLQKFKM--QAEEAerrmkqaeEEKLRQIKVVEEVAQKSAatqlqshsmsfnvkasKLEESLKKEQGTVLQLQE 1656
Cdd:COG3883 95 LYRSGGSVSYLDVllGSESF--------SDFLDRLSALSKIADADA----------------DLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1657 EAEQLRKQQEEANKAREQAEKELETwRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKD 1736
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEA-QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
250 260
....*....|....*....|...
gi 736215636 1737 NAEKELEKQRTFAEQVAQQKLSA 1759
Cdd:COG3883 230 AAAAAAAAAAAAAAASAAGAGAA 252
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1548-1759 |
2.61e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 53.34 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1548 RKQVAEETQKKKnaedelKRKSEAEKEAAKQKqkalddlqkfkmqaEEAERRMKQAEEEKLRQIKVVEeVAQKSAATQLQ 1627
Cdd:COG2268 191 RRKIAEIIRDAR------IAEAEAERETEIAI--------------AQANREAEEAELEQEREIETAR-IAEAEAELAKK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1628 shsmsfnvkaskleeslkkeqgtvlqlQEEAEQlrkqqeEANKAREQAEKELETwrQKANEALRLRLQAEEEAQKKSKTQ 1707
Cdd:COG2268 250 ---------------------------KAEERR------EAETARAEAEAAYEI--AEANAEREVQRQLEIAEREREIEL 294
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 736215636 1708 EEAERQKVEAERDA--KKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSA 1759
Cdd:COG2268 295 QEKEAEREEAELEAdvRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAE 348
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
49-157 |
2.68e-06 |
|
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: 49.34 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 49 CADERDRVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRF----HKLQNVQIALDFLK 124
Cdd:cd21306 9 HAPDKLNVVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQ 88
|
90 100 110
....*....|....*....|....*....|...
gi 736215636 125 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 157
Cdd:cd21306 89 DAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1438-1825 |
2.68e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 53.36 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1438 AQELKLKMKEEASKRQDVAVDAEQQKQNIQHELHHLKSLSEQ------EIKSKSQQLEHALVSHTKIEEEihtiriqLEM 1511
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQwerqrrELESRVAELKEELRQSREKHEE-------LEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1512 TIKQKKTAESELQQLRDKAAEAeklRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQ--KF 1589
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLAQ---RAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKqlQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1590 KMQAEEAERRMKQAEEEKLRQI---KVVEEVAQKSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQL---QEEAEQLRK 1663
Cdd:pfam07888 179 KLQQTEEELRSLSKEFQELRNSlaqRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLnasERKVEGLGE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1664 QQEEANKAREQAEKELETWRQKANEaLRLRLQAEEEAQKKSKTQEEAERQKVE--AERDAKKRAKAEDAALKqkdnAEKE 1741
Cdd:pfam07888 259 ELSSMAAQRDRTQAELHQARLQAAQ-LTLQLADASLALREGRARWAQERETLQqsAEADKDRIEKLSAELQR----LEER 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1742 LEKQRTfAEQVAQQKLSAEQECIRLkadfdhaeqQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSL-LKMKT 1820
Cdd:pfam07888 334 LQEERM-EREKLEVELGREKDCNRV---------QLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLeQRLET 403
|
....*
gi 736215636 1821 EAEKK 1825
Cdd:pfam07888 404 VADAK 408
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1733-1939 |
2.78e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 53.27 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1733 KQKDNAEKELEKQRTFAEQVA--QQKLSAEQEciRLKADfdhaEQQRgLLDNELQRLKKEVSATEKQRKLLEEELAKVRS 1810
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEelQQKQAAEQE--RLKQL----EKER-LAAQEQKKQAEEAAKQAALKQKQAEEAAAKAA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1811 EMdslLKMKTEAEKKTMSNTEKskqllESEALKMKQLADEATRlrSVAEEAKKQrqtAEEEAARQ-----RAEAEKILKE 1885
Cdd:PRK09510 143 AA---AKAKAEAEAKRAAAAAK-----KAAAEAKKKAEAEAAK--KAAAEAKKK---AEAEAAAKaaaeaKKKAEAEAKK 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 736215636 1886 KLAAINEAtrlRTEAEIALKAKEAENERlKRKAEDEAYQRKLLEDQAAQHKHDI 1939
Cdd:PRK09510 210 KAAAEAKK---KAAAEAKAAAAKAAAEA-KAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1478-1746 |
2.99e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1478 EQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQK 1557
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1558 KKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQSHSMSFNVKA 1637
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1638 SKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEA 1717
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
250 260
....*....|....*....|....*....
gi 736215636 1718 ERDAKKRAKAEDAALKQKDNAEKELEKQR 1746
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGA 312
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2258-2466 |
3.12e-06 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 53.16 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2258 AVKQKAQvedelakvriQMDELLKlKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSveaeetaRQRQIAE 2337
Cdd:PRK11637 62 SVRQQQQ----------QRASLLA-QLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLE-------QQQAAQE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2338 SNLAEQRALA----------------EKMLKEKM--------QAIQEA-TKLKAEAQELQKQKDQAQEK---AKKLLEDK 2389
Cdd:PRK11637 124 RLLAAQLDAAfrqgehtglqlilsgeESQRGERIlayfgylnQARQETiAELKQTREELAAQKAELEEKqsqQKTLLYEQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2390 QQIQQRLDKETEGFQKSLEAerkrqLEVSAEAE-----TLRLKVKELSDAQSKAENEAK-KFKKQADEAkARLKDTEKQS 2463
Cdd:PRK11637 204 QAQQQKLEQARNERKKTLTG-----LESSLQKDqqqlsELRANESRLRDSIARAEREAKaRAEREAREA-ARVRDKQKQA 277
|
...
gi 736215636 2464 TET 2466
Cdd:PRK11637 278 KRK 280
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1701-2068 |
3.29e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1701 QKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLL 1780
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1781 DNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAEE 1860
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1861 AKKQRQTAEEeaaRQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQ 1940
Cdd:COG4372 166 LAALEQELQA---LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1941 EKIIHLKSSSDSEMVRQKTIVEETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKVIAEETQKSKLKAEAEAEKL 2020
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 736215636 2021 KKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADE 2068
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1522-1718 |
3.34e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1522 ELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKrksEAEKEAAKQKQkalddlqkfkmQAEEAERRMK 1601
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE---DLEKEIKRLEL-----------EIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1602 QAEEeKLRQIKVVEEVAQksaatqlqshsmsfnvkASKLEESLKKEQGT----VLQLQEEAEQLRKQQEEANKAREQAEK 1677
Cdd:COG1579 77 KYEE-QLGNVRNNKEYEA-----------------LQKEIESLKRRISDledeILELMERIEELEEELAELEAELAELEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 736215636 1678 ELETWRQKANEALRlRLQAEEEAQKKsktQEEAERQKVEAE 1718
Cdd:COG1579 139 ELEEKKAELDEELA-ELEAELEELEA---EREELAAKIPPE 175
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1738-1934 |
3.36e-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: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1738 AEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLK 1817
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1818 mkteAEKKTMSNTEKSKQLLESEAL---------------KMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKI 1882
Cdd:COG3883 94 ----ALYRSGGSVSYLDVLLGSESFsdfldrlsalskiadADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 736215636 1883 LKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQ 1934
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1808-2482 |
3.68e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1808 VRSEMDSLLKMKTEA-----------EKKTMSNTEKSKQLLESEALKMKQLadEATRLRsvAEEAKkqrqTAEEEAARQR 1876
Cdd:PRK02224 114 VREEVTELLRMDAEAfvncayvrqgeVNKLINATPSDRQDMIDDLLQLGKL--EEYRER--ASDAR----LGVERVLSDQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1877 AEAEKILKEKLAAINEA---TRLrTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKhDIQEKIIHLKssSDSE 1953
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKdlhERL-NGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE-ERREELETLE--AEIE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1954 MVRQKtiVEETLRQKKIVEEEIHIIRinfekasKGKSDLENELKKLkviAEETQKSKLKAEAEAEKLKKLAAEEEKKRKE 2033
Cdd:PRK02224 262 DLRET--IAETEREREELAEEVRDLR-------ERLEELEEERDDL---LAEAGLDDADAEAVEARREELEDRDEELRDR 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2034 SEEKVKRITAAEEEAARqckaAQEEVARLEKKADEankqkekaekeaekqvivAKEAAQKCSSAEQKAQEVLSKNKEdsl 2113
Cdd:PRK02224 330 LEECRVAAQAHNEEAES----LREDADDLEERAEE------------------LREEAAELESELEEAREAVEDRRE--- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2114 AQQKMKEEFENakrlaqaaekakekaekeaalLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEklKKAAEEEASKRAA--- 2190
Cdd:PRK02224 385 EIEELEEEIEE---------------------LRERFGDAPVDLGNAEDFLEELREERDELR--EREAELEATLRTArer 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2191 -AEAEALKQkkqadaemAKHKKEADQALKLKSQVEkeltmvklRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDeL 2269
Cdd:PRK02224 442 vEEAEALLE--------AGKCPECGQPVEGSPHVE--------TIEEDRERVEELEAELEDLEEEVEEVEERLERAED-L 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2270 AKVRIQMDELlklklkieEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAESNlAEQRALAEK 2349
Cdd:PRK02224 505 VEAEDRIERL--------EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE-AEEAREEVA 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2350 MLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKslEAERKRQLEVSAEA---ETLRL 2426
Cdd:PRK02224 576 ELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAE--KRERKRELEAEFDEariEEARE 653
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 736215636 2427 KVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTETVVQKLETQRLQSTREA 2482
Cdd:PRK02224 654 DKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEA 709
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2147-2474 |
3.84e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.42 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2147 RQKAAEAEKQkkSAEEEAAKQAKAQKDAEKLK--KAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALK-LKSQV 2223
Cdd:COG3096 321 RESDLEQDYQ--AASDHLNLVQTALRQQEKIEryQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDsLKSQL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2224 ekeltmvklrldeTDKQKALldEELQRVKGEVNDAVKQKAQvedelAKVRIQMDELLKLKlkIEEQNRSLMKKDKDKTQK 2303
Cdd:COG3096 399 -------------ADYQQAL--DVQQTRAIQYQQAVQALEK-----ARALCGLPDLTPEN--AEDYLAAFRAKEQQATEE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2304 VLAEEAgkmkslaeeaaRLSVeAEETARQrqiaesnLAEQRALAEKMLKE--KMQAIQEATKLKAEAQELQKQKDQAQEK 2381
Cdd:COG3096 457 VLELEQ-----------KLSV-ADAARRQ-------FEKAYELVCKIAGEveRSQAWQTARELLRRYRSQQALAQRLQQL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2382 AKKL--LEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDT 2459
Cdd:COG3096 518 RAQLaeLEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKEL 597
|
330 340
....*....|....*....|
gi 736215636 2460 EKQSTE-----TVVQKLETQ 2474
Cdd:COG3096 598 AARAPAwlaaqDALERLREQ 617
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1534-1730 |
3.96e-06 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 53.08 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1534 EKLRKAAQEDAERLRkqvaEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKV 1613
Cdd:pfam05262 184 EALREDNEKGVNFRR----DMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1614 VEEVAQKSAATQlqshsmsfnvkASKLEESLKKEqgtVLQLQEEAEqlrKQQEEANKAREQAEKELetwRQKANEALRLR 1693
Cdd:pfam05262 260 LPKPADTSSPKE-----------DKQVAENQKRE---IEKAQIEIK---KNDEEALKAKDHKAFDL---KQESKASEKEA 319
|
170 180 190
....*....|....*....|....*....|....*..
gi 736215636 1694 LQAEEEAQKKSKTQEEaERQKVEAERDAKKRAKAEDA 1730
Cdd:pfam05262 320 EDKELEAQKKREPVAE-DLQKTKPQVEAQPTSLNEDA 355
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2327-2666 |
4.00e-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: 53.20 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2327 EETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKEtegfQKS 2406
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKE----EKA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2407 LEAERKRQLEvsaEAETLRlkvkelsdaQSKAENEAKKFKKQADEAKARLKDTEKQSTETVVQKLETQRlqstreadglK 2486
Cdd:pfam17380 310 REVERRRKLE---EAEKAR---------QAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIR----------Q 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2487 EAIADLEKEREKLKKEAEELQNKSnkmantqkEEIEQQKAIIQKSFISERElllkRQKAVEDEKKKLQK--QFEDEVKKA 2564
Cdd:pfam17380 368 EEIAMEISRMRELERLQMERQQKN--------ERVRQELEAARKVKILEEE----RQRKIQQQKVEMEQirAEQEEARQR 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2565 EALKDEQERQRKLMEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEKKRLDQEKQLGAENQKLREKLQCLEGASKq 2644
Cdd:pfam17380 436 EVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERK- 514
|
330 340
....*....|....*....|..
gi 736215636 2645 satKQVASKTIEVQTDVVSEEQ 2666
Cdd:pfam17380 515 ---RKLLEKEMEERQKAIYEEE 533
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
172-269 |
4.01e-06 |
|
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: 48.62 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 172 TAKEKLLLWSQRMVEGyqgLRCDNFTTGWRDGKLFNAIIHKHRPTLI-DMGKVYRQSNQENLEQAFSVAERDLGVTRLLD 250
Cdd:cd21315 16 TPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIK 92
|
90
....*....|....*....
gi 736215636 251 PEDVDVLHPDEKSIITYVS 269
Cdd:cd21315 93 PEEMVNPKVDELSMMTYLS 111
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2197-2384 |
4.08e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2197 KQKKQADAEMAKHKKEADQALKLKSQVEKELTmvklRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKvriqm 2276
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQE----RLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAK----- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2277 dELLKLKLKIEEQNRSLM---KKDKDKTQKVLAEEAGK-----MKSLAEEAARLSVEAEETARQRQIAESN---LAEQRA 2345
Cdd:PRK09510 141 -AAAAAKAKAEAEAKRAAaaaKKAAAEAKKKAEAEAAKkaaaeAKKKAEAEAAAKAAAEAKKKAEAEAKKKaaaEAKKKA 219
|
170 180 190
....*....|....*....|....*....|....*....
gi 736215636 2346 LAEKmlkeKMQAIQEATKLKAEAQELQKQKDQAQEKAKK 2384
Cdd:PRK09510 220 AAEA----KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAK 254
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2306-2621 |
4.13e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.95 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2306 AEEAGKMKSLaEEAARLSVEAEETARQRQIAE---SNLAEQRALAEKM-LKEKMQAIQEAT-KLKAEAQELQKQKDQAQE 2380
Cdd:pfam02029 16 REERRRQKEE-EEPSGQVTESVEPNEHNSYEEdseLKPSGQGGLDEEEaFLDRTAKREERRqKRLQEALERQKEFDPTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2381 KAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKArlKDTE 2460
Cdd:pfam02029 95 DEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEE--VPTE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2461 KQSTETVVQKLETQRLQSTREADGL---KEAIADLEKEREKLKKEAEELQNKSNKMANTQKEEIEQQKAIIQKSFISERE 2537
Cdd:pfam02029 173 NFAKEEVKDEKIKKEKKVKYESKVFldqKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2538 LLLKRQKAVEDEKKKL-QKQFEDEVKKAEaLKDEQERQRKLMEEEKKKlqaimdaavKKQKEAEADMKNKQtemevlEKK 2616
Cdd:pfam02029 253 LRRRRQEKESEEFEKLrQKQQEAELELEE-LKKKREERRKLLEEEEQR---------RKQEEAERKLREEE------EKR 316
|
....*
gi 736215636 2617 RLDQE 2621
Cdd:pfam02029 317 RMKEE 321
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
660-752 |
4.19e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 48.09 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 660 HAFVIAATKELMWLNEKEEEEVNYDWSERNTNMTAKKDNYSGLMRDLELREKKVNVVQATGDKLLRDGHPARKTVEAFTG 739
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 736215636 740 ALQTQWSWLLQLC 752
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1385-1599 |
4.29e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1385 ITETQRRLED---DEKASEKLKEEERKKMAEIQAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQ 1461
Cdd:COG4942 22 AAEAEAELEQlqqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1462 QKQNIQHELHHLKSLSEQEIKS--KSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKKTaesELQQLRDKAAEAEKLRKA 1539
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLAllLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA---ELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736215636 1540 AQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKF--KMQAEEAERR 1599
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAA 240
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1508-1707 |
5.02e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 52.65 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1508 QLEMTIKQKKTAESELQ------QLRDKAAEAEKLRKAAQEDAERLRKQVAEEtqKKKNAEDELKRKseaekeaakqkqk 1581
Cdd:pfam15709 367 QLERAEKMREELELEQQrrfeeiRLRKQRLEEERQRQEEEERKQRLQLQAAQE--RARQQQEEFRRK------------- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1582 aLDDLQKfKMQAEEAERrmkqAEEEKLRQikvveevaqksaatqlqshsmsfnvkaSKLEESLKKEQGTVLQLQEEA--E 1659
Cdd:pfam15709 432 -LQELQR-KKQQEEAER----AEAEKQRQ---------------------------KELEMQLAEEQKRLMEMAEEErlE 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 736215636 1660 QLRKQQEEANKAREQAEKEletwRQKANEALRLrlqAEEEAQKKSKTQ 1707
Cdd:pfam15709 479 YQRQKQEAEEKARLEAEER----RQKEEEAARL---ALEEAMKQAQEQ 519
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1532-1878 |
5.41e-06 |
|
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: 52.99 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1532 EAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDlqkfkmQAEEAERRMKQAEEEKLRQI 1611
Cdd:pfam15964 357 QCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQ------NVAQLEAQVEKVTREKNSLV 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1612 KVVEEvaqksAATQLQSHSMSFNvkaskleeslkkeqgtvlqlqEEAEQLRKQQEEANKAREQAEKELETWRQKANEALR 1691
Cdd:pfam15964 431 SQLEE-----AQKQLASQEMDVT---------------------KVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLE 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1692 LRLQAEEeaqkKSKTQEEAERQKVEAERDAKKRAKAEDAALKQK-DNAEKEL-----EK---QRTFAEQVAQQKLSAEQE 1762
Cdd:pfam15964 485 IKDQEIE----KLGLELSESKQRLEQAQQDAARAREECLKLTELlGESEHQLhltrlEKesiQQSFSNEAKAQALQAQQR 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1763 CIRLKADFDHAEQQRGLLDNE-----------LQRLKKEVSATEKQrklLEEELAKVRSEMDSLLK----MKTEAEKKTM 1827
Cdd:pfam15964 561 EQELTQKMQQMEAQHDKTVNEqyslltsqntfIAKLKEECCTLAKK---LEEITQKSRSEVEQLSQekeyLQDRLEKLQK 637
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736215636 1828 SNTEKSKQLL------ESEALKMKQL-------ADEATRLRSVAEEAKKQRQTAEEEAARQRAE 1878
Cdd:pfam15964 638 RNEELEEQCVqhgrmhERMKQRLRQLdkhcqatAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQ 701
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2162-2395 |
5.82e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2162 EEAAKQAKA-----QKDAEKLKKAAEEEASKRAAAEAEALKQK-KQADAEMAKHKK---------EADQALKLKSQVEKE 2226
Cdd:COG3206 148 ELAAAVANAlaeayLEQNLELRREEARKALEFLEEQLPELRKElEEAEAALEEFRQknglvdlseEAKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2227 LTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKA--QVEDELAKVRIQMDELlklklkieeqnRSLMKKDKDKTQKV 2304
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAEL-----------SARYTPNHPDVIAL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2305 LAEEAGKMKSLAEEAARLSVEAEetaRQRQIAESNLAEQRALAEKMLKEkmqaIQEATKLKAEAQELQKQKDQAQEKAKK 2384
Cdd:COG3206 297 RAQIAALRAQLQQEAQRILASLE---AELEALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVARELYES 369
|
250
....*....|.
gi 736215636 2385 LLEDKQQIQQR 2395
Cdd:COG3206 370 LLQRLEEARLA 380
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1429-1918 |
5.88e-06 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 52.45 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1429 KSVIKAEQEAQELKLKMKEEaSKRQDVAVdaeqqkQNIQHELHHLKSLSEQEIKSKSQQLEHALVSHTKIEEEIHT-IRI 1507
Cdd:pfam09731 45 EVVLYALGEDPPLAPKPKTF-RPLQPSVV------SAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAeAKA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1508 QLEMTIKQKKTAESELQQLRD-KAAEAEKLRKAAQEDAerlRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDL 1586
Cdd:pfam09731 118 QLPKSEQEKEKALEEVLKEAIsKAESATAVAKEAKDDA---IQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1587 QKFKMQAEeaerrmKQAEEEKLRqikvvEEVAQKSAatqlqshsmsfnvKASKLEESLKKEQGTVLQLQEEAEQLRKQQE 1666
Cdd:pfam09731 195 LKEVINLA------KQSEEEAAP-----PLLDAAPE-------------TPPKLPEHLDNVEEKVEKAQSLAKLVDQYKE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1667 EANKAREQAEKELET--------WR---------------------QKANEAL-RLRLQAEEEAQKKSKTQEEAERQKVE 1716
Cdd:pfam09731 251 LVASERIVFQQELVSifpdiipvLKednllsnddlnsliahahreiDQLSKKLaELKKREEKHIERALEKQKEELDKLAE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1717 AERDAKKRAKAEDAALKQKDNaEKELEKQRtfaeQVAQQKLSAEQEcirlKADFDHAEQQRGLLdnELQRLKKEVSATEK 1796
Cdd:pfam09731 331 ELSARLEEVRAADEAQLRLEF-EREREEIR----ESYEEKLRTELE----RQAEAHEEHLKDVL--VEQEIELQREFLQD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1797 QRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEkskqlLESEALKMKQLADEATRLRSVAEEAKKQRQTA----EEEA 1872
Cdd:pfam09731 400 IKEKVEEERAGRLLKLNELLANLKGLEKATSSHSE-----VEDENRKAQQLWLAVEALRSTLEDGSADSRPRplvrELKA 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 736215636 1873 ARQRAEAEKILKEKLAAINEATRLR-TEAEIALKAKEAENERLKRKA 1918
Cdd:pfam09731 475 LKELASDDEVVKAALASLPEEAYQRgVYTEAALRERFRRVAKEVRKV 521
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1395-1604 |
5.93e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1395 DEKASEKLKEEERKKMAEIQAELDKQKQIAEAQA-KSVIKAEQEAQELKLKMKEEASKrqdvavDAEQQKQNiqhELHHL 1473
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERlKQLEKERLAAQEQKKQAEEAAKQ------AALKQKQA---EEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1474 KSLSEQEIKSKSQQLEHALVShTKIEEEihtirIQLEMTIKQKKTAESELQqlrdKAAEAEKLRKAAQEdaerlRKQVAE 1553
Cdd:PRK09510 140 KAAAAAKAKAEAEAKRAAAAA-KKAAAE-----AKKKAEAEAAKKAAAEAK----KKAEAEAAAKAAAE-----AKKKAE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 736215636 1554 ETQKKKnAEDELKRKSEAEKEAAKQK----QKALDDLQKFKMQAEEAERRMKQAE 1604
Cdd:PRK09510 205 AEAKKK-AAAEAKKKAAAEAKAAAAKaaaeAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1475-1760 |
6.24e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1475 SLSEQEIKSKSQQLEHALVSHtkiEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLrKQVAEE 1554
Cdd:COG1340 7 SSSLEELEEKIEELREEIEEL---KEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL-KEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1555 TQKKKNaedELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQSHSMSFN 1634
Cdd:COG1340 83 LNEKLN---ELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1635 VKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQK 1714
Cdd:COG1340 160 EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 736215636 1715 VEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAE 1760
Cdd:COG1340 240 RELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTE 285
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2326-2526 |
6.36e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2326 AEETARQRQiaesnlaEQRALAEKMLKEKMQAIQEATKLKAE-AQELQKQKDQAQEKAKKLLEDKQQIQQRldKETEGFQ 2404
Cdd:PRK09510 61 VEQYNRQQQ-------QQKSAKRAEEQRKKKEQQQAEELQQKqAAEQERLKQLEKERLAAQEQKKQAEEAA--KQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2405 KSLEAERKRQLEVS---AEAETlrlkvKELSDAQSKAENEAKKF------KKQADEAKARLKDTEKQSTETVVQKLETQR 2475
Cdd:PRK09510 132 KQAEEAAAKAAAAAkakAEAEA-----KRAAAAAKKAAAEAKKKaeaeaaKKAAAEAKKKAEAEAAAKAAAEAKKKAEAE 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 736215636 2476 LQSTREADGLKEAIADLEKEREKLKKEAEELQNKSNKMANTQKEEIEQQKA 2526
Cdd:PRK09510 207 AKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAA 257
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1653-1927 |
6.50e-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: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1653 QLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQkvEAERDAK-KRAKAEDAA 1731
Cdd:pfam15558 43 KRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQ--ENQRQEKlERARQEAEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1732 LKQkdnaekelEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSE 1811
Cdd:pfam15558 121 RKQ--------CQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1812 MDSLLKmKTEAEKKTMSNTEKSKQLLESEALKMKQLADEAT----RLRSVAEEAKKQRQT------AEEEAARQRAE--A 1879
Cdd:pfam15558 193 AEELLR-RLSLEQSLQRSQENYEQLVEERHRELREKAQKEEeqfqRAKWRAEEKEEERQEhkealaELADRKIQQARqvA 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 736215636 1880 EKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKL 1927
Cdd:pfam15558 272 HKTVQDKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKKE 319
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1641-1941 |
6.51e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1641 EESLKKEQGTVLQLQEEAEQLrkqqEEANKAREQAEKELETWRQKANEALRL-----RLQAE-EEAQKKSKTQEEA--ER 1712
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELAEL----NEAESDLEQDYQAASDHLNLVQTALRQqekieRYQADlEELEERLEEQNEVveEA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1713 QKVEAERDAKKRAKAE--DAALKQKDNAEKELEKQRTFAEQV--AQQKLSAEQECIRLkADFDhAEQQRGLLDnELQRlk 1788
Cdd:PRK04863 375 DEQQEENEARAEAAEEevDELKSQLADYQQALDVQQTRAIQYqqAVQALERAKQLCGL-PDLT-ADNAEDWLE-EFQA-- 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1789 KEVSATEK----QRKLLEEELAKVRSE--MDSLLKMKTEAEKKTMSNTEKSkqlLESEALKMKQLADEATRLRSVAEEAK 1862
Cdd:PRK04863 450 KEQEATEEllslEQKLSVAQAAHSQFEqaYQLVRKIAGEVSRSEAWDVARE---LLRRLREQRHLAEQLQQLRMRLSELE 526
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 1863 kQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAeialkakEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQE 1941
Cdd:PRK04863 527 -QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEEL-------EARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3108-3141 |
7.18e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.55 E-value: 7.18e-06
10 20 30
....*....|....*....|....*....|....
gi 736215636 3108 LLEAQAATGFVIDPVKNERVTVDEAVKSGLVGPE 3141
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2313-2460 |
7.20e-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: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2313 KSLAEEAARLSVEAEETARQRQIAESNLAEQralAEKMLKEKMQAIQEATKLKAEAQElQKQKDQAQEKAKKLLEDKQQI 2392
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQ---AEEAEKQRAAEQARQKELEQRAAA-EKAAKQAEQAAKQAEEKQKQA 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736215636 2393 QQRLDKETEGFQKSLEAERKRQLEVSAE--AETLRLKvKELSDAQSKAENEAKKFK---KQADEAKARLKDTE 2460
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAkqAEEEAKA-KAAAEAKKKAEEAKKKAEaeaKAKAEAEAKAKAEE 193
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1557-2183 |
7.34e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1557 KKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEaerRMKQAEEeklrQIKVVEevaqkSAATQLQSHSMSFNVK 1636
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEE---KINNSNN----KIKILE-----QQIKDLNDKLKKNKDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1637 ASKLEESLKKeqgTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLrlqaEEEAQKKSKTQEEAERQKVE 1716
Cdd:TIGR04523 98 INKLNSDLSK---INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK----EKELEKLNNKYNDLKKQKEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1717 AERDAKKRAKAEDAALKQKDNAEKELEKQRTF---AEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSA 1793
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLlsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1794 TEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKtMSNTEKSKQLLESEALKMKQLADEATrLRSVAEEAKKQRqtaeeeaa 1873
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKK-IKELEKQLNQLKSEISDLNNQKEQDW-NKELKSELKNQE-------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1874 RQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQeKIIHLKSSSDSE 1953
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1954 MVRQKTI-------VEETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKVIAEETQKSKLKAEAEAEKLKKLAAE 2026
Cdd:TIGR04523 400 IQNQEKLnqqkdeqIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2027 EEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAekqvivaKEAAQKCSSAEQKAQEVLS 2106
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK-------KEKESKISDLEDELNKDDF 552
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 2107 KNKEDSLAQQKMKEEfENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEE 2183
Cdd:TIGR04523 553 ELKKENLEKEIDEKN-KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
52-160 |
7.34e-06 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 48.06 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 52 ERDRVQKKTFTKWVNKhlMKSQRHITDLYEDLRDGHNLISLLEV---------LSGETLPREKGRMRfhKLQNVQIALDF 122
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 736215636 123 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 160
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1985-2227 |
8.17e-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: 51.69 E-value: 8.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1985 ASKGKSDLENELKKLKVIAEETQKSKLKAEAEAEKLKKlaaeeekkrkeseeKVKRITAAEEEAARQCKAAQEEVARLEK 2064
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK--------------QLAALERRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2065 KADEANKQKEKAEkeaekqvivAKEAAQKCSSAEQ--KAQEVLSKNKEDSLAQQkmkEEFENAKRLAQAAEKAKEKAEKE 2142
Cdd:COG4942 84 ELAELEKEIAELR---------AELEAQKEELAELlrALYRLGRQPPLALLLSP---EDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2143 AALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQ 2222
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
....*
gi 736215636 2223 VEKEL 2227
Cdd:COG4942 232 LEAEA 236
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3977-4015 |
8.66e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.40 E-value: 8.66e-06
10 20 30
....*....|....*....|....*....|....*....
gi 736215636 3977 YLEGTSCIAGVYVESSKDRLSIYQAMKKNMIRPGTAFEL 4015
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2159-2447 |
9.00e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2159 SAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVE---KELTMVKLRLD 2235
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDelnEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2236 ETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQNRsLMKKDKDKTQKvlAEEAGKMKSL 2315
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKE-LVEKIKELEKE--LEKAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2316 AEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQR 2395
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 736215636 2396 LDKetegFQKSLEAERKRQLEVSaeaetlrlKVKELSDAQSKAENEAKKFKK 2447
Cdd:COG1340 239 LRE----LRKELKKLRKKQRALK--------REKEKEELEEKAEEIFEKLKK 278
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1663-1815 |
1.00e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 51.94 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1663 KQQEEAnkAREQAEKeLETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKEL 1742
Cdd:PTZ00491 662 KSQEAA--ARHQAEL-LEQEARGRLERQKMHDKAKAEEQRTKLLELQAESAAVESSGQSRAEALAEAEARLIEAEAEVEQ 738
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736215636 1743 EKQRTFAEqvaqqKLSAEQECirlkadfdhaEQQRGLLDNELQRLKKEVS-ATEKQRKLLEEELAKVRSEMDSL 1815
Cdd:PTZ00491 739 AELRAKAL-----RIEAEAEL----------EKLRKRQELELEYEQAQNElEIAKAKELADIEATKFERIVEAL 797
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1411-1606 |
1.00e-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: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1411 AEIQAELDKQKQIAEAQAKSVIKAEQEAQELKlKMKEEASKRQdvavdAEQQKQNIQHELHHLKSLSEQEIKSKSQQLEH 1490
Cdd:TIGR02794 73 LEQQAEEAEKQRAAEQARQKELEQRAAAEKAA-KQAEQAAKQA-----EEKQKQAEEAKAKQAAEAKAKAEAEAERKAKE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1491 ALVShtKIEEEihtiRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQED----AERLRKQVAEETQKKKNAEDELK 1566
Cdd:TIGR02794 147 EAAK--QAEEE----AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakakAEAAKAKAAAEAAAKAEAEAAAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 736215636 1567 RKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEE 1606
Cdd:TIGR02794 221 AAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1773-1941 |
1.01e-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: 49.92 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1773 AEQQRGLLDneLQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKmKTEAEKKTMSNTEKSKQLLESEalkMKQLADEAT 1852
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELE---IEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1853 RLRSVAEEAKKQRQ----TAEEE-AARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQrkl 1927
Cdd:COG1579 77 KYEEQLGNVRNNKEyealQKEIEsLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE--- 153
|
170
....*....|....
gi 736215636 1928 LEDQAAQHKHDIQE 1941
Cdd:COG1579 154 LEAELEELEAEREE 167
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1338-1816 |
1.02e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1338 KALQDpMASPLKKPKMdcaSDNIIQEYVTLRTRYSELMTLTSQYIK---FITETQRRLEDDEKASEKLKeeerkkMAEIQ 1414
Cdd:PRK04863 230 KAFQD-MEAALRENRM---TLEAIRVTQSDRDLFKHLITESTNYVAadyMRHANERRVHLEEALELRRE------LYTSR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1415 AELDKQKQIAEAQAKSVikAEQEAQELKLKMK-EEASKRQDVAVDAEQQKQNIQHELHHLKSLSEQeiksksqqlehaLV 1493
Cdd:PRK04863 300 RQLAAEQYRLVEMAREL--AELNEAESDLEQDyQAASDHLNLVQTALRQQEKIERYQADLEELEER------------LE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1494 SHTKIEEEIHTIRIQLEmtiKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLR--KQVAEETQKKKNAEDELKRKSEA 1571
Cdd:PRK04863 366 EQNEVVEEADEQQEENE---ARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQqaVQALERAKQLCGLPDLTADNAED 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1572 EKEAAKQKQKALDDlqkfkmQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATqlqSHSMSFNVKASKLE--ESLKKEQG 1649
Cdd:PRK04863 443 WLEEFQAKEQEATE------ELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEV---SRSEAWDVARELLRrlREQRHLAE 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1650 TVLQLQ---EEAEQLRKQQEEANKAREQAEKELEtwrqkanealrLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAK 1726
Cdd:PRK04863 514 QLQQLRmrlSELEQRLRQQQRAERLLAEFCKRLG-----------KNLDDEDELEQLQEELEARLESLSESVSEARERRM 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1727 AEDAALKQKDNAEKELEKQRTfAEQVAQQKLSAEQECIrlKADFDHAEQqrglLDNELQRLKKEVSATEKQRKLLEEELA 1806
Cdd:PRK04863 583 ALRQQLEQLQARIQRLAARAP-AWLAAQDALARLREQS--GEEFEDSQD----VTEYMQQLLERERELTVERDELAARKQ 655
|
490
....*....|
gi 736215636 1807 KVRSEMDSLL 1816
Cdd:PRK04863 656 ALDEEIERLS 665
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1422-1623 |
1.02e-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: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1422 QIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQHElhhlKSLSEQEIKSKSQQLEHALvshTKIEEE 1501
Cdd:TIGR02794 36 EIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQ----RAAEQARQKELEQRAAAEK---AAKQAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1502 ihtiriqlemtiKQKKTAESELQQLRDKAAEAEKLRKAAQEdAERLRKQvAEETQKKKNAEDELKRKSEAEKEAAKQKQK 1581
Cdd:TIGR02794 109 ------------QAAKQAEEKQKQAEEAKAKQAAEAKAKAE-AEAERKA-KEEAAKQAEEEAKAKAAAEAKKKAEEAKKK 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 736215636 1582 ALDDLQKfkmqAEEAERrmKQAEEEKLRQIKVVEEVAQKSAA 1623
Cdd:TIGR02794 175 AEAEAKA----KAEAEA--KAKAEEAKAKAEAAKAKAAAEAA 210
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1290-1824 |
1.17e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1290 KALREQLAEEKKLLEEIEKNKDKIDSCQKNAKAYIDSVKDYELQILTYKAlqdpmasplKKPKMDCASDNIIQEYVTLRT 1369
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEK---------EKLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1370 RYSELMTltsqYIKFITETQRRLEDDEKASEKLKEEERKKMAEIQaelDKQKQIAEAQAK-SVIKAEQEAQELKLKMKEE 1448
Cdd:TIGR04523 202 LLSNLKK----KIQKNKSLESQISELKKQNNQLKDNIEKKQQEIN---EKTTEISNTQTQlNQLKDEQNKIKKQLSEKQK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1449 ASKRQDVAVDA-EQQKQNIQHELHHLKSLSEQ--------EIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKKTA 1519
Cdd:TIGR04523 275 ELEQNNKKIKElEKQLNQLKSEISDLNNQKEQdwnkelksELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1520 ESELQ----QLRDKAAEAEKLRKAAQEDaerlrkqvAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEE 1595
Cdd:TIGR04523 355 ESENSekqrELEEKQNEIEKLKKENQSY--------KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1596 AERRMKQAEEEKLRQIKVVEE--VAQKSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKARE 1673
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNqdSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1674 QAEKELETWRQKANEalrlrLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTfaeqvA 1753
Cdd:TIGR04523 507 ELEEKVKDLTKKISS-----LKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQ-----T 576
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736215636 1754 QQKLSAEQEciRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEK 1824
Cdd:TIGR04523 577 QKSLKKKQE--EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2040-2482 |
1.18e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2040 RITAAEEEAA--RQCKA------AQEEVARLEKKADEANKQkekaekeaekqvivAKEAAQKCSSAEQKAQEVlsKNKED 2111
Cdd:COG4913 263 RYAAARERLAelEYLRAalrlwfAQRRLELLEAELEELRAE--------------LARLEAELERLEARLDAL--REELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2112 SLAQQKMKEefeNAKRLAQaaekakekaekeaalLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEkLKKAAEEEASKRAAA 2191
Cdd:COG4913 327 ELEAQIRGN---GGDRLEQ---------------LEREIERLERELEERERRRARLEALLAALG-LPLPASAEEFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2192 EAEALKQkkQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKA-------- 2263
Cdd:COG4913 388 EAAALLE--ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEaelpfvge 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2264 --QVEDE-------------------------LAKVRIQMDEL-LKLKLKIEEqnrslMKKDKDKTQKVLAEE---AGKM 2312
Cdd:COG4913 466 liEVRPEeerwrgaiervlggfaltllvppehYAAALRWVNRLhLRGRLVYER-----VRTGLPDPERPRLDPdslAGKL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2313 K------------SLAEEAARLSVEAEET-----------------------------ARQRQIAESNlAEQRALAEKML 2351
Cdd:COG4913 541 DfkphpfrawleaELGRRFDYVCVDSPEElrrhpraitragqvkgngtrhekddrrriRSRYVLGFDN-RAKLAALEAEL 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2352 KEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLE------DKQQIQQRLDkETEGFQKSLEA------ERKRQLE-VS 2418
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIA-ELEAELERLDAssddlaALEEQLEeLE 698
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736215636 2419 AEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTETVVQKLETQRLQSTREA 2482
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2269-2636 |
1.21e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2269 LAKVRIQMDELLKLKLKIEEQNRSLMKkDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAESNLA--EQRAL 2346
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2347 AEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRL 2426
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2427 KVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQstETVVQKLETQRLQSTR--------EADGLKEAIADLEKEREK 2498
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALE--ERLKEARLLLLIAAALlallglggSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2499 LKKEAEELQNKSNKMANTQKEEIEQQKAIIQKSFISERELLLKRQKAVEDEKKKLQKQFEDEVKKAEALKDEQERQRKL- 2577
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELq 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 2578 MEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEKKRLDQEKQLGAENQKLREKLQ 2636
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE 423
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1514-1720 |
1.24e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1514 KQKKTAESEL--QQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKknAEDELKRKSEAEKEAAKQKQKalddlqkfkm 1591
Cdd:PRK09510 102 RLKQLEKERLaaQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAK--AEAEAKRAAAAAKKAAAEAKK---------- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1592 qAEEAERRMKQAEEEKLrqiKVVEEVAQKSAAtqlqshsmsfnvkaskleeslkkeqgtvlQLQEEAEQLRKQQEEAnKA 1671
Cdd:PRK09510 170 -KAEAEAAKKAAAEAKK---KAEAEAAAKAAA-----------------------------EAKKKAEAEAKKKAAA-EA 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 736215636 1672 REQAEKELETWRQKANEALRlrlqAEEEAQKKSKTQEEAERQKVEAERD 1720
Cdd:PRK09510 216 KKKAAAEAKAAAAKAAAEAK----AAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1771-2467 |
1.26e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1771 DHAEQQrglLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLlkmKTEAEK-KTMSNTEKSKQLLESEalKMKQLAD 1849
Cdd:TIGR04523 32 DTEEKQ---LEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNS---NNKIKIlEQQIKDLNDKLKKNKD--KINKLNS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1850 EATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEaeiaLKAKEAENERLKRKAEDEAYQRKLLE 1929
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE----LEKLNNKYNDLKKQKEELENELNLLE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1930 DQaaqhKHDIQEKIIHLKSSSDSEMVRQKTIVEETLRQKKIVEEEIHIIRINfEKASKGKSDLENELKKLKVIAEETQKS 2009
Cdd:TIGR04523 180 KE----KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQN-NQLKDNIEKKQQEINEKTTEISNTQTQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2010 KLKAEAEAEKLKKlaaeeekkrkeseekvkritaaeeeaarQCKAAQEEVARLEKKADEANKQKekaekeaekqvivaKE 2089
Cdd:TIGR04523 255 LNQLKDEQNKIKK----------------------------QLSEKQKELEQNNKKIKELEKQL--------------NQ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2090 AAQKCSSAEQKAQEVLSKNkedslaqqkMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAE-EEAAKQA 2168
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNKE---------LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsENSEKQR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2169 KAQKDAEKLKKAAEEEASKRAaaEAEALKQKKQadaemakhkkEADQALKLKSQVEKELtmvKLRLDETDKQKALLDEEL 2248
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQ--EIKNLESQIN----------DLESKIQNQEKLNQQK---DEQIKKLQQEKELLEKEI 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2249 QRVKGEVNDAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQNRSL------MKKDKDKTQKVLAEEAGKMKSLAEEAARL 2322
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLsrsinkIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2323 SVEAEETarQRQIAESNLAEQRALAEKMLKE-----------KMQAIQEATKLKAEAQELQKQKDQ----------AQEK 2381
Cdd:TIGR04523 509 EEKVKDL--TKKISSLKEKIEKLESEKKEKEskisdledelnKDDFELKKENLEKEIDEKNKEIEElkqtqkslkkKQEE 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2382 AKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEK 2461
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIK 666
|
....*.
gi 736215636 2462 QSTETV 2467
Cdd:TIGR04523 667 KIKESK 672
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2146-2494 |
1.29e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2146 LRQKAAEAEKQKKSAEE---EAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKqadaemaKHKKEADQALKLKSQ 2222
Cdd:PRK04863 291 LRRELYTSRRQLAAEQYrlvEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQE-------KIERYQADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2223 VEKELTMVKlrldETDKQKALLDEELQRVKGEVNDAVKQKAQVE---DELAKVRIQMDELLKLKLKIEEQNR-------- 2291
Cdd:PRK04863 364 LEEQNEVVE----EADEQQEENEARAEAAEEEVDELKSQLADYQqalDVQQTRAIQYQQAVQALERAKQLCGlpdltadn 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2292 ------SLMKKDKDKTQKVLAEE-----AGKMKSLAEEAARL------SVEAEETARQRQIAESNLAEQRALAEKM--LK 2352
Cdd:PRK04863 440 aedwleEFQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLREQRHLAEQLqqLR 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2353 EKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELS 2432
Cdd:PRK04863 520 MRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA 599
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 2433 dAQSKAEneakkfkKQADEAKARLKD-------TEKQSTETVVQKLETQRlQSTREADGLKEAIADLEK 2494
Cdd:PRK04863 600 -ARAPAW-------LAAQDALARLREqsgeefeDSQDVTEYMQQLLERER-ELTVERDELAARKQALDE 659
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4185-4213 |
1.34e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.78 E-value: 1.34e-05
10 20
....*....|....*....|....*....
gi 736215636 4185 VRKRRVVIVDPETGKEMSVYEAYQKGLID 4213
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1638-1943 |
1.36e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1638 SKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEA 1717
Cdd:COG4372 62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1718 ERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQ 1797
Cdd:COG4372 142 QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1798 RKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRA 1877
Cdd:COG4372 222 EAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALL 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736215636 1878 EAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKI 1943
Cdd:COG4372 302 LNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2260-2454 |
1.58e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 50.61 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2260 KQKAQVEDELAKVRIQMDELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMkslAEEAARlsveaEETARQRQIAEsn 2339
Cdd:TIGR02794 54 RIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ---AEQAAK-----QAEEKQKQAEE-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2340 lAEQRALAEKmlkekmqaiqeatKLKAEAQELQKQKDQAQEKA------KKLLEDKQQIQQRLDKETEGFQKSLEAERKR 2413
Cdd:TIGR02794 124 -AKAKQAAEA-------------KAKAEAEAERKAKEEAAKQAeeeakaKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 736215636 2414 QLEvSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKA 2454
Cdd:TIGR02794 190 KAE-EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKA 229
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3975-4012 |
1.68e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.68e-05
10 20 30
....*....|....*....|....*....|....*...
gi 736215636 3975 KKYLEGTSCIAGVYVESSKDRLSIYQAMKKNMIRPGTA 4012
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2003-2216 |
1.70e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 50.61 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2003 AEETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEK 2082
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2083 QVIVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAkekaekeaallRQKAAEAEKQKKSAEE 2162
Cdd:TIGR02794 133 KAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEA-----------EAKAKAEEAKAKAEAA 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 736215636 2163 EAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQA 2216
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGA 255
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2099-2314 |
1.77e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.37 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2099 QKAQEVLSKNKED------SLAQQKMKEEFENAKrlaqaaekakekaekeaalLRQKAAEAEKQKKSAEEEAAKQaKAQK 2172
Cdd:PRK00409 505 EEAKKLIGEDKEKlneliaSLEELERELEQKAEE-------------------AEALLKEAEKLKEELEEKKEKL-QEEE 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2173 DaeKLKKAAEEEAskraaaeAEALKQKKQADAEMAKHKKEaDQALKLKSQVEKELTMVKLRLDET--DKQKALLDEELQR 2250
Cdd:PRK00409 565 D--KLLEEAEKEA-------QQAIKEAKKEADEIIKELRQ-LQKGGYASVKAHELIEARKRLNKAneKKEKKKKKQKEKQ 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736215636 2251 VKGEVNDAVK-----QKAQV-----EDElakVRIQMDeLLKLKLKIEEQNRSlmKKDKDKTQKVLAEEAGKMKS 2314
Cdd:PRK00409 635 EELKVGDEVKylslgQKGEVlsipdDKE---AIVQAG-IMKMKVPLSDLEKI--QKPKKKKKKKPKTVKPKPRT 702
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
57-164 |
1.81e-05 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 47.73 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 57 QKKTFTKWVNK---------HLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 123
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 736215636 124 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 164
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1798-2333 |
1.92e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1798 RKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEaaRQRA 1877
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREE--LEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1878 EAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEdeayQRKLLEDQAAQHKHDIQEKIIHLKSSSDSEMVRQ 1957
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1958 KTIVEETLRQKKIVEEEIhiirinfEKASKGKSDLENELKKLkviaeetqKSKLKAEAEAEKLKKLAAeeekkrkeseek 2037
Cdd:COG4717 198 AEELEELQQRLAELEEEL-------EEAQEELEELEEELEQL--------ENELEAAALEERLKEARL------------ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2038 VKRITAAEEEAARQCKAAQEEVARLEKKAdeankqkekaEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQK 2117
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGVL----------FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2118 MKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEklKKAAEEEASKRAAAEAEALK 2197
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE--AGVEDEEELRAALEQAEEYQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2198 QKKQadaemakhkkeadQALKLKSQVEKELTMVKLRLDETDKQKalLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMD 2277
Cdd:COG4717 399 ELKE-------------ELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELEELREELAELEAELE 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 2278 ELlklklkieEQNRSLMKKDKDktqkvLAEEAGKMKSLAEEAARLSVEAE--ETARQR 2333
Cdd:COG4717 464 QL--------EEDGELAELLQE-----LEELKAELRELAEEWAALKLALEllEEAREE 508
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1497-1807 |
2.09e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1497 KIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAA 1576
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1577 KQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQSHSMSFNVKASKLEESLKKeqgtVLQLQE 1656
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA----LDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1657 EAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKD 1736
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736215636 1737 NAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAK 1807
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2357-2601 |
2.24e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2357 AIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKetegFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQS 2436
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2437 KAEneaKKFKKQADEAKARLKDTEKQSTETVVQKLETQR--LQSTREADGLKEAIAdlekerekLKKEAEELQNKSNKMA 2514
Cdd:COG4942 94 ELR---AELEAQKEELAELLRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAP--------ARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2515 NTQKEEIEQQKAIIQKsfiserelLLKRQKAVEDEKKKLQKQFEDEVKKAEALKDEQERQRKLMEEEKKKLQAIMDAAVK 2594
Cdd:COG4942 163 AALRAELEAERAELEA--------LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
....*..
gi 736215636 2595 KQKEAEA 2601
Cdd:COG4942 235 EAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1271-1746 |
2.32e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1271 LGEARKRQEKIQAVPIGGSKALREQLAEEKKLLEEIEKNKDKIDSCQKNAKAYIDSVKDYELQILTYKALQDPMAsplkk 1350
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP----- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1351 pkmdcasdnIIQEYVTLRTRYSELMTLtsqyIKFITETQRRLEDDEKASEKLKEEERKKMAEIQAELDKQKQIAEAQAKS 1430
Cdd:COG4717 130 ---------LYQELEALEAELAELPER----LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1431 VIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQHELHHLKslSEQEIKSKSQQL------------EHALVSHTKI 1498
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA--LEERLKEARLLLliaaallallglGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1499 EEEIHTIRIQL-----EMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEK 1573
Cdd:COG4717 275 IAGVLFLVLGLlallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1574 EAAKQKQKAldDLQKFKMQAEEAERRMKQAEEEKLRQIkvveeVAQKSAATQLQShsmsfnvKASKLEESLKKEQGTVLQ 1653
Cdd:COG4717 355 EAEELEEEL--QLEELEQEIAALLAEAGVEDEEELRAA-----LEQAEEYQELKE-------ELEELEEQLEELLGELEE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1654 LQE--EAEQLRKQQEEANKAREQAEKELETWRQKANEaLRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAeDAA 1731
Cdd:COG4717 421 LLEalDEEELEEELEELEEELEELEEELEELREELAE-LEAELEQLEEDGELAELLQELEELKAELRELAEEWAAL-KLA 498
|
490
....*....|....*
gi 736215636 1732 LKQKDNAEKELEKQR 1746
Cdd:COG4717 499 LELLEEAREEYREER 513
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1652-1813 |
2.40e-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: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1652 LQLQE---EAEQLRKQQEEANKAREQAEKELETWRQKAnEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAE 1728
Cdd:COG1579 10 LDLQEldsELDRLEHRLKELPAELAELEDELAALEARL-EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1729 ---DAALKQKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQrglLDNELQRLKKEVSATEKQRKLLEEEL 1805
Cdd:COG1579 89 keyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE---LEEKKAELDEELAELEAELEELEAER 165
|
....*...
gi 736215636 1806 AKVRSEMD 1813
Cdd:COG1579 166 EELAAKIP 173
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1497-1588 |
2.56e-05 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 46.66 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1497 KIEEEIHTIRIQLEMTIKQKKTAESELQQLRdkaAEAEKLRKAAQEDAERLRKQVAEETQKKKNaedelKRKSEAEKEAA 1576
Cdd:cd06503 34 KIAESLEEAEKAKEEAEELLAEYEEKLAEAR---AEAQEIIEEARKEAEKIKEEILAEAKEEAE-----RILEQAKAEIE 105
|
90
....*....|..
gi 736215636 1577 KQKQKALDDLQK 1588
Cdd:cd06503 106 QEKEKALAELRK 117
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3145-3181 |
2.70e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.70e-05
10 20 30
....*....|....*....|....*....|....*..
gi 736215636 3145 RLLSAERAVSGYKDPYTGKKVSLFEAMNKGLIKKDHG 3181
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2358-2571 |
2.73e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2358 IQEATKLKAEAQELQKQkdQAQEKAKKLLEDKQQIQQRLdketegfqKSLEAERKRQLEVSAEAETLRLKVKElsdAQSK 2437
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKK--KEQQQAEELQQKQAAEQERL--------KQLEKERLAAQEQKKQAEEAAKQAAL---KQKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2438 AENEAKKfkkQADEAKARLKDTEKQSTETVVQKLETQRLQSTREADGLKEAIADLEKEREKLKKEAEELQNKSNKMANTQ 2517
Cdd:PRK09510 134 AEEAAAK---AAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 736215636 2518 KEEIEQQKAiiqksfisERELLLKRQKAVEDEKKKLQKQFEDEVKKAEALKDEQ 2571
Cdd:PRK09510 211 AAAEAKKKA--------AAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1520-1759 |
2.77e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 49.98 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1520 ESELQQLRDKAAeaeklRKAAQEDAERL-RKQVAEETQKKKNAEdelkrkseaEKEAAKQKQKAlddlqkfkMQAEEAER 1598
Cdd:PRK07735 4 EKDLEDLKKEAA-----RRAKEEARKRLvAKHGAEISKLEEENR---------EKEKALPKNDD--------MTIEEAKR 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1599 RmkQAEEEKlrqIKVVEEVAQKSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKe 1678
Cdd:PRK07735 62 R--AAAAAK---AKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAA- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1679 letwRQKANEALRLRLQAEEEAqkkskTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLS 1758
Cdd:PRK07735 136 ----KAKAAALAKQKREGTEEV-----TEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAK 206
|
.
gi 736215636 1759 A 1759
Cdd:PRK07735 207 A 207
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1520-1656 |
2.79e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1520 ESELQQLRDKAAEAEKLRKaaqeDAERLRKQVAEETQKKKNAEDELkrKSEAEKEAakqkQKALDDLQKfkmQAEEAERR 1599
Cdd:PRK00409 526 EELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEEEDKL--LEEAEKEA----QQAIKEAKK---EADEIIKE 592
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 1600 MKQAEEEKLRQIKvveevaqksaATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQE 1656
Cdd:PRK00409 593 LRQLQKGGYASVK----------AHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2045-2352 |
2.81e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 50.25 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2045 EEEAARQC-KAAQEEVARL---EKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSKNKEDSlaQQKMKE 2120
Cdd:pfam02029 4 EEEAARERrRRAREERRRQkeeEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERR--QKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2121 EFENAKRL---AQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAA--------KQAKAQKDAEKLKKAAEEEA-SKR 2188
Cdd:pfam02029 82 ALERQKEFdptIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKeeeteireKEYQENKWSTEVRQAEEEGEeEED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2189 AAAEAEALKQKKQADAEMAKHKKEADQALKLKSQV----EKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQ--K 2262
Cdd:pfam02029 162 KSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVfldqKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEeaE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2263 AQVEDELAKVRIQM-------DELLKLKLKIEEQNRSL--MKKDKDKTQKVLAEEAGKMKslAEEAARLSVEAEETARQR 2333
Cdd:pfam02029 242 VFLEAEQKLEELRRrrqekesEEFEKLRQKQQEAELELeeLKKKREERRKLLEEEEQRRK--QEEAERKLREEEEKRRMK 319
|
330
....*....|....*....
gi 736215636 2334 QIAESNLAEQralAEKMLK 2352
Cdd:pfam02029 320 EEIERRRAEA---AEKRQK 335
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2147-2632 |
2.91e-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: 50.61 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2147 RQKAAEA---EKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKR---AAAEAEALKQKKQADAEMAKHKKEADQALKLK 2220
Cdd:pfam12128 408 RQLAVAEddlQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRlnqATATPELLLQLENFDERIERAREEQEAANAEV 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2221 SQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAV---------------KQKAQVEDELAKV-------RIQMDE 2278
Cdd:pfam12128 488 ERLQSELRQARKRRDQASEALRQASRRLEERQSALDELElqlfpqagtllhflrKEAPDWEQSIGKVispellhRTDLDP 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2279 L--------------LKLKLKIEEQNRSL-----MKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAESN 2339
Cdd:pfam12128 568 EvwdgsvggelnlygVKLDLKRIDVPEWAaseeeLRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2340 LAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETegfqkSLEAERKRQLEVSA 2419
Cdd:pfam12128 648 LKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQ-----KREARTEKQAYWQV 722
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2420 EAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTeKQSTETVVQKLETQRLQSTREAdglkEAIADLEKEREKL 2499
Cdd:pfam12128 723 VEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLAS-LGVDPDVIAKLKREIRTLERKI----ERIAVRRQEVLRY 797
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2500 KKEAEELQNKSNKMANTQKEEIEQQkaiiqksfISERELLLKRQKAvedEKKKLQKQFEDEVKKAEALKDEQERQRKLME 2579
Cdd:pfam12128 798 FDWYQETWLQRRPRLATQLSNIERA--------ISELQQQLARLIA---DTKLRRAKLEMERKASEKQQVRLSENLRGLR 866
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 736215636 2580 EEKKKLQAIMDAAVKKQKEAEADMKNKQtemevLEKKRLDQEKQLGAENQKLR 2632
Cdd:pfam12128 867 CEMSKLATLKEDANSEQAQGSIGERLAQ-----LEDLKLKRDYLSESVKKYVE 914
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1656-1760 |
2.93e-05 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 47.09 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1656 EEAEQLRkqqEEANKAREQAEKELETWRQKANEalrLRLQAEEEAqkksktQEEAERQKVEAERDAKKR-AKAEDAALKQ 1734
Cdd:COG0711 41 AEAERAK---EEAEAALAEYEEKLAEARAEAAE---IIAEARKEA------EAIAEEAKAEAEAEAERIiAQAEAEIEQE 108
|
90 100 110
....*....|....*....|....*....|.
gi 736215636 1735 KDNAEKELEKQ-----RTFAEQVAQQKLSAE 1760
Cdd:COG0711 109 RAKALAELRAEvadlaVAIAEKILGKELDAA 139
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1508-1737 |
2.98e-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: 50.60 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1508 QLEMTIKQKKTAESELQQLRDKA-AEAEKlRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDL 1586
Cdd:NF012221 1543 QADAVSKHAKQDDAAQNALADKErAEADR-QRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAILEESRAVTKE 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1587 QKFKMQAEEAERRMKQAEEEK------------LRQIKVVEEVAQKSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQl 1654
Cdd:NF012221 1622 LTTLAQGLDALDSQATYAGESgdqwrnpfagglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQ- 1700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1655 qeeAEQLRKQQEEA-NKAREQAEKeletwRQKanEALRLRLQAEEEAQKKSKTQEEAER---QKVEAERDAKKRAKAEDA 1730
Cdd:NF012221 1701 ---GEQNQANAEQDiDDAKADAEK-----RKD--DALAKQNEAQQAESDANAAANDAQSrgeQDASAAENKANQAQADAK 1770
|
....*..
gi 736215636 1731 ALKQKDN 1737
Cdd:NF012221 1771 GAKQDES 1777
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1774-1907 |
3.14e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 50.40 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1774 EQQ-RGLLdnELQRLKKEVSATEKQRKLLEEEL--AKVRSEMDSllkmKTEAEKKTMSNtekskqLLESEA-LKMKQLAD 1849
Cdd:PTZ00491 676 EQEaRGRL--ERQKMHDKAKAEEQRTKLLELQAesAAVESSGQS----RAEALAEAEAR------LIEAEAeVEQAELRA 743
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736215636 1850 EATRLRSVAE-EAKKQRQTAEEEAARQRAEAEkILKEKLAAINEATRLR---------TEAEIA-----LKAK 1907
Cdd:PTZ00491 744 KALRIEAEAElEKLRKRQELELEYEQAQNELE-IAKAKELADIEATKFErivealgreTLIAIAragpeLQAK 815
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2234-2462 |
3.22e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2234 LDETDkqkalLDEELQRVKGEVNDAVKQKAQVEDELAKVRIqMDELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMK 2313
Cdd:COG4913 218 LEEPD-----TFEAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2314 SLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKmLKEKMQAIQEATKlkaeaQELQKQKDQAQEKAKKLLEDKQQIQ 2393
Cdd:COG4913 292 LLEAELEELRAELARLEAELERLEARLDALREELDE-LEAQIRGNGGDRL-----EQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 2394 QRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQ 2462
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1389-1586 |
3.61e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.42 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1389 QRRLEDDEKASEKLKEEERKKMAEIQAELDKQKQIAEAQAKsvikaeqEAQELKLKMKEEASKRQDVAVDAEQQKQNiqh 1468
Cdd:PRK09510 100 QERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAK-------AAAAAKAKAEAEAKRAAAAAKKAAAEAKK--- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1469 elhhlKSLSEQEIKSKSQQLEHAlvshtkieeeihtiriQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLR 1548
Cdd:PRK09510 170 -----KAEAEAAKKAAAEAKKKA----------------EAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAA 228
|
170 180 190
....*....|....*....|....*....|....*...
gi 736215636 1549 KQVAEetqkKKNAEDELKRKSEAEKEAAKQKQKALDDL 1586
Cdd:PRK09510 229 KAAAE----AKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2235-2470 |
3.81e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2235 DETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQNRSLMKKDKDKTQKV------LAEE 2308
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVkelkeeRDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2309 AGKMKSLAEEAARLSVEAEETAR--------QRQIA---------------ESNLAEQRALAEKMLKEKMQAIQEATKLK 2365
Cdd:COG1340 84 NEKLNELREELDELRKELAELNKaggsidklRKEIErlewrqqtevlspeeEKELVEKIKELEKELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2366 AEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKsLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKF 2445
Cdd:COG1340 164 ELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE-ADELRKEADELHKEIVEAQEKADELHEEIIELQKELREL 242
|
250 260
....*....|....*....|....*
gi 736215636 2446 KKQADEAKARLKDTEKQSTETVVQK 2470
Cdd:COG1340 243 RKELKKLRKKQRALKREKEKEELEE 267
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2230-2478 |
4.03e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2230 VKLRLDETDKQKALLDEELQRVKGEVNDAvkqkaqvEDELAKVRiqmdellklklkieEQNRSLMkkdkdktqkvLAEEA 2309
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEA-------EAALEEFR--------------QKNGLVD----------LSEEA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2310 gkmKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEAT--KLKAEAQELQKQKDQAQEK------ 2381
Cdd:COG3206 215 ---KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAELSARytpnhp 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2382 -AKKLLEDKQQIQQRLDKETEGFQKSLEAERkrqlevsaeaETLRLKVKELSDAQSKAENEAKKFKKQADEAKA--RLKD 2458
Cdd:COG3206 292 dVIALRAQIAALRAQLQQEAQRILASLEAEL----------EALQAREASLQAQLAQLEARLAELPELEAELRRleREVE 361
|
250 260
....*....|....*....|
gi 736215636 2459 TEKQSTETVVQKLETQRLQS 2478
Cdd:COG3206 362 VARELYESLLQRLEEARLAE 381
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1477-1711 |
4.07e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1477 SEQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAE--- 1553
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1554 ETQKKKNAEDELK------------RKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEvaQKS 1621
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA--AKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1622 AATQLQShsmsfnvKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQ 1701
Cdd:COG3883 172 ELEAQQA-------EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
250
....*....|
gi 736215636 1702 KKSKTQEEAE 1711
Cdd:COG3883 245 SAAGAGAAGA 254
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2159-2394 |
4.21e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2159 SAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKELtmvklrldetD 2238
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----------E 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2239 KQKALLDE---ELQRVKGEVN--DAVKQKAQVEDELAKVriqmdELLKlklKIEEQNRSLMKKDKDKTQKVLAEEAgkmk 2313
Cdd:COG3883 83 ERREELGErarALYRSGGSVSylDVLLGSESFSDFLDRL-----SALS---KIADADADLLEELKADKAELEAKKA---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2314 SLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQ 2393
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
.
gi 736215636 2394 Q 2394
Cdd:COG3883 231 A 231
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2098-2563 |
4.69e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2098 EQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKL 2177
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2178 KKAAE------------EEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKS-QVEKELTMVKLRLDETDKQKALL 2244
Cdd:COG4717 132 QELEAleaelaelperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2245 DEELQRVKGEVNDAVKQKAQVEDELakvriqmdELLKLKLKIEEQNRSLM-----------KKDKDKTQKVLAEEAGKMK 2313
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENEL--------EAAALEERLKEARLLLLiaaallallglGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2314 SLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQ-EATKLKAEAQELQKQKDQAQEKAKKLLEDKQQI 2392
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2393 QQrldketegfqKSLEAERKRQLEV--SAEAETLRLKVKELSDAQsKAENEAKKFKKQ-ADEAKARLKDTEKQSTETVVQ 2469
Cdd:COG4717 364 QL----------EELEQEIAALLAEagVEDEEELRAALEQAEEYQ-ELKEELEELEEQlEELLGELEELLEALDEEELEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2470 KLETqrlqstreadgLKEAIADLEKEREKLKKEAEELQNKSNKMANTQK-EEIEQQKAIIQksfiSERELLLKR------ 2542
Cdd:COG4717 433 ELEE-----------LEEELEELEEELEELREELAELEAELEQLEEDGElAELLQELEELK----AELRELAEEwaalkl 497
|
490 500
....*....|....*....|..
gi 736215636 2543 -QKAVEDEKKKLQKQFEDEVKK 2563
Cdd:COG4717 498 aLELLEEAREEYREERLPPVLE 519
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2160-2331 |
4.83e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2160 AEEEAAKQAK-AQKDAEKLKKAAEEEASKraaaeaEALKQKKQADAEMAKHKKEADQalkLKSQVEKELTMVKLRLDETD 2238
Cdd:PRK12704 36 AEEEAKRILEeAKKEAEAIKKEALLEAKE------EIHKLRNEFEKELRERRNELQK---LEKRLLQKEENLDRKLELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2239 KQKALLDEELQRVKGEVNDAVKQKAQVEDELAKvriQMDELLKL-KLKIEEQNRSLMKKDKDKTQkvlaEEAGKMKSLAE 2317
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEE---QLQELERIsGLTAEEAKEILLEKVEEEAR----HEAAVLIKEIE 179
|
170
....*....|....
gi 736215636 2318 EAARLsvEAEETAR 2331
Cdd:PRK12704 180 EEAKE--EADKKAK 191
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1538-1760 |
4.95e-05 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 49.77 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1538 KAAQEDAE---RLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKAlddlqkFKMQAEEAERRMKQ-AEEEKLRQIKv 1613
Cdd:pfam18971 613 KKAQKDLEkslRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDEI------FALINKEANRDARAiAYTQNLKGIK- 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1614 vEEVAQK--SAATQLQSHSMSF-------NVKASKLEESLKKEQGTVLQLQEEAEQLRKqQEEANKAreqaekeLETWRQ 1684
Cdd:pfam18971 686 -RELSDKleKISKDLKDFSKSFdefkngkNKDFSKAEETLKALKGSVKDLGINPEWISK-VENLNAA-------LNEFKN 756
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 1685 KANEALRLRLQAEEEAQKKSKtqEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFA-EQVAQQKLSAE 1760
Cdd:pfam18971 757 GKNKDFSKVTQAKSDLENSVK--DVIINQKVTDKVDNLNQAVSVAKAMGDFSRVEQVLADLKNFSkEQLAQQAQKNE 831
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1432-1885 |
5.11e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.57 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1432 IKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQHELHhLKSLSEQEIKSKsQQLEHALVSHTKIEEEIHTIrIQLEM 1511
Cdd:COG5185 177 KKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLG-SESTLLEKAKEI-INIEEALKGFQDPESELEDL-AQTSD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1512 TIKQKKTAESELQQlrDKAAEAEKLRKAAQEDAERLRKQVaeETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFkm 1591
Cdd:COG5185 254 KLEKLVEQNTDLRL--EKLGENAESSKRLNENANNLIKQF--ENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQEL-- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1592 qaeeaERRMKQAEEEKLRQIkvvEEVAQKSAatqlqshSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKA 1671
Cdd:COG5185 328 -----EESKRETETGIQNLT---AEIEQGQE-------SLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKES 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1672 REQAEKELETWRQKANEALrlrlqaeeeaqkkSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQ 1751
Cdd:COG5185 393 LDEIPQNQRGYAQEILATL-------------EDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1752 VAQQKLSAEQECI--RLKADFDHAEQQRGLLDNELQRLKKEVsatEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSN 1829
Cdd:COG5185 460 ESQSRLEEAYDEInrSVRSKKEDLNEELTQIESRVSTLKATL---EKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYA 536
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 736215636 1830 TEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKE 1885
Cdd:COG5185 537 HILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTIESQQAREDPIPD 592
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4325-4358 |
5.75e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 5.75e-05
10 20 30
....*....|....*....|....*....|....
gi 736215636 4325 EETGPVAGILDTETLEKVSITEAIHRNLVDNITG 4358
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2332-2531 |
5.85e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2332 QRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAER 2411
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2412 KRQ-----LEVSAEAETL------RLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTE------KQSTETVVQKLETQ 2474
Cdd:COG3883 97 RSGgsvsyLDVLLGSESFsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLaelealKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 2475 RLQSTREADGLKEAIADLEKEREKLKKEAEELQNKSNKMANTQKEEIEQQKAIIQKS 2531
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1411-1743 |
6.63e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 49.47 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1411 AEIQAELDK-QKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNiqhelhhLKSLSEQEIKSKSQqlE 1489
Cdd:PLN03229 432 RELEGEVEKlKEQILKAKESSSKPSELALNEMIEKLKKEIDLEYTEAVIAMGLQER-------LENLREEFSKANSQ--D 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1490 HALvsHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLrDKAAEAEKlRKAAQEDAERLRKQVAEETQKKKNAED--ELKR 1567
Cdd:PLN03229 503 QLM--HPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKL-DMLNEFSR-AKALSEKKSKAEKLKAEINKKFKEVMDrpEIKE 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1568 KSEAEK-EAAKQKQKALDDLQkfKMQAEEAERRMKQAEEEKLRQIKV----VEEVAQKSAATQLQSHSMSFNVKASKLEE 1642
Cdd:PLN03229 579 KMEALKaEVASSGASSGDELD--DDLKEKVEKMKKEIELELAGVLKSmgleVIGVTKKNKDTAEQTPPPNLQEKIESLNE 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1643 SLKKEQGTVLQ---LQEEAEQLRKQQEEANKAREQAEKE-LETWRQKANEALRLRLQAEEEAQKKSKTQEE-AERQKVEA 1717
Cdd:PLN03229 657 EINKKIERVIRssdLKSKIELLKLEVAKASKTPDVTEKEkIEALEQQIKQKIAEALNSSELKEKFEELEAElAAARETAA 736
|
330 340
....*....|....*....|....*.
gi 736215636 1718 ERDAkkRAKAEDAALKQKDNAEKELE 1743
Cdd:PLN03229 737 ESNG--SLKNDDDKEEDSKEDGSRVE 760
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1999-2199 |
7.19e-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: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1999 LKVIAEETQKSKlKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAek 2078
Cdd:COG2268 191 RRKIAEIIRDAR-IAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAA-- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2079 eaekqVIVAKEAAQKcssAEQKAQEVLSKNKEDSLAQQkmkeefENAKRLAQAAEKakekaekeaallRQKAAEAEKQKK 2158
Cdd:COG2268 268 -----YEIAEANAER---EVQRQLEIAEREREIELQEK------EAEREEAELEAD------------VRKPAEAEKQAA 321
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 736215636 2159 SAEEEA---AKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQK 2199
Cdd:COG2268 322 EAEAEAeaeAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEK 365
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1782-1958 |
7.58e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.30 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1782 NELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKtEAEKKTMSNTEKSKQLLESEA--LKMKQLADEATRLRSVAE 1859
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK-QAEQAAKQAEEKQKQAEEAKAkqAAEAKAKAEAEAERKAKE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1860 EAKKQRQT-----AEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQ 1934
Cdd:TIGR02794 147 EAAKQAEEeakakAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAE 226
|
170 180
....*....|....*....|....
gi 736215636 1935 HKHDIQEKIIHLKSSSDSEMVRQK 1958
Cdd:TIGR02794 227 RKADEAELGDIFGLASGSNAEKQG 250
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2288-2536 |
8.38e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2288 EQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRalaekmlkekmqaiQEATKLKAE 2367
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE--------------AELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2368 AQELQKQKDQAQEKAKKLLeDKQQIQQRLDKETEGF--QKSLEAERKRQL------EVSAEAETLRLKVKELSDAQSKAE 2439
Cdd:COG4942 92 IAELRAELEAQKEELAELL-RALYRLGRQPPLALLLspEDFLDAVRRLQYlkylapARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2440 NEAKKFKKQADEAKARLK--DTEKQSTETVVQKLETQRLQSTREADGLKEAiadlekereklkkeAEELQNKSNKMantQ 2517
Cdd:COG4942 171 AERAELEALLAELEEERAalEALKAERQKLLARLEKELAELAAELAELQQE--------------AEELEALIARL---E 233
|
250
....*....|....*....
gi 736215636 2518 KEEIEQQKAIIQKSFISER 2536
Cdd:COG4942 234 AEAAAAAERTPAAGFAALK 252
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1511-1939 |
8.76e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.03 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1511 MTIKQKKTAESELQQLRDKAAEAEKLRKAAQE----------DAERL---RKQVAEETQKKKNAEDELKRKSEAEKEAAK 1577
Cdd:PRK10246 188 MVFEQHKSARTELEKLQAQASGVALLTPEQVQsltaslqvltDEEKQlltAQQQQQQSLNWLTRLDELQQEASRRQQALQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1578 QKQKALDDLQK--FKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKS--AATQLQShsmSFNVKASKLEESLKKEQgtvlQ 1653
Cdd:PRK10246 268 QALAAEEKAQPqlAALSLAQPARQLRPHWERIQEQSAALAHTRQQIeeVNTRLQS---TMALRARIRHHAAKQSA----E 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1654 LQEEAEQLRKQQEEANKAReQAEKELETWRqkaneALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALK 1733
Cdd:PRK10246 341 LQAQQQSLNTWLAEHDRFR-QWNNELAGWR-----AQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAA 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1734 QKDNAEKELEKQR--TFAEQVA--QQKLSAEQECI-RLKADFDHAEQQrglLDNELQRLK---------KEVSATEKQRK 1799
Cdd:PRK10246 415 LAQHAEQRPLRQRlvALHGQIVpqQKRLAQLQVAIqNVTQEQTQRNAA---LNEMRQRYKektqqladvKTICEQEARIK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1800 LLEEELAKVRSEMDSLLKMKTEA------EKKTMSNTEKSKQLLESEalkMKQLADEATRLRSVAEEAKKQRQTAEEEAA 1873
Cdd:PRK10246 492 DLEAQRAQLQAGQPCPLCGSTSHpaveayQALEPGVNQSRLDALEKE---VKKLGEEGAALRGQLDALTKQLQRDESEAQ 568
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 1874 RQRAEAEKILKE---KLAAINEATRLRTEAEIALKAKEAENERLkrkaeDEAYQRKLLEDQAAQHKHDI 1939
Cdd:PRK10246 569 SLRQEEQALTQQwqaVCASLNITLQPQDDIQPWLDAQEEHERQL-----RLLSQRHELQGQIAAHNQQI 632
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2151-2361 |
8.91e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 48.33 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2151 AEAEKQKKSAEEEAA-KQAKAQKDAE--KLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKEL 2227
Cdd:COG2268 199 RDARIAEAEAERETEiAIAQANREAEeaELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAERE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2228 TMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEdelakvriqmdellklklkieeqnrslmkkdkdkTQKVLAE 2307
Cdd:COG2268 279 VQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAE----------------------------------KQAAEAE 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 736215636 2308 EAGKMKSLAEEAARlsvEAEetARQRQIAESNLAEQRALAEKMLkEKMQAIQEA 2361
Cdd:COG2268 325 AEAEAEAIRAKGLA---EAE--GKRALAEAWNKLGDAAILLMLI-EKLPEIAEA 372
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
57-165 |
9.09e-05 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 45.82 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 57 QKKTFTKWVNK---------HLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 123
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 736215636 124 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVN 165
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2173-2484 |
9.58e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 48.44 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2173 DAEKLKKAAEEEASKRAAAEAEALKQKKQAdAEMAKHKKEADQALK-LKSQVEKELTMVKLRLDETDKQKAlldEELQRV 2251
Cdd:PRK07735 2 DPEKDLEDLKKEAARRAKEEARKRLVAKHG-AEISKLEEENREKEKaLPKNDDMTIEEAKRRAAAAAKAKA---AALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2252 KGEVNDAVkqkaqVEDELAKVRIQMDELLKLKLKieeqnrSLMKKDKDKTQKVLAEEAGKMKSLAEEAARlsVEAEETAR 2331
Cdd:PRK07735 78 KREGTEEV-----TEEEKAKAKAKAAAAAKAKAA------ALAKQKREGTEEVTEEEKAAAKAKAAAAAK--AKAAALAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2332 QRQIAESNLAEQRALAEKMLKEKmqaiQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAER 2411
Cdd:PRK07735 145 QKREGTEEVTEEEEETDKEKAKA----KAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAK 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736215636 2412 KRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKarlKDTEKQSTETVVQKLETQRLQSTREADG 2484
Cdd:PRK07735 221 QKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAKTKGAEGKK---EEEPKQEEPSVNQPYLNKYVEVIKEKLG 290
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1515-1620 |
9.77e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1515 QKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRkqvAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKM--- 1591
Cdd:PRK00409 528 LERELEQKAEEAEALLKEAEKLKEELEEKKEKLQ---EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYasv 604
|
90 100 110
....*....|....*....|....*....|..
gi 736215636 1592 ---QAEEAERRMKQAEEEKLRQIKVVEEVAQK 1620
Cdd:PRK00409 605 kahELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1318-1594 |
9.80e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.92 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1318 KNAKAYIDSVKDYELQILTYKALQDpmaspLKKPKMDCASDNIIQEYV---TLRTRYSELmtltsQYIKFITETQRRLED 1394
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRE-----TEEVEFSLKAEVLIQKFGrslKAKKRFSLL-----KKETIYLQSAQRVEL 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1395 DEKASEKLKEEERkkmaEIQAELDKQKQIaEAQAKSVIKAEQEAQELKLKMKEEASKRqdvavdAEQQKQNIQHELHHLK 1474
Cdd:COG5022 880 AERQLQELKIDVK----SISSLKLVNLEL-ESEIIELKKSLSSDLIENLEFKTELIAR------LKKLLNNIDLEEGPSI 948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1475 SLSEQEIKSKSQQLEHALvshTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLrKQVAEE 1554
Cdd:COG5022 949 EYVKLPELNKLHEVESKL---KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQL-KELPVE 1024
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 736215636 1555 TQKKKNAEDELKRKSEAEKEAAK-QKQKALDDLQKFKMQAE 1594
Cdd:COG5022 1025 VAELQSASKIISSESTELSILKPlQKLKGLLLLENNQLQAR 1065
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2294-2603 |
9.89e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.33 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2294 MKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEaTKLKAEAQELQK 2373
Cdd:pfam02029 68 TAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETE-IREKEYQENKWS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2374 QKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAE-TLRLKVKELSDAQSKAENEAKKFKKQADEA 2452
Cdd:pfam02029 147 TEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKvFLDQKRGHPEVKSQNGEEEVTKLKVTTKRR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2453 KARLKDTEKQSTETVVQKLETQRLQSTREADGLKEaiadlekereklkkeaeelqnksnkmantqKEEIEQQKAIIQKSF 2532
Cdd:pfam02029 227 QGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKE------------------------------SEEFEKLRQKQQEAE 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736215636 2533 ISERELLLKRQ---KAVEDEKKKlQKQFEDEVKKAEalkdEQERQRKLMEEEKKKlqaiMDAAVKKQKEAEADM 2603
Cdd:pfam02029 277 LELEELKKKREerrKLLEEEEQR-RKQEEAERKLRE----EEEKRRMKEEIERRR----AEAAEKRQKLPEDSS 341
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2145-2416 |
1.02e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2145 LLRQKAAEAEKQKKSAEEEAaKQAKAQK-------DAEKlKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQAl 2217
Cdd:PRK04863 373 EADEQQEENEARAEAAEEEV-DELKSQLadyqqalDVQQ-TRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQA- 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2218 KLKSQVEkELTMVKLRLDETDKQKALLDEELQRVK---GEV--NDAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQNRS 2292
Cdd:PRK04863 450 KEQEATE-ELLSLEQKLSVAQAAHSQFEQAYQLVRkiaGEVsrSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQR 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2293 LMKKDKdkTQKVLAE---EAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQ 2369
Cdd:PRK04863 529 LRQQQR--AERLLAEfckRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWL 606
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 736215636 2370 ELQKQKDQAQEKAKKLLEDKQQ----IQQRLDKETE-GFQKSLEAERKRQLE 2416
Cdd:PRK04863 607 AAQDALARLREQSGEEFEDSQDvteyMQQLLERERElTVERDELAARKQALD 658
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2147-2458 |
1.07e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.33 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2147 RQKAAEAEKQKKSAEEEAAKqakAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKE 2226
Cdd:pfam02029 12 RRRAREERRRQKEEEEPSGQ---VTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2227 LTmvklrlDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVriqmdellklklKIEEQNRSLMKKDKDKTQKVLA 2306
Cdd:pfam02029 89 FD------PTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRY------------KEEETEIREKEYQENKWSTEVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2307 EEAGKMkslaEEAARLSVEAEETARQRQIAEsNLAEQRALAEKMLKEKMQAIQEATKL----KAEAQELQ---------- 2372
Cdd:pfam02029 151 QAEEEG----EEEEDKSEEAEEVPTENFAKE-EVKDEKIKKEKKVKYESKVFLDQKRGhpevKSQNGEEEvtklkvttkr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2373 -----KQKDQAQEKAKKLLEDKQQI----QQRLDKETEGFQKSleaeRKRQLEVSAEAETL------RLKVKELSDAQSK 2437
Cdd:pfam02029 226 rqgglSQSQEREEEAEVFLEAEQKLeelrRRRQEKESEEFEKL----RQKQQEAELELEELkkkreeRRKLLEEEEQRRK 301
|
330 340
....*....|....*....|.
gi 736215636 2438 AENEAKKFKKQadEAKARLKD 2458
Cdd:pfam02029 302 QEEAERKLREE--EEKRRMKE 320
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1653-1880 |
1.15e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1653 QLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAE---- 1728
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1729 ------DAALKQKDNAE----------------KELEKQRTFAEQVAQQKLSAEQEcirlKADfdhAEQQRGLLDNELQR 1786
Cdd:COG3883 100 gsvsylDVLLGSESFSDfldrlsalskiadadaDLLEELKADKAELEAKKAELEAK----LAE---LEALKAELEAAKAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1787 LKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQ 1866
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
250
....*....|....
gi 736215636 1867 TAEEEAARQRAEAE 1880
Cdd:COG3883 253 GAAGAAAGSAGAAG 266
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1071-1606 |
1.18e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1071 TAEQMKVQSELEGLKKDLNSITEQTEEVLASQQQissapmLRSELDVTLRKMDHVYGLSSIYLDKLKTIDVVIRNTKEAE 1150
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYE------LLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1151 AALKTYESRLLdvnkvpENEKEVEEQRSQLKSMRAEVEADQVIFDRLQDELRRAStinDKMTRIHSERDAEMEHYRQLVS 1230
Cdd:COG1196 333 EELEEELEELE------EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL---EELAEELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1231 SLLERWQVVFAQMDMRQRELDLLGRHMNSYNVSYEWLIHWLGEARKRQEKIQAVPIGGSKALREQLAEEKKLLEEIEKNK 1310
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1311 DKIDSCQKNAKAYIDSVKDYELQILTYKALQDpmaSPLKKPKMDCASDNIIQEYVTLRTRYSELMTLTSQYIKFITETQR 1390
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAALL---LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1391 RLEDDEKASEKLKEEERKKMAEIQAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQHEL 1470
Cdd:COG1196 561 AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1471 HHLKSLSEQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQ 1550
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 736215636 1551 VAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKfKMQAEEAERRMKQAEEE 1606
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE-PPDLEELERELERLERE 775
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2745-2781 |
1.24e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 41.93 E-value: 1.24e-04
10 20 30
....*....|....*....|....*....|....*...
gi 736215636 2745 LQGQSCVGGILTP-SKEKMSVYQALKENKITPNTATIL 2781
Cdd:pfam00681 2 LEAQAATGGIIDPvTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1732-1901 |
1.25e-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: 46.84 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1732 LKQKDNAEKELEKQRtfaEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRS- 1810
Cdd:COG1579 12 LQELDSELDRLEHRL---KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1811 -EMDSLLKMKTEAEKKtmsnteksKQLLESEALkmkQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAA 1889
Cdd:COG1579 89 kEYEALQKEIESLKRR--------ISDLEDEIL---ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|..
gi 736215636 1890 INEATRLRTEAE 1901
Cdd:COG1579 158 LEELEAEREELA 169
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1657-1877 |
1.28e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1657 EAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRakaeDAALKQKD 1736
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER----REELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1737 NAEKELEKQRTFAEQVAQQKlSAEQECIRLKADFDHAEQQRGLLDnELQRLKKEVsatEKQRKLLEEELAKVRSEMDSLL 1816
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSE-SFSDFLDRLSALSKIADADADLLE-ELKADKAEL---EAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736215636 1817 KMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRA 1877
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1654-1917 |
1.32e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1654 LQEEAEQLRKQQEEANKAREQAEKELETWRQKANEaLRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALK 1733
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDE-LNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1734 qkdnaeKELEKQRTFAEQVAQQKLSAEQecirLKADFDHAE--QQRGLLD--------NELQRLKKEVSATEKQRKLlEE 1803
Cdd:COG1340 92 ------EELDELRKELAELNKAGGSIDK----LRKEIERLEwrQQTEVLSpeeekelvEKIKELEKELEKAKKALEK-NE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1804 ELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLEsealKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRA------ 1877
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHE----EMIELYKEADELRKEADELHKEIVEAQEKADELHEeiielq 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 736215636 1878 ----EAEKILKEKLAAINEATRLRTEAEIALKAKEAEnERLKRK 1917
Cdd:COG1340 237 kelrELRKELKKLRKKQRALKREKEKEELEEKAEEIF-EKLKKG 279
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1393-1625 |
1.33e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1393 EDDEKASEKLKEEERKKMAEIQAELDK-QKQIAEAQAKsVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQhelh 1471
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDAlQAELEELNEE-YNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1472 hlKSLSEQEIKSKSQQLEHALVSHTKIEEEIHtiriQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQV 1551
Cdd:COG3883 90 --ERARALYRSGGSVSYLDVLLGSESFSDFLD----RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736215636 1552 AEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQ 1625
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
2088-2470 |
1.43e-04 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 48.14 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2088 KEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKaekeaallrqKAAEAEKQKKSAEEEAAKQ 2167
Cdd:pfam04747 52 KEAFASLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEA----------RRAEAEAKKRAAQEEEHKQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2168 AKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQAlklkSQVEKELTMVKLRLDET---------- 2237
Cdd:pfam04747 122 WKAEQERIQKEQEKKEADLKKLQAEKKKEKAVKAEKAEKAEKTKKASTP----APVEEEIVVKKVANDRSaapapepktp 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2238 DKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQmDELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAE 2317
Cdd:pfam04747 198 TNTPAEPAEQVQEITGKKNKKNKKKSESEATAAPASVE-QVVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2318 EAARLSVEAEETARQRQiAESNLAEQRALAEKMLKEKMQAIQEATK----------LKAEAQELQKQKDQAQEKAKKLLE 2387
Cdd:pfam04747 277 TPVEPVVETTPPASENQ-KKNKKDKKKSESEKVVEEPVQAEAPKSKkptaddnmdfLDFVTAKEEPKDEPAETPAAPVEE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2388 DKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTETV 2467
Cdd:pfam04747 356 VVENVVENVVEKSTTPPATENKKKNKKDKKKSESEKVTEQPVESAPAPPQVEQVVETTPPASENKKKNKKDKKKSESEKA 435
|
...
gi 736215636 2468 VQK 2470
Cdd:pfam04747 436 VEE 438
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1497-1744 |
1.46e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1497 KIEEEIHTIRIQLEMTIKQK---KTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKrksEAEK 1573
Cdd:PHA02562 154 KLVEDLLDISVLSEMDKLNKdkiRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELV---EEAK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1574 EAAKQKQKALDDLQKFKMQAEEAERRMKqaeeeKLRQikvveevaqksAATQLQSHSMSFNVKASKLEE---------SL 1644
Cdd:PHA02562 231 TIKAEIEELTDELLNLVMDIEDPSAALN-----KLNT-----------AAAKIKSKIEQFQKVIKMYEKggvcptctqQI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1645 KKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKR 1724
Cdd:PHA02562 295 SEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEF 374
|
250 260
....*....|....*....|....*...
gi 736215636 1725 A--KAEDAALKQ------KDNAEKELEK 1744
Cdd:PHA02562 375 VdnAEELAKLQDeldkivKTKSELVKEK 402
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2376-2727 |
1.47e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2376 DQAQEKAKKLLED-KQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRlKVKELSDAQSKAENEAKKFKKQADEAKA 2454
Cdd:PTZ00121 1090 DEATEEAFGKAEEaKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR-KAEEARKAEDAKRVEIARKAEDARKAEE 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2455 RLKDTEKQSTETVVQKLETQRLQSTREADGLKEAIAdlekereklkkeaeelqnkSNKMANTQKEEiEQQKAIIQKSFIS 2534
Cdd:PTZ00121 1169 ARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEA-------------------ARKAEEERKAE-EARKAEDAKKAEA 1228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2535 ERELLLKRQKAvEDEKKKLQKQFEDEVKKAEALKDEQ--ERQRKLMEEEKKKLQAIMDAAVKKQ----KEAEADMKNKQT 2608
Cdd:PTZ00121 1229 VKKAEEAKKDA-EEAKKAEEERNNEEIRKFEEARMAHfaRRQAAIKAEEARKADELKKAEEKKKadeaKKAEEKKKADEA 1307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2609 EMEVLEKKRLDQEKQLGAENQKLREKL-QCLEGASKQSATKQVASKTIEVQTDVVSEEQLVTMTKVGTTKTvfngsvEVD 2687
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAkKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK------KAD 1381
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 736215636 2688 GAKKVAEspfafdgirEKVPAERLHDIGVLTKKELDKLKK 2727
Cdd:PTZ00121 1382 AAKKKAE---------EKKKADEAKKKAEEDKKKADELKK 1412
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1477-1856 |
1.50e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1477 SEQEIKsksQQLEhALVSHTKIEEEIHTIRIQLEMT---IKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAE 1553
Cdd:PRK11281 37 TEADVQ---AQLD-ALNKQKLLEAEDKLVQQDLEQTlalLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1554 ETQK--KKNAEDELKRKSEAEKEAAKQKQKALDDL---------QKFKMQAE--EAERRMKQaeeekLRQIKVVEEVAQK 1620
Cdd:PRK11281 113 ETREtlSTLSLRQLESRLAQTLDQLQNAQNDLAEYnsqlvslqtQPERAQAAlyANSQRLQQ-----IRNLLKGGKVGGK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1621 ----SAATQLQSHSMSFNVKASKLEESLkkEQGTVLQlqeeaEQLRKQQEEANKAREQAEKELETWRQKANEAlrlRLQA 1696
Cdd:PRK11281 188 alrpSQRVLLQAEQALLNAQNDLQRKSL--EGNTQLQ-----DLLQKQRDYLTARIQRLEHQLQLLQEAINSK---RLTL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1697 EEEAQKKSKTQEEAERQK----VEAERDAKK-------RAKAEDAALKQK--------DNAekeLEKQRTFAEQVA---- 1753
Cdd:PRK11281 258 SEKTVQEAQSQDEAARIQanplVAQELEINLqlsqrllKATEKLNTLTQQnlrvknwlDRL---TQSERNIKEQISvlkg 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1754 -----------QQKLSAEQEC---------IRLKAdFDhAEQQRGLL-------DNELQRLKKEVSATEKqRKLLeeELA 1806
Cdd:PRK11281 335 slllsrilyqqQQALPSADLIegladriadLRLEQ-FE-INQQRDALfqpdayiDKLEAGHKSEVTDEVR-DALL--QLL 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 736215636 1807 KVRSEMDSLLkmkteaekktmsNTEKSKQLLESEALKM--KQLADEATRLRS 1856
Cdd:PRK11281 410 DERRELLDQL------------NKQLNNQLNLAINLQLnqQQLLSVSDSLQS 449
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4435-4472 |
1.52e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.52e-04
10 20 30
....*....|....*....|....*....|....*...
gi 736215636 4435 QRFLEVQYLTGGLIEPDATSRVSIDEAVKKGSLDARTA 4472
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1782-1926 |
1.54e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.56 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1782 NELQRlKKEVSATEKQRkllEEELAKVRSEMDSLLKMKTEAEKktmsNTEKSKQLLESEALKMKQLADEATRLRSvaEEA 1861
Cdd:COG2268 206 AEAER-ETEIAIAQANR---EAEEAELEQEREIETARIAEAEA----ELAKKKAEERREAETARAEAEAAYEIAE--ANA 275
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736215636 1862 KKQRQTAEEEAARQR------AEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRK 1926
Cdd:COG2268 276 EREVQRQLEIAEREReielqeKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRAL 346
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1153-1771 |
1.64e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1153 LKTYESRLLDVNKVPENEKEVEEQRSQLKSMRAEVEADQVIFDRLQDELRRASTINDKMTRIHSERDAEMEHYRQLVSSL 1232
Cdd:TIGR01612 1148 IKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLF 1227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1233 LErwqvvfaQMDMRQRELDLLGRHMNSYnvsyewlIHWLGEARKRQEKIQAvPIGGSKALREQLaeeKKLLEEIEKNKDK 1312
Cdd:TIGR01612 1228 LE-------KIDEEKKKSEHMIKAMEAY-------IEDLDEIKEKSPEIEN-EMGIEMDIKAEM---ETFNISHDDDKDH 1289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1313 IDSCQKNAKAyIDSVKDYELQIL---TYKALQDPMASPLKKPKMDCASDNI-IQEYVTLRTRYSELMTLTS--QYIKFIT 1386
Cdd:TIGR01612 1290 HIISKKHDEN-ISDIREKSLKIIedfSEESDINDIKKELQKNLLDAQKHNSdINLYLNEIANIYNILKLNKikKIIDEVK 1368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1387 ETQRRLEDDEKaseklkeeerkkmaEIQAELDKQKQIAEAqaksvIKAEQEAQELKLKMKEEASKRqdvavDAEQQKQNI 1466
Cdd:TIGR01612 1369 EYTKEIEENNK--------------NIKDELDKSEKLIKK-----IKDDINLEECKSKIESTLDDK-----DIDECIKKI 1424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1467 QHELHHLksLSEQE-----IKSKSQQLEHALVSHTKIE----EEIHTIRIQLEMTIKQKKTAESELQQLRDKA----AEA 1533
Cdd:TIGR01612 1425 KELKNHI--LSEESnidtyFKNADENNENVLLLFKNIEmadnKSQHILKIKKDNATNDHDFNINELKEHIDKSkgckDEA 1502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1534 EKLRKAAQEDAErLRKQVAEETQK--KKNAEDELKRKSEAEKEAAKQKQKALDDLQ-KFKMQAEEAERRMKQAEEEKLRq 1610
Cdd:TIGR01612 1503 DKNAKAIEKNKE-LFEQYKKDVTEllNKYSALAIKNKFAKTKKDSEIIIKEIKDAHkKFILEAEKSEQKIKEIKKEKFR- 1580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1611 ikVVEEVAQKSAAtqlqshsmsfNVKASKLEESLKKEQGTVLQLQEeaeqLRKQQEEANKAREQAEKELETW-------R 1683
Cdd:TIGR01612 1581 --IEDDAAKNDKS----------NKAAIDIQLSLENFENKFLKISD----IKKKINDCLKETESIEKKISSFsidsqdtE 1644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1684 QKANEALRLRLQAEEEAQKKSKtqEEAERQKVEAERDAKKRAKAEDAALKQKDN-----AEKELEKQRTFAEQVAQQKLS 1758
Cdd:TIGR01612 1645 LKENGDNLNSLQEFLESLKDQK--KNIEDKKKELDELDSEIEKIEIDVDQHKKNyeigiIEKIKEIAIANKEEIESIKEL 1722
|
650
....*....|...
gi 736215636 1759 AEQECIRLKADFD 1771
Cdd:TIGR01612 1723 IEPTIENLISSFN 1735
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
63-153 |
1.66e-04 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 43.83 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 63 KWVNKHLMKSQR---HITDLYEDLRDGHNLISLLEVLSGETLPREKGRM---RFHKLQNVQIALDFLkhRQVKLVN-IRN 135
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAA--EKLGCKYfLTP 94
|
90
....*....|....*...
gi 736215636 136 DDIADGNPKLTLGLIWTI 153
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1449-1850 |
1.66e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.97 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1449 ASKRQDVAVDAEQQKQNIQHELHHLKSLSEQEIKSKSQqlehaLVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQ---- 1524
Cdd:PLN02939 27 SRRRLAVSCRARRRGFSSQQKKKRGKNIAPKQRSSNSK-----LQSNTDENGQLENTSLRTVMELPQKSTSSDDDHnras 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1525 -QLRDKAAEAEKLRKAAQEDAERLRK-QVAEETQKKKNAEDELKRKSEAEKEAAKQKQKAL---DDLQK----FKMQAEE 1595
Cdd:PLN02939 102 mQRDEAIAAIDNEQQTNSKDGEQLSDfQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILtekEALQGkiniLEMRLSE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1596 AERRMKQAEEEKLR-------QIKVVEEVAQKSAATQLQSHSMSfnvkaskLEESLKKEQGtvLQLQEEAEQLRKQQEEA 1668
Cdd:PLN02939 182 TDARIKLAAQEKIHveileeqLEKLRNELLIRGATEGLCVHSLS-------KELDVLKEEN--MLLKDDIQFLKAELIEV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1669 NKAREQAEKeLETWRQKANEALR----LRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRA--KAEDAA--LKQKDNAEK 1740
Cdd:PLN02939 253 AETEERVFK-LEKERSLLDASLRelesKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRAtnQVEKAAlvLDQNQDLRD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1741 ELEKQRTFAEQVAQQKLSAEQecirlkadfdhaeqqrglldnelqrlkkeVSATEKQRKLLEEELAKVRSEMDSLLKMKT 1820
Cdd:PLN02939 332 KVDKLEASLKEANVSKFSSYK-----------------------------VELLQQKLKLLEERLQASDHEIHSYIQLYQ 382
|
410 420 430
....*....|....*....|....*....|
gi 736215636 1821 EAEKKTMSNTEKSKQllESEALKMKQLADE 1850
Cdd:PLN02939 383 ESIKEFQDTLSKLKE--ESKKRSLEHPADD 410
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1589-1793 |
1.68e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.64 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1589 FKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQSHSMSfnvKASKLEESLKKEQgtvlQLQEEAEQLRKQQEEA 1668
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLE---RAEKMREELELEQ----QRRFEEIRLRKQRLEE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1669 NKAReQAEKELETWRQkanealrlrLQAeeeAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKdnAEKELEKQrtF 1748
Cdd:pfam15709 399 ERQR-QEEEERKQRLQ---------LQA---AQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQ--RQKELEMQ--L 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 736215636 1749 AEQVAQQKLSAEQECIRLKADFDHAEQQRgLLDNELQRLKKEVSA 1793
Cdd:pfam15709 462 AEEQKRLMEMAEEERLEYQRQKQEAEEKA-RLEAEERRQKEEEAA 505
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
1474-1760 |
1.68e-04 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 47.75 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1474 KSLSEQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQlrdkaAEAEKLRKAAQEdaerlrkqvae 1553
Cdd:pfam04747 53 EAFASLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEARR-----AEAEAKKRAAQE----------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1554 ETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKF--KMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQSHSM 1631
Cdd:pfam04747 117 EEHKQWKAEQERIQKEQEKKEADLKKLQAEKKKEKAvkAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1632 SFNVKASkleeslKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRlrlQAEEEAQKKSKTQEEAE 1711
Cdd:pfam04747 197 PTNTPAE------PAEQVQEITGKKNKKNKKKSESEATAAPASVEQVVEQPKVVTEEPHQ---QAAPQEKKNKKNKRKSE 267
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 736215636 1712 RQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAE 1760
Cdd:pfam04747 268 SENVPAASETPVEPVVETTPPASENQKKNKKDKKKSESEKVVEEPVQAE 316
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2163-2412 |
1.71e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.56 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2163 EAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQK-----KQADAEMAK---HKKEADQALKLKSQVEKELTMVKLRL 2234
Cdd:COG2268 92 DAVFYVKVNSDPEDIANAAERFLGRDPEEIEELAEEKlegalRAVAAQMTVeelNEDREKFAEKVQEVAGTDLAKNGLEL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2235 DE------TDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELL---KLKLKIEEQNRSLMKKDKDKtQKVL 2305
Cdd:COG2268 172 ESvaitdlEDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAeeaELEQEREIETARIAEAEAEL-AKKK 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2306 AE---EAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAqelQKQKDQAQEKA 2382
Cdd:COG2268 251 AEerrEAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEA---EKQAAEAEAEA 327
|
250 260 270
....*....|....*....|....*....|
gi 736215636 2383 kklleDKQQIQQRLDKETEGFQKSLEAERK 2412
Cdd:COG2268 328 -----EAEAIRAKGLAEAEGKRALAEAWNK 352
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2147-2465 |
1.74e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.89 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2147 RQKAAEAE---KQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKkeaDQALKLKSQV 2223
Cdd:pfam10174 464 RERLEELEslkKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKK---EECSKLENQL 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2224 EKELTM---VKLRLDETDKQKaLLDEELQRVKGEvndAVKQKAQVEDELAKVR-IQMDELLKLKlKIEEQNRSLMKKDKD 2299
Cdd:pfam10174 541 KKAHNAeeaVRTNPEINDRIR-LLEQEVARYKEE---SGKAQAEVERLLGILReVENEKNDKDK-KIAELESLTLRQMKE 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2300 KTQKVlaeeaGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMlkekmqaiqeatklkaeaQELQKQKDQAQ 2379
Cdd:pfam10174 616 QNKKV-----ANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELM------------------GALEKTRQELD 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2380 EKAKKLLEDKQQIQQRldketEGFQKSLEAERKRQLEvsaeaETLRLKVKELSDAQSKA-------ENEAKKFKKQADEA 2452
Cdd:pfam10174 673 ATKARLSSTQQSLAEK-----DGHLTNLRAERRKQLE-----EILEMKQEALLAAISEKdaniallELSSSKKKKTQEEV 742
|
330
....*....|....*....
gi 736215636 2453 ------KARLKDTEKQSTE 2465
Cdd:pfam10174 743 malkreKDRLVHQLKQQTQ 761
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1505-1668 |
1.80e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 47.77 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1505 IRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAA-QEDAERLRKQVAEETQKKknaeDELKRKSEAEKEAAKQKQKAL 1583
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAsFERLAELRDELAELEEEL----EALKARWEAEKELIEEIQELK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1584 DDLQKFKMQAEEAERRMKQAEEE-----KLRQIKV-VEEVAQK-SAATqlqshsmsfNVKASKLEESlkkEQGTVLQLQE 1656
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEElaelaPLLREEVtEEDIAEVvSRWT---------GIPVGKLLEG---EREKLLNLEE 545
|
170
....*....|....*
gi 736215636 1657 EaeqLRKQ---QEEA 1668
Cdd:COG0542 546 E---LHERvigQDEA 557
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1415-1585 |
1.82e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1415 AELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNIQHELhhlKSLSEQEIKSKSQQLEhalvs 1494
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI---EEVEARIKKYEEQLGN----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1495 hTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKE 1574
Cdd:COG1579 85 -VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
170
....*....|.
gi 736215636 1575 AAKQKQKALDD 1585
Cdd:COG1579 164 EREELAAKIPP 174
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2200-2659 |
1.89e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2200 KQADAEMAKHKKEADQALKLKSQVEKELTMvKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDEL 2279
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVLQKDYNDYIKK-KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2280 LKLkLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAESNlAEQRALAEKMLKEKMQAIQ 2359
Cdd:PRK01156 394 SEI-LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQ-SVCPVCGTTLGEEKSNHII 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2360 EatKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAE 2439
Cdd:PRK01156 472 N--HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYE 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2440 nEAKKFKKQADEAKARLKDTEKQSTETVVQKLETQRLQSTREA---------DGLKEAIADLEKEREKLKKEAEELQNKS 2510
Cdd:PRK01156 550 -EIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEikkqlndleSRLQEIEIGFPDDKSYIDKSIREIENEA 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2511 NKMANtQKEEIEQQKAIIQKSfiserelllkrQKAVEDEKKKLQKQFEDEVKKAEALKDEQErqrklMEEEKKKLQAIMD 2590
Cdd:PRK01156 629 NNLNN-KYNEIQENKILIEKL-----------RGKIDNYKKQIAEIDSIIPDLKEITSRIND-----IEDNLKKSRKALD 691
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736215636 2591 AAVKKQKEAEADMKNKQTEMEVLE------KKRLDQEKQLGAENQKLREKLQCLEGASKQSATKQVASKTIEVQT 2659
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSdrindiNETLESMKKIKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSLT 766
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1666-1787 |
1.91e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 45.33 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1666 EEANKAREQAEKELETWRQKANEALrlrlqaEEEAQKKSKTQEEAERQKVEAERDAK-------KRAKAEDAALKQKDNA 1738
Cdd:PRK07352 49 EERREAILQALKEAEERLRQAAQAL------AEAQQKLAQAQQEAERIRADAKARAEairaeieKQAIEDMARLKQTAAA 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 736215636 1739 EKELEKQRTFAE---QVAQQKLS-AEQEcirLKADFDHAEQQRgLLDNELQRL 1787
Cdd:PRK07352 123 DLSAEQERVIAQlrrEAAELAIAkAESQ---LPGRLDEDAQQR-LIDRSIANL 171
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1636-1823 |
1.98e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1636 KASKLEESLK--KEQGTVLQLQEEAEQLRKQQEEANKAREQAE---KELETWRQKANEALRLRLQAEEEAQKKSKTQE-E 1709
Cdd:COG3206 190 ELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARaelAEAEARLAALRAQLGSGPDALPELLQSPVIQQlR 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1710 AERQKVEAERD-AKKRAKAEDAALKQkdnAEKELEKQRTFAEQVAQQKLSAeqecirLKADFDHAEQQRGLLDNELQRLK 1788
Cdd:COG3206 270 AQLAELEAELAeLSARYTPNHPDVIA---LRAQIAALRAQLQQEAQRILAS------LEAELEALQAREASLQAQLAQLE 340
|
170 180 190
....*....|....*....|....*....|....*...
gi 736215636 1789 KEVSAT-EKQRKL--LEEELAKVRSEMDSLLKMKTEAE 1823
Cdd:COG3206 341 ARLAELpELEAELrrLEREVEVARELYESLLQRLEEAR 378
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3772-3805 |
2.23e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.23e-04
10 20 30
....*....|....*....|....*....|....
gi 736215636 3772 LLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPE 3805
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1651-2068 |
2.25e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.43 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1651 VLQLQEEAEQLRKQQE----EANKAREQAEKELETWRQKANEAL-RLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRA 1725
Cdd:pfam05557 11 LSQLQNEKKQMELEHKrariELEKKASALKRQLDRESDRNQELQkRIRLLEKREAEAEEALREQAELNRLKKKYLEALNK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1726 KAEDAALKQKDNAEKELEKQRTFAE-----QVAQQKLSA---EQECIR-----LKADFDHAEQQRglldNELQRLKKEVS 1792
Cdd:pfam05557 91 KLNEKESQLADAREVISCLKNELSElrrqiQRAELELQStnsELEELQerldlLKAKASEAEQLR----QNLEKQQSSLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1793 ATEKQRKLLEEELAKvrSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAEEAKK---QRQTAE 1869
Cdd:pfam05557 167 EAEQRIKELEFEIQS--QEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRkleREEKYR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1870 EEAARQRAEAEKILKE----KLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAY---------QRKLLEDQAAQHK 1936
Cdd:pfam05557 245 EEAATLELEKEKLEQElqswVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLtssarqlekARRELEQELAQYL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1937 HDIQEKIIHLKsssdsemvRQKTIVEETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKVI---AEETQKSKLKA 2013
Cdd:pfam05557 325 KKIEDLNKKLK--------RHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLLERIeeaEDMTQKMQAHN 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 736215636 2014 EAEAEKLKKLAAEEEKKRKESEEKVKRITA-AEEEAARQCKAAQEEVARLEKKADE 2068
Cdd:pfam05557 397 EEMEAQLSVAEEELGGYKQQAQTLERELQAlRQQESLADPSYSKEEVDSLRRKLET 452
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
1520-1891 |
2.25e-04 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 47.33 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1520 ESELQQLRDKAAEAEKLRKAAQEdaerLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERR 1599
Cdd:pfam01271 157 EGELSEVFENPRSQATLKKVFEE----VSRLDTPSKQKREKSDEREKSSQESGEDTYRQENIPQEDQVGPEDQEPSEEGE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1600 MKQAEEEKLRQIKVVEEVAQ----KSAATQLQSHSMSFNVKASKLEES--LKKEQGTVLQLQEEAEQLRKQQEEAnkaRE 1673
Cdd:pfam01271 233 EDATQEEVKRSRPRTHHGRSlpdeSSRGGQLGLEEEASEEEEEYGEESrgLSAVQTYLLRLVNARGRGRSEKRAE---RE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1674 QAEKELETWRQKANEALRLRLQA-----EEEAQKKSKTQEEAERQKVEAERdakkrakAEDAALKQKDNAEKELEKQRTF 1748
Cdd:pfam01271 310 RSEESEEEELKRASPYEELEITAnlqipPSEEERMLKKAGRSPRGRVDEAG-------ALEALEALEEKRKLDLDHSRVF 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1749 AEQ-----VAQQKLSAEQECIRL----KADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVR-SEMDSLLKM 1818
Cdd:pfam01271 383 ESSedgapRAPQGAWVEALRNYLsygeEGMEGKWNQQGPYFPNEENREEARFRLPQYLGELSNPWEDPKQwKPSDFERKE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1819 KTE------AEKKTMSNTEKSK----------QLLESEALKMKQLADEATRLRSV---------------AEEAKKQRQT 1867
Cdd:pfam01271 463 LTAdkflegEEENEYTLSMKNSfpeynydgyeKRVPSPGLDLKRQYDPVAREDQLlhyrkkssefpdfydSEEKKEPPVG 542
|
410 420
....*....|....*....|....*.
gi 736215636 1868 A--EEEAARQRAEAEKILKEKLAAIN 1891
Cdd:pfam01271 543 AekEEDSANRQTRDEDKELENLAAMD 568
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1719-2165 |
2.28e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.21 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1719 RDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQR 1798
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1799 KLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAE 1878
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1879 AEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSSDSEMVRQK 1958
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1959 TIVEETLRQKKIVEEEIHIIRINFEKASKGKSDLENELKKLKVIAEETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKV 2038
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2039 KRITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKM 2118
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 736215636 2119 KEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAA 2165
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASA 528
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1520-1743 |
2.28e-04 |
|
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: 45.81 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1520 ESELQQLRDkaAEAEKLRKAAQEDAERLRKqvaeeTQKKKNAEDELKRK----SEAEKEAAKQKQKALDDLQKFKMQAEE 1595
Cdd:pfam15665 13 EAEIQALKE--AHEEEIQQILAETREKILQ-----YKSKIGEELDLKRRiqtlEESLEQHERMKRQALTEFEQYKRRVEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1596 aerrmkqaeeeklRQIKVVEEVAQKSAatqlqshSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQA 1675
Cdd:pfam15665 86 -------------RELKAEAEHRQRVV-------ELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALEELRAKHRQEI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1676 EKELETWRQKANEALRLRLQAEEeaqkKSKTQEEAERQKVEAERDAKKRAKA--EDAALKQKDNAEKELE 1743
Cdd:pfam15665 146 QELLTTQRAQSASSLAEQEKLEE----LHKAELESLRKEVEDLRKEKKKLAEeyEQKLSKAQAFYERELE 211
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2196-2489 |
2.32e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 46.73 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2196 LKQKKQADAEMAKHKKEadqalklksqVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQ 2275
Cdd:pfam15905 61 LKKKSQKNLKESKDQKE----------LEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2276 MDELLK----LKLKIEEqnrslmkkdkDKTQKvlaeeagKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKML 2351
Cdd:pfam15905 131 LLELTRvnelLKAKFSE----------DGTQK-------KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2352 KE-KMQAIQEATKLKAEAQELQKQKDQAQekakKLLEDKQQIQQRLDKetegfqksleaERKRQLEVSAEAETLRLKVKE 2430
Cdd:pfam15905 194 EHsKGKVAQLEEKLVSTEKEKIEEKSETE----KLLEYITELSCVSEQ-----------VEKYKLDIAQLEELLKEKNDE 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 2431 LSDAQSKAENEAKKFKKQADEAKARLKDTEKQsTETVVQKLETQRLQSTREADGLKEAI 2489
Cdd:pfam15905 259 IESLKQSLEEKEQELSKQIKDLNEKCKLLESE-KEELLREYEEKEQTLNAELEELKEKL 316
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3846-3882 |
2.36e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.36e-04
10 20 30
....*....|....*....|....*....|....*..
gi 736215636 3846 LRVLEAQNATGGFIDPEYYFRLPTDVAMQRGYINKET 3882
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2044-2252 |
2.38e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.25 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2044 AEEEAARQCKAAQEEVARLEKKAD--EANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEE 2121
Cdd:PRK05035 463 EREKAAREARHKKAAEARAAKDKDavAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAA 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2122 FE-------------NAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEK-LKKAAEEEASK 2187
Cdd:PRK05035 543 ADpkkaavaaaiaraKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVdPKKAAVAAAIA 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736215636 2188 RAAAEAEALKQK-KQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVK 2252
Cdd:PRK05035 623 RAKAKKAEQQANaEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAK 688
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1382-1597 |
2.42e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1382 IKFITETQRRLEDDEKASEKLKEEERKKMAEIQAELDK-QKQIAEAQAKSViKAEQEAQELKLKMKEEASKRQDVAVDAE 1460
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNElQAELEALQAEID-KLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1461 QQKQNIQHELHHLKSLSEQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEmtiKQKKTAESELQQLRDKAAEAEKLRKAA 1540
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELE---AKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 1541 QEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAE 1597
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
58-123 |
2.44e-04 |
|
first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409070 Cd Length: 106 Bit Score: 43.42 E-value: 2.44e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 58 KKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPREK----GRMRFHKLQNVQIALDFL 123
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1418-1623 |
2.66e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1418 DKQKQIAEAQAKSVIKAEQEAQELklkmkeeaskRQDVAVDAEQQKQNIQhelhhlKSLSEQEIKSKSQQLEhalvshtK 1497
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEEL----------QQKQAAEQERLKQLEK------ERLAAQEQKKQAEEAA-------K 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1498 IEEEihtiriqlemtiKQKKTAESELQQLRDKAAEAEKLRKAAQEDAerlrKQVAEETQKKKNAEdelkrkseAEKEAAK 1577
Cdd:PRK09510 126 QAAL------------KQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA----KKAAAEAKKKAEAE--------AAKKAAA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 736215636 1578 QKQKALDDLQKFKMQAE-----EAERRMKQAEEEKLRQIKVVEEVAQKSAA 1623
Cdd:PRK09510 182 EAKKKAEAEAAAKAAAEakkkaEAEAKKKAAAEAKKKAAAEAKAAAAKAAA 232
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1311-1572 |
2.74e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 46.92 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1311 DKIDSCQKNAKAYIDSVKDYELQ--------ILTYKALQDPMASPLKKPKMDCASDNIIQEYVTLRTRYSELMTLTSQyi 1382
Cdd:pfam05262 79 DHILNLRRILAGYLMAAYGYERSdaetiakfITIYNAVYRGDLDYFKEFYKEVVTKSLTKENAGLARRYDQWPGKTQI-- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1383 kFITETQRRLEDDEKASEKLKEEERKKMAEIQAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQ 1462
Cdd:pfam05262 157 -VIPLKKNILSGNVSDVDTDSISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1463 KQNIQHELHHLKSLSEQEIKSKSQQLEHALVSHTKIEEEI-HTIRIQLEMTIKQKKTAESELQQLRDKAAE--------A 1533
Cdd:pfam05262 236 ADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVaENQKREIEKAQIEIKKNDEEALKAKDHKAFdlkqeskaS 315
|
250 260 270
....*....|....*....|....*....|....*....
gi 736215636 1534 EKLRKAAQEDAERLRKQVAEETQKKKNaEDELKRKSEAE 1572
Cdd:pfam05262 316 EKEAEDKELEAQKKREPVAEDLQKTKP-QVEAQPTSLNE 353
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1410-1577 |
2.85e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1410 MAEIQAELDKQKQIAEAQAKsvikaeQEAQELKLKMKEEA-SKRQDVavdAEQQKQNIQHelhhlkslsEQEIKSKSQQL 1488
Cdd:PRK12704 44 LEEAKKEAEAIKKEALLEAK------EEIHKLRNEFEKELrERRNEL---QKLEKRLLQK---------EENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1489 EhalvshtKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKaaEAEKLRKAA---QEDA-ERLRKQVAEETQKKKNA--- 1561
Cdd:PRK12704 106 E-------KREEELEKKEKELEQKQQELEKKEEELEELIEE--QLQELERISgltAEEAkEILLEKVEEEARHEAAVlik 176
|
170
....*....|....*.
gi 736215636 1562 EDELKRKSEAEKEAAK 1577
Cdd:PRK12704 177 EIEEEAKEEADKKAKE 192
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
57-164 |
2.88e-04 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 44.23 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 57 QKKTFTKWVNKHLMKSQ--RHIT-------DLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 123
Cdd:cd21324 25 EKYAFVNWINKALENDPdcKHVIpmnpntdDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 736215636 124 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 164
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1389-1694 |
2.88e-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: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1389 QRRLEDDEKASEKLKEEERKKMAEIQAELDKQKQIAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVDAEQQKQNI-- 1466
Cdd:pfam13868 35 KAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEed 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1467 --QHELHHLKSLSEQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDA 1544
Cdd:pfam13868 115 qaEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1545 ERLRKQVAEETQKKKNAEDELKRKS-EAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAA 1623
Cdd:pfam13868 195 KAQDEKAERDELRAKLYQEEQERKErQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDE 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736215636 1624 TQLQshsmsfnVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRL 1694
Cdd:pfam13868 275 EIEQ-------EEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| Selenoprotein_S |
pfam06936 |
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) ... |
1664-1741 |
2.90e-04 |
|
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) sequences. SelS is a plasma membrane protein and is present in a variety of tissues and cell types. Selenoprotein S (SelS) is an intrinsically disordered protein. It formsa selenosulfide bond between cys 174 and Sec 188, that has a redox potential -234 mV. In vitro, SelS is an efficient reductase that depends on the presence of selenocysteine. Due to the high reactivity, SelS also has peroxidase activity that can catalyze the reduction of hydrogen peroxide. It is also resistant to inactivation by hydrogen peroxide which might provide evolutionary advantage compared to cysteine containing peroxidases.
Pssm-ID: 462043 [Multi-domain] Cd Length: 192 Bit Score: 45.21 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1664 QQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQ------KKSKTQEEAERQKVEaERDAKKRAKAEDAALKQKDN 1737
Cdd:pfam06936 62 RQRSSDHSAATVDPDLVVKRQEALEASRLRMQEELDAQaekfkeKQKQLEEEKRRQKIE-MWESMQEGKSYKGNAKLAQE 140
|
....
gi 736215636 1738 AEKE 1741
Cdd:pfam06936 141 ETEE 144
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2311-2631 |
2.97e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2311 KMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQ 2390
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2391 QIQ---QRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQadEAKARLKDTEKQSTETV 2467
Cdd:COG4372 119 ELQkerQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--EAEQALDELLKEANRNA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2468 VQKLETQRLQSTREADGLKEAIADlekeREKLKKEAEELQNKSNKMANTQKEEIEQQKAIIQKSFISERELLLKRQKAVE 2547
Cdd:COG4372 197 EKEEELAEAEKLIESLPRELAEEL----LEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2548 DEKKKLQKQFEDEVKKAEALKDEQERQRKLMEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEKKRLDQEKQLGAE 2627
Cdd:COG4372 273 TEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLD 352
|
....
gi 736215636 2628 NQKL 2631
Cdd:COG4372 353 NDVL 356
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1905-2199 |
3.14e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1905 KAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIhlksssdSEMVRQKTIVEETLRQKKIVEEEihiirinfeK 1984
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRA-------AEQARQKELEQRAAAEKAAKQAE---------Q 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1985 ASKGKSDLENELKKLKVIAEETQKSKLKAEAEAEKLKKLAAEeekkrkeseekvkritaAEEEAARQCKAAQeevarlEK 2064
Cdd:TIGR02794 110 AAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQ-----------------AEEEAKAKAAAEA------KK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2065 KADEANKQkekaekeaekqvivAKEAAQKCSSAEQKAQEVLSKNKEdslAQQKMKEEFENAKRLAQAaekakekaekeaa 2144
Cdd:TIGR02794 167 KAEEAKKK--------------AEAEAKAKAEAEAKAKAEEAKAKA---EAAKAKAAAEAAAKAEAE------------- 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736215636 2145 llRQKAAEAEKQKKSAEEEA------AKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQK 2199
Cdd:TIGR02794 217 --AAAAAAAEAERKADEAELgdifglASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2191-2636 |
3.18e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2191 AEAEALKQKKQADAEMAKHKKEADQALKL---KSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQK----- 2262
Cdd:PRK11281 43 AQLDALNKQKLLEAEDKLVQQDLEQTLALldkIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstls 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2263 -AQVEDELAKVRIQMDEllklklkieeqnrslmkkdkdkTQKVLAEEAGKMKSLAEEAARlsVEAEETARQRQIAE---- 2337
Cdd:PRK11281 123 lRQLESRLAQTLDQLQN----------------------AQNDLAEYNSQLVSLQTQPER--AQAALYANSQRLQQirnl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2338 --SNLAEQRALAEKmLKEKMQAIQEATklkaEAQELQKQK-----DQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAE 2410
Cdd:PRK11281 179 lkGGKVGGKALRPS-QRVLLQAEQALL----NAQNDLQRKslegnTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2411 RkrqLEVSAEaetlrlKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTE---TVVQK-LETQ----RLQSTREA 2482
Cdd:PRK11281 254 R---LTLSEK------TVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEklnTLTQQnLRVKnwldRLTQSERN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2483 dgLKEAIADLE---------KEREKLKKEAEELQNKSNKMANTQKE--EIEQQkaiiqksfiseRELLLKRQKAVEDEKK 2551
Cdd:PRK11281 325 --IKEQISVLKgslllsrilYQQQQALPSADLIEGLADRIADLRLEqfEINQQ-----------RDALFQPDAYIDKLEA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2552 KLQKQFEDEVKKAeaLKDEQERQRKLMEEEKKKLQAIMDAAVKKQkeaeadmknkqtemevlekkrLDQeKQLGAENQKL 2631
Cdd:PRK11281 392 GHKSEVTDEVRDA--LLQLLDERRELLDQLNKQLNNQLNLAINLQ---------------------LNQ-QQLLSVSDSL 447
|
....*
gi 736215636 2632 REKLQ 2636
Cdd:PRK11281 448 QSTLT 452
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2337-2462 |
3.20e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2337 ESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLD-----KETEGFQKSLEAER 2411
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnKEYEALQKEIESLK 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 2412 KRQ-------LEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQ 2462
Cdd:COG1579 103 RRIsdledeiLELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2334-2488 |
3.71e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2334 QIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEgfQKSLEAERKR 2413
Cdd:TIGR02794 36 EIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKA--AKQAEQAAKQ 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736215636 2414 QLEVSAEAEtlRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDtEKQSTETVVQKLETQRLQSTREADGLKEA 2488
Cdd:TIGR02794 114 AEEKQKQAE--EAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEA-KAKAAAEAKKKAEEAKKKAEAEAKAKAEA 185
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2300-2623 |
3.74e-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: 46.07 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2300 KTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQ 2379
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2380 EKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAEtlrLKVKELSDAQSKAENEAKKFKKQADEAKARLKDt 2459
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREED---ERILEYLKEKAEREEEREAEREEIEEEKEREIA- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2460 ekqstetVVQKLETQRLQSTREADGLKEAIADLEKEREKLKKEAEELQNKSNKMANTQKEEIEQQKAIiqksfisERELL 2539
Cdd:pfam13868 188 -------RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELK-------ERRLA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2540 LKRQKAVEDEKKKLQKQFEDEVKKAEalkdEQERQRKLMEEEKKKLQAIMD---AAVKKQKEAEADMKNKQTEMEVLEKK 2616
Cdd:pfam13868 254 EEAEREEEEFERMLRKQAEDEEIEQE----EAEKRRMKRLEHRRELEKQIEereEQRAAEREEELEEGERLREEEAERRE 329
|
....*..
gi 736215636 2617 RLDQEKQ 2623
Cdd:pfam13868 330 RIEEERQ 336
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1853-2009 |
3.74e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.63 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1853 RLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIAlkAKEAENERLKRKAED---EAYQRKLLE 1929
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE--ELQREEERLVQKEEQldaRAEKLDNLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1930 DQAAQHKH---DIQEKIIHLKSSSDSEMVRQKTIVEETLRQ-------KKIVEEEIHIIRINFEKAskgksDLENELKKL 1999
Cdd:PRK12705 105 NQLEEREKalsARELELEELEKQLDNELYRVAGLTPEQARKlllklldAELEEEKAQRVKKIEEEA-----DLEAERKAQ 179
|
170
....*....|
gi 736215636 2000 KVIAEETQKS 2009
Cdd:PRK12705 180 NILAQAMQRI 189
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1661-2007 |
3.76e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1661 LRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEK 1740
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1741 ELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLkkevsatEKQRKLLEEELAKVRSEMDSLLKMKT 1820
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL-------EEQLESLQEELAALEQELQALSEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1821 EAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEA 1900
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1901 EIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSSDSEMVRQKTIVEETLRQKKIVEEEIHIIRI 1980
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
330 340
....*....|....*....|....*..
gi 736215636 1981 NFEKASKGKSDLENELKKLKVIAEETQ 2007
Cdd:COG4372 342 LLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2322-2632 |
3.76e-04 |
|
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: 46.67 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2322 LSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKL----------KAEAQELQKQ-------KDQAQEKAKK 2384
Cdd:pfam07111 61 LSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELdalavaekagQAEAEGLRAAlagaemvRKNLEEGSQR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2385 LLEDKQQI-QQRLDKETEGFQKSLE--AERKRQLEVSAEA-ETLRL-KVKELSDAQSKAENEAKKFKKQADEAKARLKDT 2459
Cdd:pfam07111 141 ELEEIQRLhQEQLSSLTQAHEEALSslTSKAEGLEKSLNSlETKRAgEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2460 E---KQSTETVVQKLETQRLQSTREA--DGLKEAIADLEKEREKLKKEAEELQNKSNKMAnTQKEEIEQQkaiIQKSFIS 2534
Cdd:pfam07111 221 EslrKYVGEQVPPEVHSQTWELERQEllDTMQHLQEDRADLQATVELLQVRVQSLTHMLA-LQEEELTRK---IQPSDSL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2535 ERELLLKRQKAVEDEKKK-------LQKQFEDEVKKAEALKDE-QERQRKLMEEEKKklQAIMDAAVK-KQKEAEAD--- 2602
Cdd:pfam07111 297 EPEFPKKCRSLLNRWREKvfalmvqLKAQDLEHRDSVKQLRGQvAELQEQVTSQSQE--QAILQRALQdKAAEVEVErms 374
|
330 340 350
....*....|....*....|....*....|
gi 736215636 2603 MKNKQTEMEVLEKKRLDQEKQLGAENQKLR 2632
Cdd:pfam07111 375 AKGLQMELSRAQEARRRQQQQTASAEEQLK 404
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1662-1937 |
3.84e-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: 46.07 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1662 RKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKE 1741
Cdd:pfam13868 24 RDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1742 LEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRglldNELQRLKKEvsatekQRKLLEEELAKVRSEMDSLLKMKTE 1821
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQ----AEWKELEKE------EEREEDERILEYLKEKAEREEEREA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1822 AEKKTMSNTEKSKQLLESEALKMKQLADEATRLRS--VAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTE 1899
Cdd:pfam13868 174 EREEIEEEKEREIARLRAQQEKAQDEKAERDELRAklYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLA 253
|
250 260 270
....*....|....*....|....*....|....*...
gi 736215636 1900 AEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKH 1937
Cdd:pfam13868 254 EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEH 291
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1638-1812 |
3.94e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1638 SKLEESLKKEQGTVLQLQEEAEQLRKQ-----QEEANKAREQAEKELETWRQKANEALRlRLQAEEEAQKKSktQEEAER 1712
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEalleaKEEIHKLRNEFEKELRERRNELQKLEK-RLLQKEENLDRK--LELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1713 QKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQqkLSAEQecirlkadfdhAEQQrgLLDNELQRLKKEVS 1792
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG--LTAEE-----------AKEI--LLEKVEEEARHEAA 172
|
170 180
....*....|....*....|
gi 736215636 1793 ATEKQrkllEEELAKVRSEM 1812
Cdd:PRK12704 173 VLIKE----IEEEAKEEADK 188
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1514-1588 |
3.96e-04 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 43.45 E-value: 3.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736215636 1514 KQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAedelkRKSEAEKEAAKQKQKALDDLQK 1588
Cdd:PRK07353 54 EAEKLEAQYEQQLASARKQAQAVIAEAEAEADKLAAEALAEAQAEAQA-----SKEKARREIEQQKQAALAQLEQ 123
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2307-2442 |
4.06e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 46.53 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2307 EEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRalaekmlKEKMQAIQEATKL--KAEAQElQKQKDQAQEKAKK 2384
Cdd:pfam05262 210 EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQR-------DEVRQKQQEAKNLpkPADTSS-PKEDKQVAENQKR 281
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736215636 2385 LLEDKQQIQQRLDKE--------TEGFQKSLEAERKRQLEVSAEAETLRL-------KVKELSDAQSKAENEA 2442
Cdd:pfam05262 282 EIEKAQIEIKKNDEEalkakdhkAFDLKQESKASEKEAEDKELEAQKKREpvaedlqKTKPQVEAQPTSLNED 354
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1516-1817 |
4.12e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 46.56 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1516 KKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQvaeeTQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQA-E 1594
Cdd:pfam05667 211 RNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRKR----TKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFsG 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1595 EAERRMKQAEEEKLRQikvveevAQKSAATQLQSHSMSFNVKASKLEESLKKEQGTVL-QLQEEAEQLR----------- 1662
Cdd:pfam05667 287 SSTTDTGLTKGSRFTH-------TEKLQFTNEAPAATSSPPTKVETEEELQQQREEELeELQEQLEDLEssiqelekeik 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1663 ------KQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAQK-KSKTQEEAERQKVEAERDAKKRAK--AEDAALK 1733
Cdd:pfam05667 360 klessiKQVEEELEELKEQNEELEKQYKVKKKTLDLLPDAEENIAKlQALVDASAQRLVELAGQWEKHRVPliEEYRALK 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1734 QKdNAEKELEKQRTFAE-QVAQQKLSAEQECIRLKadfdhAEQQRGLLDnELQRLKKEVSATEKQRKLLE---------E 1803
Cdd:pfam05667 440 EA-KSNKEDESQRKLEEiKELREKIKEVAEEAKQK-----EELYKQLVA-EYERLPKDVSRSAYTRRILEivknikkqkE 512
|
330
....*....|....
gi 736215636 1804 ELAKVRSEMDSLLK 1817
Cdd:pfam05667 513 EITKILSDTKSLQK 526
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2820-2852 |
4.22e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.22e-04
10 20 30
....*....|....*....|....*....|...
gi 736215636 2820 LSAERAATGFKDPYTGAKISLFEAMKKGLIEKE 2852
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1636-1926 |
4.28e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1636 KASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANkareqaeKELETWRQKANEaLRLRLQAEEEAQKKSKTQEEAERQKV 1715
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELN-------EELKELAEKRDE-LNAQVKELREEAQELREKRDELNEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1716 EAERDAKKRAKAEDAALKqkdnaeKELEKQRTFAEQVAQQKLSAEQecirLKADFDHAE--QQRGLLD--------NELQ 1785
Cdd:COG1340 74 KELKEERDELNEKLNELR------EELDELRKELAELNKAGGSIDK----LRKEIERLEwrQQTEVLSpeeekelvEKIK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1786 RLKKEVSATEKQRKlLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLEsealKMKQLADEATRLRSVAEEAKKQR 1865
Cdd:COG1340 144 ELEKELEKAKKALE-KNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHE----EMIELYKEADELRKEADELHKEI 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736215636 1866 QTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRK 1926
Cdd:COG1340 219 VEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKG 279
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2221-2583 |
4.59e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.49 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2221 SQVEKELTMVKLRLDETDKQKALLD-EELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELLKLKL-------KIEEQNRS 2292
Cdd:COG5185 206 SIKESETGNLGSESTLLEKAKEIINiEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLgenaessKRLNENAN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2293 LMKKDKDKTQKVLAE--EAGKMKSLAEE------AARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKL 2364
Cdd:COG5185 286 NLIKQFENTKEKIAEytKSIDIKKATESleeqlaAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIEN 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2365 KAE-------AQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSK 2437
Cdd:COG5185 366 IVGevelsksSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2438 AENEAKKFKKQADEAKARLKDTEKQSTETVVQKletqrlqstrEADGLKEAIADLEKEREKLKKEAEELQNKSNKMANTQ 2517
Cdd:COG5185 446 LISELNKVMREADEESQSRLEEAYDEINRSVRS----------KKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGV 515
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736215636 2518 KEEIEQQKAIIqKSFISERELLLKRQKAVEDEKKKLQKQFEDEVKKAEAlkdeQERQRKLMEEEKK 2583
Cdd:COG5185 516 RSKLDQVAESL-KDFMRARGYAHILALENLIPASELIQASNAKTDGQAA----NLRTAVIDELTQY 576
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3476-3512 |
4.66e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.66e-04
10 20 30
....*....|....*....|....*....|....*..
gi 736215636 3476 KLLAAEKAVTGYKDPYTGSKISLFQAMKKELVLREHA 3512
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1772-2215 |
4.91e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 46.54 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1772 HAEQQRGllDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLK----------------MKTEAEKKTMSNTEKSKQ 1835
Cdd:NF033838 36 HAEEVRG--GNNPTVTSSGNESQKEHAKEVESHLEKILSEIQKSLDkrkhtqnvalnkklsdIKTEYLYELNVLKEKSEA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1836 LLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTE-AEIALKAKEAENERL 1914
Cdd:NF033838 114 ELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEiAESDVEVKKAELELV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1915 KRKAedeayqrklledqaaqhkhdiqekiihlKSSSDSEMVRQktiVEETLRQKKIVEEEIHIIRINFEKAskgksdlEN 1994
Cdd:NF033838 194 KEEA----------------------------KEPRDEEKIKQ---AKAKVESKKAEATRLEKIKTDREKA-------EE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1995 ELKKLKVIAEETQKSKLKAEAEAEKLKKlaaeeekkrkeseekvkritaaeeeaaRQCKAAQEEVARLEKKADEANKQKE 2074
Cdd:NF033838 236 EAKRRADAKLKEAVEKNVATSEQDKPKR---------------------------RAKRGVLGEPATPDKKENDAKSSDS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2075 KAEKEAEKQVIVAKEaaQKCSSAEQKAQEvlsknkedslAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEA- 2153
Cdd:NF033838 289 SVGEETLPSPSLKPE--KKVAEAEKKVEE----------AKKKAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELe 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2154 ---EKQKKSAEEEAAKQAKAQKDA--------EKLK------------KAAEEEASKRAAAEAEALKQKKQADAEMAKHK 2210
Cdd:NF033838 357 lvkEEAKEPRNEEKIKQAKAKVESkkaeatrlEKIKtdrkkaeeeakrKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPE 436
|
....*
gi 736215636 2211 KEADQ 2215
Cdd:NF033838 437 KPAEQ 441
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2365-2603 |
4.94e-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: 45.61 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2365 KAEAQELQKQKDQAQEKAKKllEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAEtlrlkvKELSDAQSKAENEAKK 2444
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKK--EQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAE------KAAKQAEQAAKQAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2445 fKKQADEAKARLKDTEKQSTETVVQKLETQRLQSTREADGLKEAIADLEkereklkkeaeelqnKSNKMANTQKEEIEQQ 2524
Cdd:TIGR02794 118 -QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAK---------------KKAEEAKKKAEAEAKA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2525 KAiiqksfiserellLKRQKAVEDEKKKLQKQFEDEVKKAEALKDEQERQRKL-MEEEKKKLQAIMDAAVKKQKEAEADM 2603
Cdd:TIGR02794 182 KA-------------EAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAaAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1513-1762 |
5.05e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 45.80 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1513 IKQKKTAESElQQLRDKAAEAEKLRKaaqedaERLRKQVAEETQKKKNAEDELKrkseaEKEAAKQKQKALDDLQKFKMQ 1592
Cdd:pfam15558 84 RREKQVIEKE-SRWREQAEDQENQRQ------EKLERARQEAEQRKQCQEQRLK-----EKEEELQALREQNSLQLQERL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1593 AEEAERRMKQAEEEklrQIKVVEEVAQKSAATQLQSHSMSFNVKASK------LEESLKKEQGTVLQLQE---------- 1656
Cdd:pfam15558 152 EEACHKRQLKEREE---QKKVQENNLSELLNHQARKVLVDCQAKAEEllrrlsLEQSLQRSQENYEQLVEerhrelreka 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1657 --EAEQLRKQQEEANKAREQAEKELETWRQKANEALR-LRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALK 1733
Cdd:pfam15558 229 qkEEEQFQRAKWRAEEKEEERQEHKEALAELADRKIQqARQVAHKTVQDKAQRARELNLEREKNHHILKLKVEKEEKCHR 308
|
250 260 270
....*....|....*....|....*....|.
gi 736215636 1734 Q--KDNAEKELEKqrtfAEQVAQQKLSAEQE 1762
Cdd:pfam15558 309 EgiKEAIKKKEQR----SEQISREKEATLEE 335
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
2151-2254 |
5.18e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 44.18 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2151 AEAEKQKKSAEEEAAKQ----AKAQKDAEKLKKAAEEEAS-------KRAAAEAEALKQKKQADAEmakhkKEADQAL-K 2218
Cdd:PRK07352 60 KEAEERLRQAAQALAEAqqklAQAQQEAERIRADAKARAEairaeieKQAIEDMARLKQTAAADLS-----AEQERVIaQ 134
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 736215636 2219 LKSQV-----EKELTMVKLRLDEtDKQKALLDEELQRVKGE 2254
Cdd:PRK07352 135 LRREAaelaiAKAESQLPGRLDE-DAQQRLIDRSIANLGGN 174
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1473-1689 |
5.34e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1473 LKSLSEQ--EIKSKSQQLEHALVSHtKIEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQ 1550
Cdd:COG3206 177 LEFLEEQlpELRKELEEAEAALEEF-RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1551 VAEETQKKkNAEDELKRKSEAEKEAAKQKQKALD---DLQKFKMQAEEAERRMKQAEEEKLRQIkvveEVAQKSAATQLQ 1627
Cdd:COG3206 256 LPELLQSP-VIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQLQQEAQRILASL----EAELEALQAREA 330
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736215636 1628 ShsmsfnvkaskLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQaekeLETWRQKANEA 1689
Cdd:COG3206 331 S-----------LQAQLAQLEARLAELPELEAELRRLEREVEVAREL----YESLLQRLEEA 377
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1566-1978 |
5.67e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 46.19 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1566 KRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMK-QAEEEKLRQIKVVEEVAQKSAATQLQSHSMSFNVKASKLEESL 1644
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKeEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1645 KKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALR-----LRLQAEEE---AQKKSKTQEEAERQKVE 1716
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRkaeeeAKRKAEEErkaAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1717 AERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEK 1796
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1797 QRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQR 1876
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1877 AEAEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSSDSEMVR 1956
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGL 400
|
410 420
....*....|....*....|..
gi 736215636 1957 QKTIVEETLRQKKIVEEEIHII 1978
Cdd:COG3064 401 LGLRLDLGAALLEAASAVELRV 422
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1465-1620 |
5.67e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 46.15 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1465 NIQHELHHLKSLSEQEIKSKSQQLEhalvshtkieEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDA 1544
Cdd:pfam05262 195 NFRRDMTDLKERESQEDAKRAQQLK----------EELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1545 E----RLRKQVAEEtqKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKfkmQAEEAERRMKQAEEEKLRQIKVVEEVAQK 1620
Cdd:pfam05262 265 DtsspKEDKQVAEN--QKREIEKAQIEIKKNDEEALKAKDHKAFDLKQ---ESKASEKEAEDKELEAQKKREPVAEDLQK 339
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
2155-2603 |
5.68e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.61 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2155 KQKKSAEEEAAKQAKAQKdaeKLKKAAEEEASKRAaaeaEALKQKKQADAEMAKH-KKEADQALKLKSQVEKELTMVKLR 2233
Cdd:COG5022 813 RSYLACIIKLQKTIKREK---KLRETEEVEFSLKA----EVLIQKFGRSLKAKKRfSLLKKETIYLQSAQRVELAERQLQ 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2234 -LDETDK---QKALLDEELQRVKGEVNdavkqKAQVEDELAKVRIQMDELLKLK---LKIEEQNRSLMKKDKDKTQKVLA 2306
Cdd:COG5022 886 eLKIDVKsisSLKLVNLELESEIIELK-----KSLSSDLIENLEFKTELIARLKkllNNIDLEEGPSIEYVKLPELNKLH 960
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2307 EEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMqAIQEATKLKAEAQELQKQKDQAQEKAKKLL 2386
Cdd:COG5022 961 EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYG-ALQESTKQLKELPVEVAELQSASKIISSES 1039
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2387 EDKQQiQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSkAENEAKKFKkqADEAKARLKDTEKQSTET 2466
Cdd:COG5022 1040 TELSI-LKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLES-TENLLKTIN--VKDLEVTNRNLVKPANVL 1115
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2467 VVQKLETQRLQSTREADG-LKEAIADLEKEREKLKKEAEELQNKSNKMANTQKEEIEQQKAIIQKSFISERELLLK---- 2541
Cdd:COG5022 1116 QFIVAQMIKLNLLQEISKfLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKskls 1195
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736215636 2542 --RQKAVEDEKKKLQKQFEDEVKKAEALKDEQeRQRKLMEEEKKKLQAIMDAAVKKQKEAEADM 2603
Cdd:COG5022 1196 ssEVNDLKNELIALFSKIFSGWPRGDKLKKLI-SEGWVPTEYSTSLKGFNNLNKKFDTPASMSN 1258
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1601-1976 |
5.78e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1601 KQAEEEKLRQIKVVEEVAQKSAA-----TQLQSHSMSFN--VKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKARE 1673
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAesdleQDYQAASDHLNlvQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1674 QAEKELEtwrQKANEALRLRLQ------AEEEAQKKSKtqeeAERQKVEAERDAKKRAKAEDAALkqkDNAEKELEKQRT 1747
Cdd:PRK04863 380 ENEARAE---AAEEEVDELKSQladyqqALDVQQTRAI----QYQQAVQALERAKQLCGLPDLTA---DNAEDWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1748 FAEQVAQQKLSAEQeciRLKADFDHAEQQRGLLdNELQRLKKEVSATEKQR--KLLEEELAKVRSEMDSLLKMktEAEKK 1825
Cdd:PRK04863 450 KEQEATEELLSLEQ---KLSVAQAAHSQFEQAY-QLVRKIAGEVSRSEAWDvaRELLRRLREQRHLAEQLQQL--RMRLS 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1826 TMsnteksKQLLESEAlkmkqladEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALK 1905
Cdd:PRK04863 524 EL------EQRLRQQQ--------RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLE 589
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736215636 1906 AKEAENERLKRKA-EDEAYQRKL--LEDQAAQHKHDIQEKIIHLKSSSDSEmvRQKTIVEETLR-QKKIVEEEIH 1976
Cdd:PRK04863 590 QLQARIQRLAARApAWLAAQDALarLREQSGEEFEDSQDVTEYMQQLLERE--RELTVERDELAaRKQALDEEIE 662
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1410-1992 |
6.08e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1410 MAEIQAELDKQ--KQIAEAQAKSvikAEQEAQELKLKMK---EEASKRQDVAVDAEQQKQNIQHELHHLKSLSeQEIKSk 1484
Cdd:PRK04863 399 LADYQQALDVQqtRAIQYQQAVQ---ALERAKQLCGLPDltaDNAEDWLEEFQAKEQEATEELLSLEQKLSVA-QAAHS- 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1485 sqQLEHALVSHTKIEEEI------HTIRIQLEMTIKQKKTAESeLQQLRDKAAEAEKlRKAAQEDAERLRKQVAEETQKK 1558
Cdd:PRK04863 474 --QFEQAYQLVRKIAGEVsrseawDVARELLRRLREQRHLAEQ-LQQLRMRLSELEQ-RLRQQQRAERLLAEFCKRLGKN 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1559 KNAEDELkrksEAEKEAAKQKQKALDDlqkfkMQAEEAERRMK-QAEEEKLRQ-IKVVEEVAQK-----SAATQLQSHSm 1631
Cdd:PRK04863 550 LDDEDEL----EQLQEELEARLESLSE-----SVSEARERRMAlRQQLEQLQArIQRLAARAPAwlaaqDALARLREQS- 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1632 sfnvkasklEESLKKEQGTVLQLQEEAEQLRKQQEEANK---AREQAEKELETWRQK-ANEALRLRLQAE---------- 1697
Cdd:PRK04863 620 ---------GEEFEDSQDVTEYMQQLLERERELTVERDElaaRKQALDEEIERLSQPgGSEDPRLNALAErfggvllsei 690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1698 ----------------------------EEAQKKSKTQEEAE------RQKVEAERDAKKRAKAEDAALKQKDNA----- 1738
Cdd:PRK04863 691 yddvsledapyfsalygparhaivvpdlSDAAEQLAGLEDCPedlyliEGDPDSFDDSVFSVEELEKAVVVKIADrqwry 770
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1739 --------------EKELEKQRTFAEQVAQQ--KLSAE-QECIRLKADFDH--------------------AEQQRGLLD 1781
Cdd:PRK04863 771 srfpevplfgraarEKRIEQLRAEREELAERyaTLSFDvQKLQRLHQAFSRfigshlavafeadpeaelrqLNRRRVELE 850
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1782 NELQRL-KKEVSATEKQRKL---------------------LEEELAKVRSEMDSLLkmktEAEK------KTMSNTEKS 1833
Cdd:PRK04863 851 RALADHeSQEQQQRSQLEQAkeglsalnrllprlnlladetLADRVEEIREQLDEAE----EAKRfvqqhgNALAQLEPI 926
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1834 KQLLES-----EALKM------KQLADEATRLRSVAE------------------------EAKKQRQtaeEEAARQRAE 1878
Cdd:PRK04863 927 VSVLQSdpeqfEQLKQdyqqaqQTQRDAKQQAFALTEvvqrrahfsyedaaemlaknsdlnEKLRQRL---EQAEQERTR 1003
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1879 AEKILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAYQRKL-LEDQAAQHKHDIQEKiIHLKSSSDSEMVRQ 1957
Cdd:PRK04863 1004 AREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSgAEERARARRDELHAR-LSANRSRRNQLEKQ 1082
|
730 740 750
....*....|....*....|....*....|....*....
gi 736215636 1958 KTIVEETLR--QKKI--VEEEIHIIRINFEKASKGKSDL 1992
Cdd:PRK04863 1083 LTFCEAEMDnlTKKLrkLERDYHEMREQVVNAKAGWCAV 1121
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1556-1670 |
6.32e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 42.63 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1556 QKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERR-----MKQAEE-EKLRQIKvvEEVAQ-KSAATQLQS 1628
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNyerelVLHAEDiKALQALR--EELNElKAEIAELKA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 736215636 1629 HSMSFNVKASKLEESLKKEQGtvlQLQEEAEQLRKQQEEANK 1670
Cdd:pfam07926 79 EAESAKAELEESEESWEEQKK---ELEKELSELEKRIEDLNE 117
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2156-2448 |
6.65e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.22 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2156 QKKSAEEEAAKQAKAQKDAEKlkkaAEEEASKRAAAEAEALKQKKQAdaemakhkkEADQALKLKSQVEKEltmvklrld 2235
Cdd:TIGR02794 44 DPGAVAQQANRIQQQKKPAAK----KEQERQKKLEQQAEEAEKQRAA---------EQARQKELEQRAAAE--------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2236 etdkqkalldeelqrvkgevndavkQKAQVEDELAKVriqmdellklklKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSL 2315
Cdd:TIGR02794 102 -------------------------KAAKQAEQAAKQ------------AEEKQKQAEEAKAKQAAEAKAKAEAEAERKA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2316 AEEAARlsvEAEETARQRQIAESnlAEQRALAEKMLKEKMQAIQEAtKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQR 2395
Cdd:TIGR02794 145 KEEAAK---QAEEEAKAKAAAEA--KKKAEEAKKKAEAEAKAKAEA-EAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAA 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 736215636 2396 LDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQ 2448
Cdd:TIGR02794 219 AAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA 271
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1765-1919 |
7.17e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1765 RLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLlkmkteaeKKTMSNTEKSKQLlesEALkM 1844
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY--------EEQLGNVRNNKEY---EAL-Q 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736215636 1845 KQLaDEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEatrLRTEAEIALKAKEAENERLKRKAE 1919
Cdd:COG1579 96 KEI-ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAERE 166
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3071-3108 |
7.19e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 40.00 E-value: 7.19e-04
10 20 30
....*....|....*....|....*....|....*...
gi 736215636 3071 LQGTPSIGGLLYEPTKEKMPFYQAMKKELLSPETVANL 3108
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1493-1621 |
7.19e-04 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 44.98 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1493 VSHTKIEEEIHTIRIQLEMTIKQKKTAEsELQQLRDKAAEAEklRKAAQEDAERLRkQVAEETQKKKNAEDE-LKRKSEA 1571
Cdd:cd03406 155 VTKPKIPEAIRRNYEAMEAEKTKLLIAE-QHQKVVEKEAETE--RKRAVIEAEKDA-EVAKIQMQQKIMEKEaEKKISEI 230
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 736215636 1572 EKEAAKQKQKALDDLQKFKMqaeeaerrMKQAEEEKLR------QIKVVEEVAQKS 1621
Cdd:cd03406 231 EDEMHLAREKARADAEYYRA--------LREAEANKLKltpeylELKKYQAIANNT 278
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1654-1750 |
7.42e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.42 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1654 LQEEAEQLRKQQEEANKAREQAEKELEtwrqKANEALRlrlQAEEEAQK-KSKTQEEAERQKveaeRDAKKRAKAEDAAL 1732
Cdd:cd06503 28 LDEREEKIAESLEEAEKAKEEAEELLA----EYEEKLA---EARAEAQEiIEEARKEAEKIK----EEILAEAKEEAERI 96
|
90
....*....|....*...
gi 736215636 1733 KQKDNAEKELEKQRTFAE 1750
Cdd:cd06503 97 LEQAKAEIEQEKEKALAE 114
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1508-1934 |
7.85e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 45.67 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1508 QLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQkkknaedeLKRKSEAEKEAAKQKQKALDDLQ 1587
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLL--------LLALALAALLLAAAALLLLLLAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1588 KFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEE 1667
Cdd:COG5278 183 AALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAAL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1668 ANKAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRT 1747
Cdd:COG5278 263 LAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAA 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1748 FAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTM 1827
Cdd:COG5278 343 ALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEAL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1828 SNTEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAK 1907
Cdd:COG5278 423 ELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLA 502
|
410 420
....*....|....*....|....*..
gi 736215636 1908 EAENERLKRKAEDEAYQRKLLEDQAAQ 1934
Cdd:COG5278 503 LALAALLLAAAEAALAAALAAALASAE 529
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
57-154 |
8.12e-04 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 42.65 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 57 QKKTFTKWVN---------KHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 123
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 736215636 124 KHRQVKLVNIRNDDIADGNPKLTLGLIWTII 154
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2541-2653 |
8.13e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.47 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2541 KRQKAVEDEKKKLQKQFEDEVKKAEALKD-------EQERQRKLMEEEKKKLQAIMDAAVKK--QKEAEA-DMKNKQTEM 2610
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEakelllrERNQQRQEARREREELQREEERLVQKeeQLDARAeKLDNLENQL 107
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 736215636 2611 EVLEKKRLDQEKQLGAENQKLREKLQCLEGASKQSATKQVASK 2653
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKL 150
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1757-1925 |
8.58e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 45.63 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1757 LSAEQECIRLKADFDH-AEQQRGLLDNELQRLKKE--VSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKS 1833
Cdd:PRK00106 38 LNAEQEAVNLRGKAERdAEHIKKTAKRESKALKKEllLEAKEEARKYREEIEQEFKSERQELKQIESRLTERATSLDRKD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1834 KQLLESEAL---KMKQLADEA----TRLRSVAEEAKKQRQTAEEEAARQRAEAEKIlkeklaaINEATRLRTEAEIALKA 1906
Cdd:PRK00106 118 ENLSSKEKTlesKEQSLTDKSkhidEREEQVEKLEEQKKAELERVAALSQAEAREI-------ILAETENKLTHEIATRI 190
|
170 180
....*....|....*....|....*
gi 736215636 1907 KEAENE---RLKRKAED---EAYQR 1925
Cdd:PRK00106 191 REAEREvkdRSDKMAKDllaQAMQR 215
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3439-3472 |
8.65e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 8.65e-04
10 20 30
....*....|....*....|....*....|....
gi 736215636 3439 LLEAQAGTGFITDPVKNQKYSVDDAVKVGVVGPE 3472
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
2197-2416 |
8.74e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 45.05 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2197 KQKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDelaKVRIQM 2276
Cdd:pfam15742 6 KLKYQQQEEVQQLRQNLQRLQILCTSAEKELRYERGKNLDLKQHNSLLQEENIKIKAELKQAQQKLLDSTK---MCSSLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2277 DELLKLKLKIEEQNRSLMKKDKD-KTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQiaESNLAEQRALAEKMLKEKM 2355
Cdd:pfam15742 83 AEWKHCQQKIRELELEVLKQAQSiKSQNSLQEKLAQEKSRVADAEEKILELQQKLEHAH--KVCLTDTCILEKKQLEERI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736215636 2356 -QAIQEATKLKAEAQE--------------LQKQKDQAQEKAKKLLEDKQQIQQRLdKETEGFQKSLEAERKRQLE 2416
Cdd:pfam15742 161 kEASENEAKLKQQYQEeqqkrklldqnvneLQQQVRSLQDKEAQLEMTNSQQQLRI-QQQEAQLKQLENEKRKSDE 235
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
1435-1743 |
8.81e-04 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 45.44 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1435 EQEAQELKLKMKEEASKRQDVAVDAE-QQKQNIQHELHHLKSLSEQEIKSKSQQLEHAlvSHTKIEEEihtiRIQLEMTI 1513
Cdd:pfam04747 62 EQPQQVEKVKKSEKKKAQKQIAKDHEaEQKVNAKKAAEKEARRAEAEAKKRAAQEEEH--KQWKAEQE----RIQKEQEK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1514 KQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAED-------ELKRKSEAEKEAAKQKQKALDDL 1586
Cdd:pfam04747 136 KEADLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDrsaapapEPKTPTNTPAEPAEQVQEITGKK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1587 QKFKMQAEEAERRMKQAE-EEKLRQIKVVEEVAQKSAATQLQSHSMsfNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQ 1665
Cdd:pfam04747 216 NKKNKKKSESEATAAPASvEQVVEQPKVVTEEPHQQAAPQEKKNKK--NKRKSESENVPAASETPVEPVVETTPPASENQ 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 1666 EEANKAREQAEKEletwrqkanEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELE 1743
Cdd:pfam04747 294 KKNKKDKKKSESE---------KVVEEPVQAEAPKSKKPTADDNMDFLDFVTAKEEPKDEPAETPAAPVEEVVENVVE 362
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1169-1608 |
8.98e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1169 NEKEVEEQRSQLKSMRAEVEAdqviFDRLQDELRRASTINDKMTRIHSERDAEMEHYRQLVS--SLLERWQVVFAQMDMR 1246
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1247 QRELDLLGRHMNSYNVSYEWLIHWLGEARKRQEKIQAVPIGGSKALREQLAEEKKLLEEIEKNKDKIDSCQKNAKAYIDS 1326
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1327 VKDyELQILTYKALQDPMASPLKKPKMD-------CASDNIIQEYVTLRTRYSELMTLTSQYIKFITETQRRLEDDEKAS 1399
Cdd:COG4717 225 LEE-ELEQLENELEAAALEERLKEARLLlliaaalLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1400 EKLKEEERKKMAEIQAELDKQKQ----IAEAQAKSVIKAEQEAQELKLKMKEEASKRQDVAVdaEQQKQNIQHELHHLKS 1475
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAalglPPDLSPEELLELLDRIEELQELLREAEELEEELQL--EELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1476 LSEQEIKSKSQQLEHAlvshTKIEEEIHTIRIQLEMTIK--QKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAE 1553
Cdd:COG4717 382 EDEEELRAALEQAEEY----QELKEELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEELEEELEELREELAE 457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 1554 ETQKKKNAE--DELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKL 1608
Cdd:COG4717 458 LEAELEQLEedGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2278-2611 |
9.59e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2278 ELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEetaRQRQIAESNLAEQRALAEKMLKEKMQA 2357
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELE---SRVAELKEELRQSREKHEELEEKYKEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2358 IQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQR-LDKETE-----------GFQKSLEAERKRQLEV---SAEAE 2422
Cdd:pfam07888 107 SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRvLERETElermkerakkaGAQRKEEEAERKQLQAklqQTEEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2423 TLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTETVVQKLETQrLQSTRE--------ADGLKEAIADLEK 2494
Cdd:pfam07888 187 LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEE-LRSLQErlnaserkVEGLGEELSSMAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2495 EREKLKKEAEELQNKSNKMaNTQKEEIEQQKAIIQKSFISERELLlkrQKAVEDEKKKLQKQFEDEVKKAEALKDEQERQ 2574
Cdd:pfam07888 266 QRDRTQAELHQARLQAAQL-TLQLADASLALREGRARWAQERETL---QQSAEADKDRIEKLSAELQRLEERLQEERMER 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 736215636 2575 RKL--------------MEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEME 2611
Cdd:pfam07888 342 EKLevelgrekdcnrvqLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1651-1754 |
1.02e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1651 VLQLQEEAEQLRKQQEEANKAR-EQAEKELETWRQKANEalrlrLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAED 1729
Cdd:COG0542 420 LEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEA-----LKARWEAEKELIEEIQELKEELEQRYGKIPELEKEL 494
|
90 100
....*....|....*....|....*
gi 736215636 1730 AALKQKDNAEKELEKQRTFAEQVAQ 1754
Cdd:COG0542 495 AELEEELAELAPLLREEVTEEDIAE 519
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2174-2603 |
1.04e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.03 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2174 AEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKG 2253
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2254 EVNDAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQR 2333
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2334 QIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKR 2413
Cdd:COG3064 162 AAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2414 QLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTETVVQKLETQRLQSTREADGlkEAIADLE 2493
Cdd:COG3064 242 EAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVA--AEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2494 KEREKLKKEAEELQNKSNKMANTQKEEIEQQKAIIQKSFISERELLLKRQKAVEDEKKKLQKQFEDEVKKAEALKDEQER 2573
Cdd:COG3064 320 AAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
410 420 430
....*....|....*....|....*....|
gi 736215636 2574 QRKLMEEEKKKLQAIMDAAVKKQKEAEADM 2603
Cdd:COG3064 400 LLGLRLDLGAALLEAASAVELRVLLALAGA 429
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2781-2814 |
1.05e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.05e-03
10 20 30
....*....|....*....|....*....|....
gi 736215636 2781 LLEAQAASGYIVDPVKNKLLSVDEAVKCELIGPE 2814
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2855-2891 |
1.05e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.05e-03
10 20 30
....*....|....*....|....*....|....*..
gi 736215636 2855 TKFLDVQLATGGIVDPINSHRVQLQTAYKQGQFDADM 2891
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1788-1918 |
1.08e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.39 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1788 KKEVSATEKQRKLLEEElAKVRSEmdsLLKMKTEAEkktmsNTEKSKQLLESEAlkmKQLADEATRlRSVAE-----EAK 1862
Cdd:PTZ00491 662 KSQEAAARHQAELLEQE-ARGRLE---RQKMHDKAK-----AEEQRTKLLELQA---ESAAVESSG-QSRAEalaeaEAR 728
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 736215636 1863 KQRQTAEEEAARQRAEAEKILKEklaAINEATRLRTEAEIALKAKEAENERLKRKA 1918
Cdd:PTZ00491 729 LIEAEAEVEQAELRAKALRIEAE---AELEKLRKRQELELEYEQAQNELEIAKAKE 781
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1561-1776 |
1.08e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.60 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1561 AEDELKRKSEAEKEAAKQ---KQKALDDlqkfKMQAEEAERRMKQAEEEKLRQI----KVVEEVAQKSAATQLQSHSMSF 1633
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQddaAQNALAD----KERAEADRQRLEQEKQQQLAAIsgsqSQLESTDQNALETNGQAQRDAI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1634 NVKASKLEESLKKEQGTVLQLQEEA-------EQLRKQ---------QEEANKAREQAEKELETWRQKANEalrlRLQAE 1697
Cdd:NF012221 1612 LEESRAVTKELTTLAQGLDALDSQAtyagesgDQWRNPfagglldrvQEQLDDAKKISGKQLADAKQRHVD----NQQKV 1687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1698 EEAQKKSKT-QEEAERQKVEAER-------DAKKRakaEDAALKQKDNAEKELEKQRTFAEQvAQQKLSAEQECIRLKAD 1769
Cdd:NF012221 1688 KDAVAKSEAgVAQGEQNQANAEQdiddakaDAEKR---KDDALAKQNEAQQAESDANAAAND-AQSRGEQDASAAENKAN 1763
|
....*..
gi 736215636 1770 FDHAEQQ 1776
Cdd:NF012221 1764 QAQADAK 1770
|
|
| PRK13428 |
PRK13428 |
F0F1 ATP synthase subunit delta; Provisional |
2146-2348 |
1.12e-03 |
|
F0F1 ATP synthase subunit delta; Provisional
Pssm-ID: 184048 [Multi-domain] Cd Length: 445 Bit Score: 45.11 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2146 LRQKAAE-AEKQKKSAEEEAAkQAKAQKDAeklkKAAEEEASKRAAAEAEALKQ--KKQADAEMAKHKKEADQALKL-KS 2221
Cdd:PRK13428 37 VRQQLAEsATAADRLAEADQA-HTKAVEDA----KAEAARVVEEAREDAERIAEqlRAQADAEAERIKVQGARQVQLlRA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2222 QVEKELtmvKLRLDETDKQKAlldEELqrVKGEVNDAVKQKAQVEDELakvriqmDELLKLKLKIEEQNRSLMKKDKDKT 2301
Cdd:PRK13428 112 QLTRQL---RLELGHESVRQA---GEL--VRNHVADPAQQSATVDRFL-------DELDAMAPSTADVDYPLLAKMRSAS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 736215636 2302 QKVLAEEAGKMKSLAE--EAARLSVEAEETARQRQIAESNLAEQRALAE 2348
Cdd:PRK13428 177 RRALASLVDRFDSVAAdlDNQALTTLADELVSVAKLLDREPVLTKHLTE 225
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2507-2630 |
1.14e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2507 QNKSNKMANTQKEEIEQQKAIIQ---KSFISERELLLKRQKAVEDEKKKL---QKQFEDEVKK-AEALKDEQERQRKLME 2579
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQKQAAEQerlKQLEKERLAAQEQKKQAEEAAKQAalkQKQAEEAAAKaAAAAKAKAEAEAKRAA 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 736215636 2580 EEKKKLQAIMD--AAVKKQKEAEADMKnKQTEMEVLEKKRLDQEKQLGAENQK 2630
Cdd:PRK09510 158 AAAKKAAAEAKkkAEAEAAKKAAAEAK-KKAEAEAAAKAAAEAKKKAEAEAKK 209
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2325-2633 |
1.17e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2325 EAEETARQRqiaesnlaEQRALAEKM-LKEKMQAIQEAT-KLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEG 2402
Cdd:pfam02029 3 DEEEAARER--------RRRAREERRrQKEEEEPSGQVTeSVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2403 FQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKqsteTVVQKLETQRLQSTREA 2482
Cdd:pfam02029 75 RQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEET----EIREKEYQENKWSTEVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2483 DGLKEAIADLEKEREKLKKEAEELQNKSNKMANTQKEE--------IEQQKAIIQKSFISERELLLKRQKAVEDEKK--- 2551
Cdd:pfam02029 151 QAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKkvkyeskvFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQggl 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2552 ---KLQKQFEDEVKKAEALKDEQERQR-KLMEEEKKKLQaimdaavKKQKEAEAdmknkqtEMEVLEKKRLDQEKQLGAE 2627
Cdd:pfam02029 231 sqsQEREEEAEVFLEAEQKLEELRRRRqEKESEEFEKLR-------QKQQEAEL-------ELEELKKKREERRKLLEEE 296
|
....*.
gi 736215636 2628 NQKLRE 2633
Cdd:pfam02029 297 EQRRKQ 302
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
110-154 |
1.21e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 41.66 E-value: 1.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 736215636 110 FHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 154
Cdd:cd21294 78 FQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2150-2382 |
1.25e-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: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2150 AAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADqalKLKSQVEKELTM 2229
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2230 VKLR--------------------------LDETDKQKALLD---EELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELL 2280
Cdd:COG3883 88 LGERaralyrsggsvsyldvllgsesfsdfLDRLSALSKIADadaDLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2281 KLKLKIEEQnrslmkkdKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQE 2360
Cdd:COG3883 168 AAKAELEAQ--------QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260
....*....|....*....|..
gi 736215636 2361 ATKLKAEAQELQKQKDQAQEKA 2382
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGS 261
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
57-154 |
1.28e-03 |
|
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409142 Cd Length: 116 Bit Score: 41.74 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 57 QKKTFTKWVNKHLMKS---------QRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 122
Cdd:cd21293 2 EKGSYVDHINRYLGDDpflkqflpiDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 736215636 123 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 154
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| I-BAR_IMD |
cd07605 |
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ... |
2512-2615 |
1.28e-03 |
|
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module that binds and bends membranes; Inverse (I)-BAR (or IMD) is a member of the Bin/Amphiphysin/Rvs (BAR) domain family. It is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. IMD domains are found in Insulin Receptor tyrosine kinase Substrate p53 (IRSp53), Missing in Metastasis (MIM), and Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-like (BAIAP2L) proteins. These are multi-domain proteins that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. Most members contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus, exccept for MIM which does not carry an SH3 domain. Some members contain additional domains and motifs. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.
Pssm-ID: 153289 [Multi-domain] Cd Length: 223 Bit Score: 43.51 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2512 KMANTQKEeIEQQKAIIQKSFISEreLLLKRQKAVEDEKK---KLQKQFEDEVK-KAEALKDEQERQRKLmeeEKKKLQA 2587
Cdd:cd07605 72 QIVDTHKS-IEASLEQVAKAFHGE--LILPLEKKLELDQKvinKFEKDYKKEYKqKREDLDKARSELKKL---QKKSQKS 145
|
90 100
....*....|....*....|....*...
gi 736215636 2588 IMDAAVKKQKEAEADMKNKQTEMEVLEK 2615
Cdd:cd07605 146 GTGKYQEKLDQALEELNDKQKELEAFVS 173
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
50-158 |
1.30e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 41.90 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 50 ADERDRVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLKH 125
Cdd:cd21337 14 APDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQD 93
|
90 100 110
....*....|....*....|....*....|...
gi 736215636 126 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 158
Cdd:cd21337 94 GGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2170-2454 |
1.30e-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: 44.52 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2170 AQKDAEKLKKAAEEEASKRAAAEAEALKQK---KQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDE 2246
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERRLDEMMEEERERaleEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2247 ELQRVKgevndavkqkaqvEDELAKVRIQMDELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEA 2326
Cdd:pfam13868 106 IVERIQ-------------EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEERE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2327 EETARQRQIAESNLAEQRALAEKMLKEKmQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKS 2406
Cdd:pfam13868 173 AEREEIEEEKEREIARLRAQQEKAQDEK-AERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERR 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 736215636 2407 LEAERKRqlevsAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKA 2454
Cdd:pfam13868 252 LAEEAER-----EEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRE 294
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2350-2635 |
1.32e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2350 MLkEKMQAIQEATKLKAEAQEL---QKQKDQAQEKAKkLLEDKQQIQQRLDKETEgfqkslEAERKRQLEVSAEAETLRL 2426
Cdd:COG4913 217 ML-EEPDTFEAADALVEHFDDLeraHEALEDAREQIE-LLEPIRELAERYAAARE------RLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2427 KVKELSDAQSKAENEAKKFKKQADEAKARLKDTEkqstetvvqkletqrlqstREADGLKEAIADLekereklkkeaeel 2506
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALR-------------------EELDELEAQIRGN-------------- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2507 qnksnkmANTQKEEIEQQKAIIQKsfisERELLLKRQKAVEDEKKKLQKQFEDEVKKAEALKDEQERQRKLMEEEKKKLQ 2586
Cdd:COG4913 336 -------GGDRLEQLEREIERLER----ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE 404
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 736215636 2587 AIMDAAVKKQKEAEADMKNKQTEMEVLEKKRLDqekqLGAENQKLREKL 2635
Cdd:COG4913 405 EALAEAEAALRDLRRELRELEAEIASLERRKSN----IPARLLALRDAL 449
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2172-2397 |
1.33e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.21 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2172 KDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKELtmvklrlDETDKQKALLDEELQRv 2251
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQL-------ESTDQNALETNGQAQR- 1608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2252 kgevnDAVKQKAQ-VEDELAKVRIQMDEL-------------------LKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGK 2311
Cdd:NF012221 1609 -----DAILEESRaVTKELTTLAQGLDALdsqatyagesgdqwrnpfaGGLLDRVQEQLDDAKKISGKQLADAKQRHVDN 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2312 MKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLK----AEAQELQKQKDQ----AQEKAK 2383
Cdd:NF012221 1684 QQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAEsdanAAANDAQSRGEQdasaAENKAN 1763
|
250
....*....|....
gi 736215636 2384 KLLEDKQQIQQRLD 2397
Cdd:NF012221 1764 QAQADAKGAKQDES 1777
|
|
| PRK05901 |
PRK05901 |
RNA polymerase sigma factor; Provisional |
2005-2201 |
1.40e-03 |
|
RNA polymerase sigma factor; Provisional
Pssm-ID: 235640 [Multi-domain] Cd Length: 509 Bit Score: 44.60 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2005 ETQKSKLKAEAEAE-KLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEkq 2083
Cdd:PRK05901 4 ASTKAELAAEEEAKkKLKKLAAKSKSKGFITKEEIKEALESKKKTPEQIDQVLIFLSGMVKDTDDATESDIPKKKTKT-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2084 viVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEE 2163
Cdd:PRK05901 82 --AAKAAAAKAPAKKKLKDELDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDDDDDDDDDLDDDDIDDDDDDEDDDED 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 736215636 2164 AAKQAKAQKDAEKLKKAAEEEASKRAA-----AEAEALKQKKQ 2201
Cdd:PRK05901 160 DDDDDVDDEDEEKKEAKELEKLSDDDDfvwdeDDSEALRQARK 202
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
161-274 |
1.48e-03 |
|
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: 41.33 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 161 DIQVNGQSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQ-ENLEQAFSVA 239
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPvTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|....*
gi 736215636 240 ERDLGVTRLLDPEDVDVLHPDEKSIITYVSSLYDA 274
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3515-3543 |
1.49e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.49e-03
10 20
....*....|....*....|....*....
gi 736215636 3515 LLEAQFSTGGIIDPVSSHRVPNDVAIQRG 3543
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRG 31
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2087-2444 |
1.50e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.65 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2087 AKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKrlAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAK 2166
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAE--EERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2167 QAKAQKDAEKLKKAAEEEASKRAA-AEAEALKQKKQADAEMAKH---KKEADQALKLKSQVEKeltmvKLRLDETDKQKA 2242
Cdd:COG3064 79 LAEAEKAAAEAEKKAAAEKAKAAKeAEAAAAAEKAAAAAEKEKAeeaKRKAEEEAKRKAEEER-----KAAEAEAAAKAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2243 LLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARL 2322
Cdd:COG3064 154 AEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2323 SVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEG 2402
Cdd:COG3064 234 LAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAA 313
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 736215636 2403 FQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKK 2444
Cdd:COG3064 314 EEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGA 355
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
1992-2216 |
1.52e-03 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 44.98 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1992 LENELKKLKVIAEETQKSKLKAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAArqcKAAQEEVArlekkADEANK 2071
Cdd:PRK14900 865 LQNPSFVQNAPPAVVEKDRARAEELREKRGKLEAHRAMLSGSEANSARRDTMEIQNEQ---KPTQDGPA-----AEAQPA 936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2072 QKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSKnkedslaqqkmkEEFENAKRLAQaaekakekaekeaallRQKAA 2151
Cdd:PRK14900 937 QENTVVESAEKAVAAVSEAAQQAATAVASGIEKVAE------------AVRKTVRRSVK----------------KAAAT 988
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736215636 2152 EAEKQKKSAEEEAAKQAKAQKDAEKlKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQA 2216
Cdd:PRK14900 989 RAAMKKKVAKKAPAKKAAAKKAAAK-KAAAKKKVAKKAPAKKVARKPAAKKAAKKPARKAAGRKA 1052
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1639-1833 |
1.62e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.61 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1639 KLEESLKKEQGTVLQLQEEAEQLRKQQ-EEANKAREQAEKELEtwrQKANEAlrlrlqaEEEAQKKSKTQEEAERQKVEA 1717
Cdd:pfam05262 181 KVVEALREDNEKGVNFRRDMTDLKEREsQEDAKRAQQLKEELD---KKQIDA-------DKAQQKADFAQDNADKQRDEV 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1718 ERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKlsAEQECIRLKADFDHAEQQrglldnelqrLKKEVSATEKQ 1797
Cdd:pfam05262 251 RQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIE--IKKNDEEALKAKDHKAFD----------LKQESKASEKE 318
|
170 180 190
....*....|....*....|....*....|....*..
gi 736215636 1798 RKLLEEELAKVRSEMDS-LLKMKTEAEKKTMSNTEKS 1833
Cdd:pfam05262 319 AEDKELEAQKKREPVAEdLQKTKPQVEAQPTSLNEDA 355
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2341-2615 |
1.66e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2341 AEQRALAEKMLKEKMQAIQEATklkaeaqeLQKQKDQAQEKAKKLLEDKQQIQQRLDKetegFQKSLEAERKRQLEVSAE 2420
Cdd:COG3206 144 SPDPELAAAVANALAEAYLEQN--------LELRREEARKALEFLEEQLPELRKELEE----AEAALEEFRQKNGLVDLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2421 AETLRL--KVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTE----TVVQKLETQRLQSTREADGLKEaiadlek 2494
Cdd:COG3206 212 EEAKLLlqQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEllqsPVIQQLRAQLAELEAELAELSA------- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2495 ereklkkeaeELQNKSNKMANTQkEEIEQQKAIIQKSFISERELLLKRQKAVEDEKKKLQKQFEDEVKKAEALKDEQERQ 2574
Cdd:COG3206 285 ----------RYTPNHPDVIALR-AQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 736215636 2575 RKLmEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEK 2615
Cdd:COG3206 354 RRL-EREVEVARELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4052-4083 |
1.69e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 1.69e-03
10 20 30
....*....|....*....|....*....|..
gi 736215636 4052 KLLSAERAVTGYKDPYSGKIISLFQAMKKGLI 4083
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1984-2263 |
1.72e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.20 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1984 KASKGKSDLENELKKLKVIAEETQKSKLKAEAEAeklKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLE 2063
Cdd:PRK07735 36 KLEEENREKEKALPKNDDMTIEEAKRRAAAAAKA---KAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2064 KKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEA 2143
Cdd:PRK07735 113 REGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2144 ALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEM--AKHKKEADQALKLKS 2221
Cdd:PRK07735 193 EEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAKTkgAEGKKEEEPKQEEPS 272
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 736215636 2222 QVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKA 2263
Cdd:PRK07735 273 VNQPYLNKYVEVIKEKLGEDVLEDSYINKLSKDVPTLVVEPE 314
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1772-1934 |
1.85e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1772 HAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLA--- 1848
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGera 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1849 --------------------------DEATRLRSVAEEAKK---QRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTE 1899
Cdd:COG3883 93 ralyrsggsvsyldvllgsesfsdflDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190
....*....|....*....|....*....|....*
gi 736215636 1900 AEIALKAKEAENERLKRKAEDEAYQRKLLEDQAAQ 1934
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
52-160 |
1.85e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 41.51 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 52 ERDRVQKKTFTKWVNKhlMKSQRHITDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 122
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 736215636 123 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 160
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2316-2626 |
1.86e-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: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2316 AEEAARLSVEAEETARQRQIAESNLAEQRALAEKM--LKEKMQAIQEATKLKAEAQelQKQKDQAQEKAKKLLE-DKQQI 2392
Cdd:COG3064 10 AEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLaeLEAKRQAEEEAREAKAEAE--QRAAELAAEAAKKLAEaEKAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2393 QQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTETVVQKLE 2472
Cdd:COG3064 88 EAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2473 TQRLQSTREADGLKEAIADLEKEREKLKKEAEELQNKSNKMANTQKEEIEQQKAIIQKSFISERELLLKRQKAVEDEKKK 2552
Cdd:COG3064 168 AAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGG 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736215636 2553 LQKQFEDEVKKAEALKDEQERQRKLMEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEKKRLDQEKQLGA 2626
Cdd:COG3064 248 AEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAA 321
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
192-273 |
1.92e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 41.13 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 192 RCDNFTTGWRDGKLFNAIIHKHRPTLIDMGKVYRQSNQENLEQ-AFSVAE--RDLGVTRLLDPEdvDVLHPDEKSIITYV 268
Cdd:cd21218 32 RVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKrAEKVLQaaEKLGCKYFLTPE--DIVSGNPRLNLAFV 109
|
....*
gi 736215636 269 SSLYD 273
Cdd:cd21218 110 ATLFN 114
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1992-2586 |
1.96e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.36 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1992 LENELKKLKviaEETQKSKLKAEAEAEKLKKLAaeeekkrkeseeKVKRITAAEEEAARQCKAAQEEVarlEKKADEANK 2071
Cdd:pfam07111 78 LEEEVRLLR---ETSLQQKMRLEAQAMELDALA------------VAEKAGQAEAEGLRAALAGAEMV---RKNLEEGSQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2072 QKEKAEKEaekqviVAKEAAQKCSSAEQKAQEVLSKNKE---DSLAQQKMKEEFEnAKRLAQAaekakekaekeaallrQ 2148
Cdd:pfam07111 140 RELEEIQR------LHQEQLSSLTQAHEEALSSLTSKAEgleKSLNSLETKRAGE-AKQLAEA----------------Q 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2149 KAAEA-EKQKKSAEEEAAKQAKAqkdAEKLKKAAEEEASKRAAAEAEALKQKKQADAemAKHKKEADQALK-----LKSQ 2222
Cdd:pfam07111 197 KEAELlRKQLSKTQEELEAQVTL---VESLRKYVGEQVPPEVHSQTWELERQELLDT--MQHLQEDRADLQatvelLQVR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2223 VEKELTMVKLRLDE---------------TDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELLKLKLKIE 2287
Cdd:pfam07111 272 VQSLTHMLALQEEEltrkiqpsdslepefPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQS 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2288 EQNRSLMKKDKDKTQKVLAEEAGkMKSLAEEAARlsveAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEA-TKLKA 2366
Cdd:pfam07111 352 QEQAILQRALQDKAAEVEVERMS-AKGLQMELSR----AQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTmTRVEQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2367 EAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQL--EVSAEAETLRLKVKELSdaqskAENEAKK 2444
Cdd:pfam07111 427 AVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVdaDLSLELEQLREERNRLD-----AELQLSA 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2445 FKKQADEAKARLK-DTEKQSTETVVQKLEtQRLQSTREAdglkeaiadlEKEREKLKKEAEELQNKSNKMANTQKEEIEQ 2523
Cdd:pfam07111 502 HLIQQEVGRAREQgEAERQQLSEVAQQLE-QELQRAQES----------LASVGQQLEVARQGQQESTEEAASLRQELTQ 570
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 2524 QKAIIQKSF---ISERELLLKRQkaVEDEKKKLQKQFEDEVKKAEALKDEQER--QRKLMEEEKKKLQ 2586
Cdd:pfam07111 571 QQEIYGQALqekVAEVETRLREQ--LSDTKRRLNEARREQAKAVVSLRQIQHRatQEKERNQELRRLQ 636
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2280-2447 |
2.07e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2280 LKLKLKIEEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQ 2359
Cdd:PRK00409 497 LGLPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2360 EATK-LKAEAQELQK------QKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQL----------------- 2415
Cdd:PRK00409 577 QAIKeAKKEADEIIKelrqlqKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVgdevkylslgqkgevls 656
|
170 180 190
....*....|....*....|....*....|....*..
gi 736215636 2416 -----EVSAEAETLRLKVKeLSDAQSKAENEAKKFKK 2447
Cdd:PRK00409 657 ipddkEAIVQAGIMKMKVP-LSDLEKIQKPKKKKKKK 692
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1372-1696 |
2.12e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.44 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1372 SELMTLTSQYIKFITE---TQRRLEDDEKASEKLKeeerkkmaeiQAELDKQKQIAeAQAKSVIKAEQEAQeLKLkmkEE 1448
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERAEADRQ----------RLEQEKQQQLA-AISGSQSQLESTDQ-NAL---ET 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1449 ASKRQDVAVDAEQqkQNIQHEL----HHLKSLSEQEI---KSKSQQLEHALVS-----HTKIEEEIHTIRIQLEmtiKQK 1516
Cdd:NF012221 1603 NGQAQRDAILEES--RAVTKELttlaQGLDALDSQATyagESGDQWRNPFAGGlldrvQEQLDDAKKISGKQLA---DAK 1677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1517 KTAESELQQLRDKAAEAEklrkAAQEDAERLRKQVAEETQKKKNAEDelKRKSEA---EKEAAKQKQKAlddlqkfKMQA 1593
Cdd:NF012221 1678 QRHVDNQQKVKDAVAKSE----AGVAQGEQNQANAEQDIDDAKADAE--KRKDDAlakQNEAQQAESDA-------NAAA 1744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1594 EEAERRMKQaeeeklrqikvvEEVAQKSAATQLQShsmsfNVKASKLEESLKKEQ---------GTVLQLQEEAEQLRKQ 1664
Cdd:NF012221 1745 NDAQSRGEQ------------DASAAENKANQAQA-----DAKGAKQDESDKPNRqgaagsglsGKAYSVEGVAEPGSHI 1807
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 736215636 1665 QEEANKA---------REQAEKELETWRQKANealRLRLQA 1696
Cdd:NF012221 1808 NPDSPAAadgrfseglTEQEQEALEGATNAVN---RLQINA 1845
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1622-1747 |
2.16e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1622 AATQLQSHSMSFNVKASKLEEsLKKEQGT----VLQLQEEAEQLRKQ-QEEANKAREQAEKELETWRQKANEALRlrlQA 1696
Cdd:PRK00409 507 AKKLIGEDKEKLNELIASLEE-LERELEQkaeeAEALLKEAEKLKEElEEKKEKLQEEEDKLLEEAEKEAQQAIK---EA 582
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 736215636 1697 EEEAQKKSKTQEEAERQKVEA--ERDAKKRAKAEDAALKQKDNAEKELEKQRT 1747
Cdd:PRK00409 583 KKEADEIIKELRQLQKGGYASvkAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1410-1803 |
2.33e-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: 44.35 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1410 MAEIQAELDKQKQIAE-----AQAKSVIKAEQEAQELKLKMKEEAskrQDVAVDAEQQKQNIQHELHHLKSL-------- 1476
Cdd:pfam05557 199 IPELEKELERLREHNKhlnenIENKLLLKEEVEDLKRKLEREEKY---REEAATLELEKEKLEQELQSWVKLaqdtglnl 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1477 -SEQEIKSKSQQLEHALVSHTkieEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEET 1555
Cdd:pfam05557 276 rSPEDLSRRIEQLQQREIVLK---EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1556 QkkknaedelkrkseaEKEAAKQKQKALDDlqkfkmqaeeaERRMKQAEEEKLRQIKVVEEVAQKsaatqLQSHSMSFNV 1635
Cdd:pfam05557 353 K---------------ERDGYRAILESYDK-----------ELTMSNYSPQLLERIEEAEDMTQK-----MQAHNEEMEA 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1636 KASKLEESLK--KEQGTVLqlqEEAEQLRKQQEEANKAREQAEkELETWRQKANEalrLRLQAEEEAQKKSKTQEEAERQ 1713
Cdd:pfam05557 402 QLSVAEEELGgyKQQAQTL---ERELQALRQQESLADPSYSKE-EVDSLRRKLET---LELERQRLREQKNELEMELERR 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1714 KVEAERDAKKRakaedAALKQKDNAEKELEKQRtfAEQVaqQKLSAEQECIR--LKADFDHAEQQRGL-------LDNEL 1784
Cdd:pfam05557 475 CLQGDYDPKKT-----KVLHLSMNPAAEAYQQR--KNQL--EKLQAEIERLKrlLKKLEDDLEQVLRLpettstmNFKEV 545
|
410
....*....|....*....
gi 736215636 1785 QRLKKEVSATEKQRKLLEE 1803
Cdd:pfam05557 546 LDLRKELESAELKNQRLKE 564
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4473-4510 |
2.36e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.36e-03
10 20 30
....*....|....*....|....*....|....*...
gi 736215636 4473 QKLRDVSAYSKYLTCPKTKLKISYKDAMERSMVEEGTG 4510
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2045-2263 |
2.40e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.82 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2045 EEEAARQCK--AAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKEEF 2122
Cdd:PRK07735 11 KKEAARRAKeeARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2123 ENAKRLAQAAEkakekaekeaallRQKAAEAEKQKKSAEEEAAKQAKAqkdaeklkkAAEEEASKRAAAEAEALKQKKQA 2202
Cdd:PRK07735 91 AKAKAKAAAAA-------------KAKAAALAKQKREGTEEVTEEEKA---------AAKAKAAAAAKAKAAALAKQKRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736215636 2203 DAEMAKHKKEADQALKLKSqveKELTMVKLRLDETDKQKALLD-EELQRVKGEVNDAVKQKA 2263
Cdd:PRK07735 149 GTEEVTEEEEETDKEKAKA---KAAAAAKAKAAALAKQKAAEAgEGTEEVTEEEKAKAKAKA 207
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
563-657 |
2.42e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.39 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 563 MRYIQDLLGWVEENQRRVDDGQWGSDLPTVESQLGSHRGLHQSVEEFHSKIQRAKADESQI---SPASKGAYRDYLGKLE 639
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 736215636 640 LQYGKLLNASKARLHSLD 657
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1673-1753 |
2.43e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 41.69 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1673 EQAEKELETWRQKANEALRlrlQAEEEAQKkskTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAE-- 1750
Cdd:PRK05759 48 ERAKKELELAQAKYEAQLA---EARAEAAE---IIEQAKKRAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREElr 121
|
....
gi 736215636 1751 -QVA 1753
Cdd:PRK05759 122 kQVA 125
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2151-2218 |
2.43e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 41.69 E-value: 2.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 2151 AEAEKQKKSAE------EEAAKQAKAQ-----KDAEKLKKAAEEEAskRAAAEAEALKQKKQADAEMAKHKKEADQALK 2218
Cdd:PRK05759 45 AAAERAKKELElaqakyEAQLAEARAEaaeiiEQAKKRAAQIIEEA--KAEAEAEAARIKAQAQAEIEQERKRAREELR 121
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
59-151 |
2.55e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 44.16 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 59 KTFTKWVNKHLMKSQrhITDLYEDLRDGHNLISLLEVLSGE---TLPREKGR-------MRFHKLQNVQIALDFLKHRQV 128
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGF 459
|
90 100
....*....|....*....|...
gi 736215636 129 KLVNIRNDDIADGNpKLTLGLIW 151
Cdd:COG5069 460 SLVGIKGLEILDGI-RLKLTLVW 481
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1511-1758 |
2.71e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 43.70 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1511 MTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNaEDELKRKSEAEKeaakqkqkalddlqkfk 1590
Cdd:PRK00106 22 ISIKMKSAKEAAELTLLNAEQEAVNLRGKAERDAEHIKKTAKRESKALKK-ELLLEAKEEARK----------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1591 mQAEEAERRMKqAEEEKLRQIkvveEVAQKSAATQLQSHSMSFNVKASKLEeslKKEQgtvlQLQEEAEQLRKQQEEANK 1670
Cdd:PRK00106 84 -YREEIEQEFK-SERQELKQI----ESRLTERATSLDRKDENLSSKEKTLE---SKEQ----SLTDKSKHIDEREEQVEK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1671 AREQAEKELETWRQKANEALRLRLQAEEEaqkKSKTQEEAERQKvEAERDAKKRAkaedaalkqkDNAEKEL---EKQRT 1747
Cdd:PRK00106 151 LEEQKKAELERVAALSQAEAREIILAETE---NKLTHEIATRIR-EAEREVKDRS----------DKMAKDLlaqAMQRL 216
|
250
....*....|.
gi 736215636 1748 FAEQVAQQKLS 1758
Cdd:PRK00106 217 AGEYVTEQTIT 227
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1446-1610 |
2.81e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.86 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1446 KEEASKRQDVAVDAEQQKQNIQHELHHLKSLSEQ--EIKSKSQQLEHAL----VSHTKIEEEIHTIRIQLEMTIKQKKTA 1519
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQQREEELEELQEQleDLESSIQELEKEIkkleSSIKQVEEELEELKEQNEELEKQYKVK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1520 ESELQQLRDKAAEAEKLRKAAQEDAERLrKQVAEETQKKKNAE-DELKRKSEAEKEAAKQKQKALDDLQKF--KMQAEEA 1596
Cdd:pfam05667 390 KKTLDLLPDAEENIAKLQALVDASAQRL-VELAGQWEKHRVPLiEEYRALKEAKSNKEDESQRKLEEIKELreKIKEVAE 468
|
170
....*....|....
gi 736215636 1597 ERRMKqaeEEKLRQ 1610
Cdd:pfam05667 469 EAKQK---EELYKQ 479
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1709-1871 |
2.89e-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: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1709 EAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDN--ELQR 1786
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1787 LKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEkktmsntEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQ 1866
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELE-------AELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*
gi 736215636 1867 TAEEE 1871
Cdd:COG1579 167 ELAAK 171
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
2232-2585 |
2.89e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 44.27 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2232 LRLDETDKQK----ALLDEELQR-----------VKGEVNDAVKQKAQVEDELAKVRI-QMDELLKLKL-KIEEQNRSLM 2294
Cdd:PTZ00108 988 VRLDLYKKRKeyllGKLERELARlsnkvrfikhvINGELVITNAKKKDLVKELKKLGYvRFKDIIKKKSeKITAEEEEGA 1067
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2295 KKDKDKTQKVLAEEAGKMKSL------------AEEAARLSVEAEETARQRQIAESNLAEQRALAE--KMLK--EKMQAI 2358
Cdd:PTZ00108 1068 EEDDEADDEDDEEELGAAVSYdyllsmpiwsltKEKVEKLNAELEKKEKELEKLKNTTPKDMWLEDldKFEEalEEQEEV 1147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2359 QEATKLKAEAQElQKQKDQAQEKAKKLLEDK-QQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSk 2437
Cdd:PTZ00108 1148 EEKEIAKEQRLK-SKTKGKASKLRKPKLKKKeKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQ- 1225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2438 aENEAKKFKKQADEAKARLKDTEKQSTETVVQKlETQRLQSTREADGLKEAIADLEKEREKLKKEAEELQNKSNKMANTQ 2517
Cdd:PTZ00108 1226 -EDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDN-DEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPS 1303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 2518 KEEIEQQKAIIQKSfiserelllkrQKAVEDEKKKLQKQFEDEVKKAEALKDEQERQRKLMEEEKKKL 2585
Cdd:PTZ00108 1304 SPTKKKVKKRLEGS-----------LAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKK 1360
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1774-1927 |
2.93e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1774 EQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATr 1853
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAK- 583
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736215636 1854 lrsvAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRlrtEAEIALKAKEAENERLkrKAEDEAYQRKL 1927
Cdd:PRK00409 584 ----KEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANE---KKEKKKKKQKEKQEEL--KVGDEVKYLSL 648
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2046-2213 |
2.97e-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: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2046 EEAARQCKAAQEEVARLEKKADEANKQKEKAEKEaekqvivAKEAAQKCSSAEQKAQevLSKNKEDSLAQQKMKEEFENA 2125
Cdd:pfam05262 216 QQLKEELDKKQIDADKAQQKADFAQDNADKQRDE-------VRQKQQEAKNLPKPAD--TSSPKEDKQVAENQKREIEKA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2126 KRLAQaaekakekaekeaallrQKAAEAEKQKKSAEEEAAKQAKAQkdaEKLKKAAEEEASKRAAAEAEALKQKKQADAE 2205
Cdd:pfam05262 287 QIEIK-----------------KNDEEALKAKDHKAFDLKQESKAS---EKEAEDKELEAQKKREPVAEDLQKTKPQVEA 346
|
....*...
gi 736215636 2206 MAKHKKEA 2213
Cdd:pfam05262 347 QPTSLNED 354
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2146-2444 |
3.02e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.12 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2146 LRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKK-----EADQALKLK 2220
Cdd:PLN02939 86 LPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARlqaleDLEKILTEK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2221 SQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQNRSLmKKDKDK 2300
Cdd:PLN02939 166 EALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLL-KDDIQF 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2301 TQKVLAEEAGKMKSLAE--------EAARLSVEAEETARQRQIAESNLAEQRALAEKMlkEKMQAIQEATKLKAEA---- 2368
Cdd:PLN02939 245 LKAELIEVAETEERVFKlekersllDASLRELESKFIVAQEDVSKLSPLQYDCWWEKV--ENLQDLLDRATNQVEKaalv 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2369 ----QELQKQKDQAQEK------AKKLLEDKQQIQQRLDKETEGFQKSlEAERKRQLEVSAEAetlrlkVKELSDAQSKA 2438
Cdd:PLN02939 323 ldqnQDLRDKVDKLEASlkeanvSKFSSYKVELLQQKLKLLEERLQAS-DHEIHSYIQLYQES------IKEFQDTLSKL 395
|
....*.
gi 736215636 2439 ENEAKK 2444
Cdd:PLN02939 396 KEESKK 401
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2326-2601 |
3.07e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.78 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2326 AEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEAtKLKAEAQELQKQKDQAQEKAKKLLEDKQqiqqrlDKETEGFQK 2405
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLEREKAAREA-RHKKAAEARAAKDKDAVAAALARVKAKK------AAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2406 SLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTETVVQKletqrlqstrEADGL 2485
Cdd:PRK05035 509 KAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEE----------EVDPK 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2486 KEAIADLEKEREKLKKEAEELQNKSNKMANTQKEEIEQQKAIIQKSFISERELLLKRQKAVEDEKKKlqKQFEDEVKKAE 2565
Cdd:PRK05035 579 KAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRK--AAVAAAIARAK 656
|
250 260 270
....*....|....*....|....*....|....*.
gi 736215636 2566 ALKDEQERQRKLMEEEKKKLQAIMDAAVKKQKEAEA 2601
Cdd:PRK05035 657 ARKAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKA 692
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1653-1759 |
3.58e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1653 QLQEEAEQLRKQQEEANKAREQAEKELetwrqkanEALRLRLQaeeeaQKKSKTQEEAERQKVEAERDAKKR---AKAEd 1729
Cdd:PRK00409 520 ELIASLEELERELEQKAEEAEALLKEA--------EKLKEELE-----EKKEKLQEEEDKLLEEAEKEAQQAikeAKKE- 585
|
90 100 110
....*....|....*....|....*....|
gi 736215636 1730 AALKQKDNAEKELEKQRTFAEQVAQQKLSA 1759
Cdd:PRK00409 586 ADEIIKELRQLQKGGYASVKAHELIEARKR 615
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1498-1588 |
3.62e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.93 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1498 IEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEEtqKKKNAEDELKR-KSEAEKEAA 1576
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEE--AKAEAEAEAERiIAQAEAEIE 106
|
90
....*....|..
gi 736215636 1577 KQKQKALDDLQK 1588
Cdd:COG0711 107 QERAKALAELRA 118
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1845-1942 |
3.81e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1845 KQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKIlkEKLAAINEATRLRTEAEIA-LKAKEAENERLKRKaedeay 1923
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVAL--EGLAAELEEKQQELEAQLEqLQEKAAETSQERKQ------ 216
|
90
....*....|....*....
gi 736215636 1924 QRKLLEDQAAQhKHDIQEK 1942
Cdd:PRK11448 217 KRKEITDQAAK-RLELSEE 234
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2140-2383 |
3.82e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2140 EKEAAllrqKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAE-------EEASKRAAAEAEA-----LKQKKQADAEMA 2207
Cdd:PRK07735 11 KKEAA----RRAKEEARKRLVAKHGAEISKLEEENREKEKALPknddmtiEEAKRRAAAAAKAkaaalAKQKREGTEEVT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2208 KHKKEADQAlklksqveKELTMVKLRLDETDKQKAlldEELQRVKGEVNDAVKQKAQVEdelAKVRIQMDELLKLKLKIE 2287
Cdd:PRK07735 87 EEEKAKAKA--------KAAAAAKAKAAALAKQKR---EGTEEVTEEEKAAAKAKAAAA---AKAKAAALAKQKREGTEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2288 EQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQRQIAEsnlAEQRALAEKMLKEKMQAIQEATKLKAE 2367
Cdd:PRK07735 153 VTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAK---AKAKAAAAAKAKAAALAKQKASQGNGD 229
|
250
....*....|....*..
gi 736215636 2368 A-QELQKQKDQAQEKAK 2383
Cdd:PRK07735 230 SgDEDAKAKAIAAAKAK 246
|
|
| F-BAR_PSTPIP |
cd07647 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ... |
1719-1881 |
3.88e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153331 [Multi-domain] Cd Length: 239 Bit Score: 42.46 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1719 RDAKKRAKAEDAALKQKDNAEKELEKqrtfAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDN---EL-QRLKKEVSAT 1794
Cdd:cd07647 15 KEGKKMCKELEDFLKQRAKAEEDYGK----ALLKLSKSAGPGDEIGTLKSSWDSLRKETENVANahiQLaQSLREEAEKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1795 EKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMsnteKSKQLLESEAlKMKQLADEATRlRSVAEEAKKQRQTAEEEAAR 1874
Cdd:cd07647 91 EEFREKQKEERKKTEDIMKRSQKNKKELYKKTM----KAKKSYEQKC-REKDKAEQAYE-KSSSGAQPKEAEKLKKKAAQ 164
|
....*..
gi 736215636 1875 QRAEAEK 1881
Cdd:cd07647 165 CKTSAEE 171
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1514-1956 |
3.97e-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: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1514 KQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKF---- 1589
Cdd:COG3064 32 EQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAaaae 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1590 KMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEAN 1669
Cdd:COG3064 112 KAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1670 KAREQAEKELETWRQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFA 1749
Cdd:COG3064 192 AADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1750 EQVAQQKLSAEQEcIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLLEEELAKVRSEMDSLLKMKTEAEKKTMSN 1829
Cdd:COG3064 272 AALSSGLVVVAAA-LAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1830 TEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEKILKEKLAAINEATRLRTEAEIALKAKEA 1909
Cdd:COG3064 351 AAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAA 430
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 736215636 1910 ENERLKRKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSSDSEMVR 1956
Cdd:COG3064 431 GAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVL 477
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1367-1719 |
4.00e-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: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1367 LRTRYSELMTLTSQYIKFITETQRRLEDDEKASEKLKEEERKKMAEIQAELDKQKqiaeaqaKSVIKAEQEAQELKLKMK 1446
Cdd:pfam10174 420 LKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLK-------KENKDLKEKVSALQPELT 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1447 EEASKRQDVAVDAEQQKQNIQHELHHLKSLsEQEIKSKSQQLEHALVSHTKIEEEIHTIRIQLEMTIKQkKTAESELQQL 1526
Cdd:pfam10174 493 EKESSLIDLKEHASSLASSGLKKDSKLKSL-EIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRI-RLLEQEVARY 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1527 RDKAAEaeklrkaAQEDAERLRkQVAEETQKKKNAEDelKRKSEAEKEAAKQ-KQKALDDLQKFKMQAEEAERRMKQAEE 1605
Cdd:pfam10174 571 KEESGK-------AQAEVERLL-GILREVENEKNDKD--KKIAELESLTLRQmKEQNKKVANIKHGQQEMKKKGAQLLEE 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1606 EKLRQikvvEEVAQKSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQL-------RKQQEEANKAREQA--- 1675
Cdd:pfam10174 641 ARRRE----DNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLtnlraerRKQLEEILEMKQEAlla 716
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 736215636 1676 ---EKEletwrqkANEALrlrlqAEEEAQKKSKTQEEAERQKVEAER 1719
Cdd:pfam10174 717 aisEKD-------ANIAL-----LELSSSKKKKTQEEVMALKREKDR 751
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2177-2640 |
4.07e-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: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2177 LKKaaEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALK--------LKSQVEKELTMVKLRLDETDKQKALLDEEL 2248
Cdd:pfam10174 41 LKK--ERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQdelraqrdLNQLLQQDFTTSPVDGEDKFSTPELTEENF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2249 QRVKGEVNDAVKqkaqvedELAKVRIQMDELlklKLKIEEQNRSLMKKDkDKTQKVLaeEAGKMKSLAeeaARLSVEAEE 2328
Cdd:pfam10174 119 RRLQSEHERQAK-------ELFLLRKTLEEM---ELRIETQKQTLGARD-ESIKKLL--EMLQSKGLP---KKSGEEDWE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2329 TARQRQIAESNLAEQRALAEKMLKE----------KMQAIQEATKLKAEAQ--ELQKQKDQAQEKAKKLLEDKQQIQQrl 2396
Cdd:pfam10174 183 RTRRIAEAEMQLGHLEVLLDQKEKEnihlreelhrRNQLQPDPAKTKALQTviEMKDTKISSLERNIRDLEDEVQMLK-- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2397 dkeTEGFQKSLEAERK-RQLEVsaeaetlrlkvkelsdaqskAENEAKKFKKQADEAKARL--KDTEKQSTETVVQKLET 2473
Cdd:pfam10174 261 ---TNGLLHTEDREEEiKQMEV--------------------YKSHSKFMKNKIDQLKQELskKESELLALQTKLETLTN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2474 QRLQSTREADGLKEAIAdlekereklkkeaeelqnksnkmANTQKEEIEQQKAIIQKSFISERELLL-KRQKAVED---E 2549
Cdd:pfam10174 318 QNSDCKQHIEVLKESLT-----------------------AKEQRAAILQTEVDALRLRLEEKESFLnKKTKQLQDlteE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2550 KKKLQKQFED-----EVK---------KAEALKDEQERQRKLMEEEKKKLQAIM------DAAVKKQKEAEAD----MKN 2605
Cdd:pfam10174 375 KSTLAGEIRDlkdmlDVKerkinvlqkKIENLQEQLRDKDKQLAGLKERVKSLQtdssntDTALTTLEEALSEkeriIER 454
|
490 500 510
....*....|....*....|....*....|....*
gi 736215636 2606 KQTEMEVLEKKRLDQEKQLGAENQKLREKLQCLEG 2640
Cdd:pfam10174 455 LKEQREREDRERLEELESLKKENKDLKEKVSALQP 489
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2145-2472 |
4.09e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2145 LLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVE 2224
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2225 KELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQNRSLMKKDKDKTQKV 2304
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2305 LAEEAGKMKSLAEEAARLSVEAEETARQRQIAE-----SNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQ 2379
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELleakdSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2380 EKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDT 2459
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
330
....*....|...
gi 736215636 2460 EKQSTETVVQKLE 2472
Cdd:COG4372 348 VGLLDNDVLELLS 360
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1523-1723 |
4.22e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1523 LQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQkkknaeDELKRKSEAEKEAAKqkqkalddlqkfkmqaeeAERRMKQ 1602
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAK------ELLLRERNQQRQEAR------------------REREELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1603 AEEEKLRQikvveevaqksAATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEEAEQLRKQ-QEEANKAREQAEKELet 1681
Cdd:PRK12705 81 REEERLVQ-----------KEEQLDARAEKLDNLENQLEEREKALSARELELEELEKQLDNElYRVAGLTPEQARKLL-- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 736215636 1682 wrqkaneALRLRLQAEEEAQKKSKTQEeaERQKVEAERDAKK 1723
Cdd:PRK12705 148 -------LKLLDAELEEEKAQRVKKIE--EEADLEAERKAQN 180
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1837-2458 |
4.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1837 LESEALKMKQLADEATRLRSVAEEAKKQRQTAEE-EAARQRAEAEKILKEKLAAINEATRLRTeAEIALKAKEAENERLK 1915
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIELLEPiRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1916 RKAEDEAYQRKLLEDQAAQHKHDIQEKIIHLKSSSdsemvrqktiveetLRQKKIVEEEIHIIRINFEKASKGKSDLENE 1995
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNG--------------GDRLEQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1996 LKKLKVIAEETQKSklkAEAEAEKLKKLAAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADeankqkek 2075
Cdd:COG4913 368 LAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS-------- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2076 aekEAEKQVIVAKEA-AQKCSSAEQKAQ---EVLSKNKEDslaqqkmkEEFENAkrlaqaaekakekaekEAALLR---- 2147
Cdd:COG4913 437 ---NIPARLLALRDAlAEALGLDEAELPfvgELIEVRPEE--------ERWRGA----------------IERVLGgfal 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2148 ---------QKAAEA------------EKQKKSAEEEAAKQAKAQKDAEKLK-------KAAEEEASKRAAAE----AEA 2195
Cdd:COG4913 490 tllvppehyAAALRWvnrlhlrgrlvyERVRTGLPDPERPRLDPDSLAGKLDfkphpfrAWLEAELGRRFDYVcvdsPEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2196 LKQKKQA--DAEMAKHKKE-------------------ADQALKLKsqvEKELTMVKLRLDETDKQKALLDEELQRVKG- 2253
Cdd:COG4913 570 LRRHPRAitRAGQVKGNGTrhekddrrrirsryvlgfdNRAKLAAL---EAELAELEEELAEAEERLEALEAELDALQEr 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2254 ---------------EVNDAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQnrslmKKDKDKTQKVLAEEAGKMKSLAEE 2318
Cdd:COG4913 647 realqrlaeyswdeiDVASAEREIAELEAELERLDASSDDLAALEEQLEEL-----EAELEELEEELDELKGEIGRLEKE 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2319 AARLSVEAEE-TARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLD 2397
Cdd:COG4913 722 LEQAEEELDElQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWP 801
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736215636 2398 KETEGFQKSLEA-----ERKRQLevsaEAETLRLKVKELSDAQSKAENEAK-----KFKKQADEAKARLKD 2458
Cdd:COG4913 802 AETADLDADLESlpeylALLDRL----EEDGLPEYEERFKELLNENSIEFVadllsKLRRAIREIKERIDP 868
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2147-2218 |
4.34e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.50 E-value: 4.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736215636 2147 RQKAAEAEKQKKSAEEeaaKQAKAQKDAEKLKKAAEEEASK-----RAAAEAEALKQKKQADAEMAKHKKEADQALK 2218
Cdd:cd06503 43 EKAKEEAEELLAEYEE---KLAEARAEAQEIIEEARKEAEKikeeiLAEAKEEAERILEQAKAEIEQEKEKALAELR 116
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1420-1636 |
4.37e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1420 QKQIAEAQAKsVIKAEQEAQELKLK-----MKEEASKRQDVAVDAEQQKQNIQHELhhlkslseQEIKSKSQQLEHALVS 1494
Cdd:COG3206 181 EEQLPELRKE-LEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAEL--------AEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1495 HTKIEEEIHTIRIQLEMtikqkktaESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKE 1574
Cdd:COG3206 252 GPDALPELLQSPVIQQL--------RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736215636 1575 AAKQK----QKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAATQLQSHSMSFNVK 1636
Cdd:COG3206 324 ALQAReaslQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1653-1731 |
4.55e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1653 QLQEEAEQLRKQQEEANKAREQAEKELEtwrQKANEALRLRLQAEEEAQKKSKTQEE-----AERQKVEAERDAKKRAKA 1727
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAE---AQQQELVALEGLAAELEEKQQELEAQleqlqEKAAETSQERKQKRKEIT 222
|
....
gi 736215636 1728 EDAA 1731
Cdd:PRK11448 223 DQAA 226
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2346-2475 |
4.60e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.07 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2346 LAEKMLKEKMQAIQEATKlkaEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERK--RQLEVSAEAET 2423
Cdd:pfam05262 196 FRRDMTDLKERESQEDAK---RAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNlpKPADTSSPKED 272
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 736215636 2424 LRL---KVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTETVVQK-LETQR 2475
Cdd:pfam05262 273 KQVaenQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKeLEAQK 328
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1433-2462 |
4.62e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.67 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1433 KAEQEAQELKLKMKEEASKRQDVAVDA-EQQKQNIQHELHHLKSLSEQEIKSKSQQLEHALV-SHTKIEEEIHTIRIQLE 1510
Cdd:PTZ00440 659 KSKEDLQTLLNTSKNEYEKLEFMKSDNiDNIIKNLKKELQNLLSLKENIIKKQLNNIEQDISnSLNQYTIKYNDLKSSIE 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1511 MTIKQKKTAESELQQLRDKAaeaEKLRKAAQEDAERLR--KQVAEETQKKKNAEDELKRKSEAEKEAAKQ-KQKALDDLQ 1587
Cdd:PTZ00440 739 EYKEEEEKLEVYKHQIINRK---NEFILHLYENDKDLPdgKNTYEEFLQYKDTILNKENKISNDINILKEnKKNNQDLLN 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1588 KF--KMQAEEAERRMKQAEEEKLRQ--------IKVVE------EVAQKSAATQLQSHSMSFNVKASKLEESLKKEQGTV 1651
Cdd:PTZ00440 816 SYniLIQKLEAHTEKNDEELKQLLQkfptedenLNLKElekefnENNQIVDNIIKDIENMNKNINIIKTLNIAINRSNSN 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1652 LQLqeeAEQLRKQQEEANKAREQAEKELETW---RQKANEALRLRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAE 1728
Cdd:PTZ00440 896 KQL---VEHLLNNKIDLKNKLEQHMKIINTDniiQKNEKLNLLNNLNKEKEKIEKQLSDTKINNLKMQIEKTLEYYDKSK 972
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1729 DAALKQKDNAEKELEKQRTFAEQVAQQ--KLSAEQECIRLKADfDHAEQQR----GLLDNELQRLKKEVSATEKQR-KLL 1801
Cdd:PTZ00440 973 ENINGNDGTHLEKLDKEKDEWEHFKSEidKLNVNYNILNKKID-DLIKKQHddiiELIDKLIKEKGKEIEEKVDQYiSLL 1051
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1802 EEELAKVRSemdsllKMKTEAEKKTMSNTEKSK-QLLE--SEAL--KMKQLADEATRLRSVAEE----AKKQRQTAEEEA 1872
Cdd:PTZ00440 1052 EKMKTKLSS------FHFNIDIKKYKNPKIKEEiKLLEekVEALlkKIDENKNKLIEIKNKSHEhvvnADKEKNKQTEHY 1125
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1873 ARQRAEAEKILKEKLAAINEatrLRTEAEIALKAKEAENERLKrkaedeaYQRKLLedqaaqhkHDIQEKIIHLKSSSDS 1952
Cdd:PTZ00440 1126 NKKKKSLEKIYKQMEKTLKE---LENMNLEDITLNEVNEIEIE-------YERILI--------DHIVEQINNEAKKSKT 1187
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1953 EMVRQKTIVEET-LRQKKIVEEEIHIIR---------------------INFEKASKGKSDLENELKKLKVIAEET---- 2006
Cdd:PTZ00440 1188 IMEEIESYKKDIdQVKKNMSKERNDHLTtfeynayydkatasyenieelTTEAKGLKGEANRSTNVDELKEIKLQVfsyl 1267
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2007 QKSKLKAEAEAEKLKKL----AAEEEKKRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKAdEANKQKEKAEKEAEK 2082
Cdd:PTZ00440 1268 QQVIKENNKMENALHEIknmyEFLISIDSEKILKEILNSTKKAEEFSNDAKKELEKTDNLIKQV-EAKIEQAKEHKNKIY 1346
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2083 QVIVAKEAAQKCSSAEQKAQEVLSKNKEDSLAQQKMKE-------EFENAKRLAQAAEKAKEKAEKEAALLR----QKAA 2151
Cdd:PTZ00440 1347 GSLEDKQIDDEIKKIEQIKEEISNKRKEINKYLSNIKSnkekcdlHVRNASRGKDKIDFLNKHEAIEPSNSKevniIKIT 1426
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2152 EAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKqadaeMAKHKKEADQALK----LKSQVEKEL 2227
Cdd:PTZ00440 1427 DNINKCKQYSNEAMETENKADENNDSIIKYEKEITNILNNSSILGKKTK-----LEKKKKEATNIMDdingEHSIIKTKL 1501
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2228 TMVKLRLDETDKQKALLDEE------------------LQRVKGEVNDAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQ 2289
Cdd:PTZ00440 1502 TKSSEKLNQLNEQPNIKREGdvlnndkstiayetiqynLGRVKHNLLNILNIKDEIETILNKAQDLMRDISKISKIVENK 1581
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2290 NRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLsveaEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQ 2369
Cdd:PTZ00440 1582 NLENLNDKEADYVKYLDNILKEKQLMEAEYKKL----NEIYSDVDNIEKELKKHKKNYEIGLLEKVIEINKNIKLYMDST 1657
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2370 E------------LQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQKSLEAERKRQLEVSAEAEtlrlkvkELSDAQSK 2437
Cdd:PTZ00440 1658 KeslnslvnnfssLFNNFYLNKYNINENLEKYKKKLNEIYNEFMESYNIIQEKMKEVSNDDVDYN-------EAKTLREE 1730
|
1130 1140
....*....|....*....|....*
gi 736215636 2438 AENEAKKFKKQADEAKARLKDTEKQ 2462
Cdd:PTZ00440 1731 AQKEEVNLNNKEEEAKKYLNDIKKQ 1755
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1845-2070 |
4.74e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.53 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1845 KQLADEATRLRSVAEEAKKQRQTAEEEAARQRAEAEK-ILKEKLAAINEATRLRTEAEIALKAKEAENERLKRKAEDEAY 1923
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKqRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1924 QRKLLEDQAAQHKHDIQEKIIHLKSSSdsemvrqktiveETLRQKKIVEEEIHiirinfeKASKGKSDLENELKKLKVIA 2003
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQA------------EEEAKAKAAAEAKK-------KAEEAKKKAEAEAKAKAEAE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 2004 EETQKSKLKAEAEAEKLKklaaeeekkrkeseekvkritaAEEEAARQCKAAQEEVARL--EKKADEAN 2070
Cdd:TIGR02794 187 AKAKAEEAKAKAEAAKAK----------------------AAAEAAAKAEAEAAAAAAAeaERKADEAE 233
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1659-1922 |
4.77e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1659 EQLRKqqEEANKAREQAEKELETwRQKANEAlrlrlQAEEEAQKKSKTQEEAERQKV-EAERDAKKRAKAEDAAL-KQKD 1736
Cdd:PRK07735 8 EDLKK--EAARRAKEEARKRLVA-KHGAEIS-----KLEEENREKEKALPKNDDMTIeEAKRRAAAAAKAKAAALaKQKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1737 NAEKELekqrTFAEQVAQQKLSAEQECIRLKAdfdhaeqqrglldnelqrLKKEVSATEKQRKLLEEELAKVRSEMDSLL 1816
Cdd:PRK07735 80 EGTEEV----TEEEKAKAKAKAAAAAKAKAAA------------------LAKQKREGTEEVTEEEKAAAKAKAAAAAKA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1817 KMKTEAEKKTMSNTEKSKQLLESEALKMKQLADEATRLRSVAeeakkqrqTAEEEAARQRAEAEKILKEKLAAineatrl 1896
Cdd:PRK07735 138 KAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAA--------LAKQKAAEAGEGTEEVTEEEKAK------- 202
|
250 260
....*....|....*....|....*.
gi 736215636 1897 rTEAEIALKAKEAENERLKRKAEDEA 1922
Cdd:PRK07735 203 -AKAKAAAAAKAKAAALAKQKASQGN 227
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1389-1677 |
4.82e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1389 QRRLEDDEkaseklkeeerkkmaeiQAELDKQKQIAEAQAKSVIKAEQEAQElKLKMKEEASKRQDVAVDAEQQKQNIQH 1468
Cdd:PRK05035 459 QARLEREK-----------------AAREARHKKAAEARAAKDKDAVAAALA-RVKAKKAAATQPIVIKAGARPDNSAVI 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1469 ELHHLKSLSEQEIKSKSQQLEHALVSHTKIEEEIhtiriqleMTIKQKKTAeseLQQLRDKAAEAEKLRKAAQEDAerlr 1548
Cdd:PRK05035 521 AAREARKAQARARQAEKQAAAAADPKKAAVAAAI--------ARAKAKKAA---QQAANAEAEEEVDPKKAAVAAA---- 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1549 kqVAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQKSAAtqlqs 1628
Cdd:PRK05035 586 --IARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKAR----- 658
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 736215636 1629 hsmsfnvkaskleeslKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEK 1677
Cdd:PRK05035 659 ----------------KAAQQQANAEPEEAEDPKKAAVAAAIARAKAKK 691
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2117-2264 |
4.92e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.07 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2117 KMKEEFENAKR---LAQAAEKAKEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEA 2193
Cdd:pfam05262 204 KERESQEDAKRaqqLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREI 283
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736215636 2194 EALKQKKQADAEMAKHKKEAdQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQ 2264
Cdd:pfam05262 284 EKAQIEIKKNDEEALKAKDH-KAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNE 353
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2086-2227 |
5.08e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2086 VAKEAAQKCSSAEQKAQ-EVLSKNKEDSLAQQKMKEEFENAKRLAQAAEKAKEKAEKEAALLRQKaAEAEKQKKSAEEEA 2164
Cdd:COG2268 197 IIRDARIAEAEAERETEiAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETAR-AEAEAAYEIAEANA 275
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 2165 AKQ-------AKAQKD-----AEKLKKAAEEEASKRAAAEAEALKQKKQADAE----MAKHKKEAdQALKLKSQVEKEL 2227
Cdd:COG2268 276 EREvqrqleiAEREREielqeKEAEREEAELEADVRKPAEAEKQAAEAEAEAEaeaiRAKGLAEA-EGKRALAEAWNKL 353
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1534-1744 |
5.11e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1534 EKLRKAAQEDAERLRKQVAEETQKKKNAEDELKRKSEAEKEAAKQKQkaldDLQKFKMQAEEAERRMKQAEEEKLRQI-- 1611
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKE----ELEEKKEKLQEEEDKLLEEAEKEAQQAik 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1612 ---KVVEEVAQKSAATQLQSHSmsfNVKASKLEESLKKEQGtvlQLQEEAEQLRKQQEEANKAREQAEKELETWRQKA-- 1686
Cdd:PRK00409 581 eakKEADEIIKELRQLQKGGYA---SVKAHELIEARKRLNK---ANEKKEKKKKKQKEKQEELKVGDEVKYLSLGQKGev 654
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736215636 1687 ------NEA------LRLRLQAEEeaQKKSKTQEEAERQKVEAERDAKKRAKAE-DAALKQKDNAEKELEK 1744
Cdd:PRK00409 655 lsipddKEAivqagiMKMKVPLSD--LEKIQKPKKKKKKKPKTVKPKPRTVSLElDLRGMRYEEALERLDK 723
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1505-1606 |
5.23e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 41.07 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1505 IRIQLEMTIKQKKTAESElQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQkkknAEDELKRKSEAEKEAAKQKQKALD 1584
Cdd:pfam08614 60 AQLREELAELYRSRGELA-QRLVDLNEELQELEKKLREDERRLAALEAERAQ----LEEKLKDREEELREKRKLNQDLQD 134
|
90 100
....*....|....*....|..
gi 736215636 1585 DLQKFKMQAEEAERRMKQAEEE 1606
Cdd:pfam08614 135 ELVALQLQLNMAEEKLRKLEKE 156
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2540-2649 |
5.35e-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: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2540 LKRQKAVEDEKKKLQKQF---EDEVKKAEALKDEQERQRKLMEEEKKKLQAIMDAAVKKQKEAEADMKNKqteMEvLEKK 2616
Cdd:pfam02841 182 LQSKEAVEEAILQTDQALtakEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEK---ME-AERE 257
|
90 100 110
....*....|....*....|....*....|...
gi 736215636 2617 RLDQEKQLGAENQKLREKLQCLEGASKQSATKQ 2649
Cdd:pfam02841 258 QLLAEQERMLEHKLQEQEELLKEGFKTEAESLQ 290
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2543-2648 |
5.38e-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: 42.44 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2543 QKAVEDEKKKLQKQFEDEVKKAEALKDEQERQRKLMEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEKKRLDQEK 2622
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100
....*....|....*....|....*.
gi 736215636 2623 QLGAENQKLREKLQCLEGASKQSATK 2648
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLA 123
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2274-2404 |
5.63e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.18 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2274 IQMDELLK--LKLKIEEQNrSLMKKDKDKTQKVLAEEAGKMKSLAEEAarlsvEAEETARQRQIAESNLAEQralaEKML 2351
Cdd:cd16269 166 VKAEEVLQefLQSKEAEAE-AILQADQALTEKEKEIEAERAKAEAAEQ-----ERKLLEEQQRELEQKLEDQ----ERSY 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 736215636 2352 KEKMQAIQEatKLKAEAQELQKQKDQA-----QEKAKKLLEDKQQIQQRLDKETEGFQ 2404
Cdd:cd16269 236 EEHLRQLKE--KMEEERENLLKEQERAlesklKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2407-2615 |
5.63e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2407 LEAERKRQLevsaeAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARlKDTEKQSTETVVQKLETQRLQST--READg 2484
Cdd:COG2268 186 LDALGRRKI-----AEIIRDARIAEAEAERETEIAIAQANREAEEAELE-QEREIETARIAEAEAELAKKKAEerREAE- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2485 LKEAIADlekereklkkeaeelqnksnkmANTQKEEIEQQKAIIQKSFISERELLLKRQKAveDEKKKLQKQFEDEVKKA 2564
Cdd:COG2268 259 TARAEAE----------------------AAYEIAEANAEREVQRQLEIAEREREIELQEK--EAEREEAELEADVRKPA 314
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 736215636 2565 EALKDEQERQRKLmEEEKKKLQAIMDAAVKKQK-EAEADMKNKQTEMEVLEK 2615
Cdd:COG2268 315 EAEKQAAEAEAEA-EAEAIRAKGLAEAEGKRALaEAWNKLGDAAILLMLIEK 365
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
1523-1740 |
5.74e-03 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 43.06 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1523 LQQLRDKAAEAEKLRK----AAQEDAERLRKqvAEETQKKKNAEDELKRKSEAEKEAAKQKQKALDDlQKFKMQAEEAER 1598
Cdd:PRK14900 834 LAGVIDLAAETARVDKeigkVDQDLAVLERK--LQNPSFVQNAPPAVVEKDRARAEELREKRGKLEA-HRAMLSGSEANS 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1599 RMKQAEEEKLRQIKVVEEVAQKSAATQlqshsmsfnvkASKLEESLKKEQGTVLQLQEEA--------EQLRKqqEEANK 1670
Cdd:PRK14900 911 ARRDTMEIQNEQKPTQDGPAAEAQPAQ-----------ENTVVESAEKAVAAVSEAAQQAatavasgiEKVAE--AVRKT 977
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1671 AREQAEKELETWRQKANEALRlRLQAEEEAQKKSKTQEEAERQKVEAERDAKKRAKAEDAALKQKDNAEK 1740
Cdd:PRK14900 978 VRRSVKKAAATRAAMKKKVAK-KAPAKKAAAKKAAAKKAAAKKKVAKKAPAKKVARKPAAKKAAKKPARK 1046
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2321-2635 |
5.78e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2321 RLSVEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKEt 2400
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2401 egfQKSLEAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTETVVQKLETQRLQSTR 2480
Cdd:COG4372 93 ---QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2481 EADGLKEAIADLEKEREKLKKEAEELQNKSNKMANTQKEEIEQQKAIIQKSFISERELLLKRQKAVEDEKKKLQKQFEDE 2560
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736215636 2561 VKKAEALKDEQERQRKLMEEEKKKLQAIMDAAVKKQKEAEADMKNKQTEMEVLEKKRLDQEKQLGAENQKLREKL 2635
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| NtpH |
COG2811 |
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ... |
1657-1744 |
5.80e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit H is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 442060 [Multi-domain] Cd Length: 108 Bit Score: 39.51 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1657 EAEQLRKqqEEANKAREQAEKELETWRQKANEalrLRLQAEEEAQKKSKTQEEAERQKVEAERDaKKRAKAEDAALKQKD 1736
Cdd:COG2811 12 EAEEEAD--EIIEEAKEEREERIAEAREEAEE---IIEQAEEEAEEEAQERLEEAREEAEAEAE-EIIEEGEKEAEALKK 85
|
....*...
gi 736215636 1737 NAEKELEK 1744
Cdd:COG2811 86 KAEDKLDK 93
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
1515-1762 |
5.80e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 42.74 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1515 QKKTAESELQqLRDKAAEAEKLRKAAQEDAErlrKQVAeetqKKKNAEDELKRKSEAEKEAAKQKQKALddlqkfKMQAE 1594
Cdd:pfam04747 50 QRKEAFASLE-LTEQPQQVEKVKKSEKKKAQ---KQIA----KDHEAEQKVNAKKAAEKEARRAEAEAK------KRAAQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1595 EAERRMKQAEEEKLRQIKVVEEVAQKsaatqlqshsmsfnvkasKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQ 1674
Cdd:pfam04747 116 EEEHKQWKAEQERIQKEQEKKEADLK------------------KLQAEKKKEKAVKAEKAEKAEKTKKASTPAPVEEEI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1675 AEKELETWRQKAnealrlrlQAEEEAQKKSKTQEEAER-QKVEAERDAKKRAKAEDAALKQKDNAEKELEKQRTFAEQVA 1753
Cdd:pfam04747 178 VVKKVANDRSAA--------PAPEPKTPTNTPAEPAEQvQEITGKKNKKNKKKSESEATAAPASVEQVVEQPKVVTEEPH 249
|
....*....
gi 736215636 1754 QQKLSAEQE 1762
Cdd:pfam04747 250 QQAAPQEKK 258
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1499-1685 |
5.82e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.35 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1499 EEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAE-AEKLRKAAQEDAERLRKQVAEetqKKKNAEDELKRKSEAEKEAAK 1577
Cdd:COG1842 36 EEDLVEARQALAQVIANQKRLERQLEELEAEAEKwEEKARLALEKGREDLAREALE---RKAELEAQAEALEAQLAQLEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1578 QKQKALDDLQKFKMQAEEAERRMKQAeeeKLRqikvveevaQKSAATQLQSHSMSFNVKASKLEESLKKEQGTVLQLQEE 1657
Cdd:COG1842 113 QVEKLKEALRQLESKLEELKAKKDTL---KAR---------AKAAKAQEKVNEALSGIDSDDATSALERMEEKIEEMEAR 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 736215636 1658 AEQLRKQQEEAN--------KAREQAEKELETWRQK 1685
Cdd:COG1842 181 AEAAAELAAGDSlddelaelEADSEVEDELAALKAK 216
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2365-2616 |
5.85e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2365 KAEAQElQKQKDQAQEKAKKLLEDKqqiQQRLDKE----TEGFQKSLEAERKRQLEVSAEAETlRLKVKELSDAQSKAEN 2440
Cdd:PRK05035 435 KAEIRA-IEQEKKKAEEAKARFEAR---QARLEREkaarEARHKKAAEARAAKDKDAVAAALA-RVKAKKAAATQPIVIK 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2441 EAKKFKKQADEAKARLKDTEKQStetvvqklETQRLQSTREADGLKEAIADLEKEREKLKKEAEELQNKSNKMANTQKEE 2520
Cdd:PRK05035 510 AGARPDNSAVIAAREARKAQARA--------RQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAA 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2521 IEQQ--KAIIQKSFISERELLLKRQKAVEDEKKklqKQFEDEVKKAEALKDEQERQRKLMEEEKKKLQAIMDAAVK-KQK 2597
Cdd:PRK05035 582 VAAAiaRAKAKKAAQQAASAEPEEQVAEVDPKK---AAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARaKAR 658
|
250
....*....|....*....
gi 736215636 2598 EAEADMKNKQTEMEVLEKK 2616
Cdd:PRK05035 659 KAAQQQANAEPEEAEDPKK 677
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1560-1824 |
5.87e-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: 42.54 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1560 NAEDELKRksEAE--KEAAKQKQKALDDLQKFKMQAEEAERRMKQAEEEKLRQIKVVEEVAQ---KSAATQLQSHSMSFN 1634
Cdd:pfam03148 116 EVEKELLK--EVEliEGIQELLQRTLEQAWEQLRLLRAARHKLEKDLSDKKEALEIDEKCLSlnnTSPNISYKPGPTRIP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1635 VKASKLEESLKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAEEEAqkksKTQEEAERQK 1714
Cdd:pfam03148 194 PNSSTPEEWEKFTQDNIERAEKERAASAQLRELIDSILEQTANDLRAQADAVNFALRKRIEETEDA----KNKLEWQLKK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1715 VEAE-RDAKKRAKAEDAALKQKDNAEKelekqrtfaeqVAQQKLSAEQECIRLKADFDHAEqqrglldnelQRLKKEVSA 1793
Cdd:pfam03148 270 TLQEiAELEKNIEALEKAIRDKEAPLK-----------LAQTRLENRTYRPNVELCRDEAQ----------YGLVDEVKE 328
|
250 260 270
....*....|....*....|....*....|.
gi 736215636 1794 TEKQRKLLEEELAKVRSEMDSLLKMKTEAEK 1824
Cdd:pfam03148 329 LEETIEALKQKLAEAEASLQALERTRLRLEE 359
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1691-1821 |
5.94e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1691 RLRLQ-----AEEEAQKKSKTQEEAERQKVEAERDAKKRAKAedAALKQKdnaEKELEKQRTFAEQVAQQKLSAEQECIR 1765
Cdd:COG0542 401 RVRMEidskpEELDELERRLEQLEIEKEALKKEQDEASFERL--AELRDE---LAELEEELEALKARWEAEKELIEEIQE 475
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736215636 1766 LKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKLL--EEELAKV-------------RSEMDSLLKMKTE 1821
Cdd:COG0542 476 LKEELEQRYGKIPELEKELAELEEELAELAPLLREEvtEEDIAEVvsrwtgipvgkllEGEREKLLNLEEE 546
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2146-2251 |
6.10e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.93 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2146 LRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEadqalklKSQVEK 2225
Cdd:pfam07926 31 LEKQAEIAREAQQNYERELVLHAEDIKALQALREELNELKAEIAELKAEAESAKAELEESEESWEEQ-------KKELEK 103
|
90 100
....*....|....*....|....*.
gi 736215636 2226 ELTMVKLRLDETDKQKALLDEELQRV 2251
Cdd:pfam07926 104 ELSELEKRIEDLNEQNKLLHDQLESL 129
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2165-2489 |
6.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2165 AKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALL 2244
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2245 DEELQRVKGEVNDAVKQKAQVEDELAKVRIQMDELLKLKLKIEEQNRSLmKKDKDKTQKVLAEEAGKMKSLaeeaarlsv 2324
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL-EAQIAELQSEIAEREEELKEL--------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2325 EAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQAQEKAKKLLEDKQQIQQRLDKETEGFQ 2404
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2405 KSL--EAERKRQLEVSAEAETLRLKVKELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTETVVQKLETQRLQSTREA 2482
Cdd:COG4372 236 SALldALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
....*..
gi 736215636 2483 DGLKEAI 2489
Cdd:COG4372 316 ALLAALL 322
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2308-2491 |
6.48e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2308 EAGK------MKSLAEEAARLSVEAEETARQRqIAESNLAEQRALAEKM--LKEKMQAIQEATKLKAEAQELQKQKDQAQ 2379
Cdd:COG4717 33 EAGKstllafIRAMLLERLEKEADELFKPQGR-KPELNLKELKELEEELkeAEEKEEEYAELQEELEELEEELEELEAEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2380 EKAKKLLEDKQQIQQRLDKETEgfQKSLEAERKrqlEVSAEAETLRLKVKELSDAQ---SKAENEAKKFKKQADEAKARL 2456
Cdd:COG4717 112 EELREELEKLEKLLQLLPLYQE--LEALEAELA---ELPERLEELEERLEELRELEeelEELEAELAELQEELEELLEQL 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 736215636 2457 KDTEK---QSTETVVQKLETQRLQSTREADGLKEAIAD 2491
Cdd:COG4717 187 SLATEeelQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1799-2008 |
6.52e-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: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1799 KLLEEELAKV--RSEMDSLLKMKTEAEKKTMSNTEKSKQLLESEALKMKQLAD----EATRLRSVAEEAKKQRQTAEEEA 1872
Cdd:pfam05262 185 ALREDNEKGVnfRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADfaqdNADKQRDEVRQKQQEAKNLPKPA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1873 ARQRAEAEKILKEKLAAINEATRLRTE--AEIALKAKEAENERLKR--KAEDEAYQRKLLEDQA---------------- 1932
Cdd:pfam05262 265 DTSSPKEDKQVAENQKREIEKAQIEIKknDEEALKAKDHKAFDLKQesKASEKEAEDKELEAQKkrepvaedlqktkpqv 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1933 -AQHKHDIQEKI------IHLKSSSDSEM------------VRQKTIVEETLRQKKIVEEEIHIIRINFEKASKGKSDLE 1993
Cdd:pfam05262 345 eAQPTSLNEDAIdssnpvYGLKVVDPITNlselvlidlkteVRLRESAQQTIRRRGLYEREKDLVAIAITSGNAKLQLVD 424
|
250
....*....|....*
gi 736215636 1994 NELKKLKVIAEETQK 2008
Cdd:pfam05262 425 IDLKNLEVIKESNFE 439
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2744-2778 |
6.57e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.08 E-value: 6.57e-03
10 20 30
....*....|....*....|....*....|....*.
gi 736215636 2744 CLQGQSCVGGILTP-SKEKMSVYQALKENKITPNTA 2778
Cdd:smart00250 3 LLEAQSAIGGIIDPeTGQKLSVEEALRRGLIDPETG 38
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1498-1577 |
6.76e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1498 IEEEIHTIRIQLEMTIKQKKTAESELQQLRDKAAEAEKLRKAAQEDAERLRKQVAEETQKKKNAEDELK-RKSEAEKEAA 1576
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKqKRKEITDQAA 226
|
.
gi 736215636 1577 K 1577
Cdd:PRK11448 227 K 227
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2146-2333 |
6.79e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.20 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2146 LRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAaeAEALKQKKQADAEMAKHKKEADQALKLKSQVEK 2225
Cdd:pfam04012 41 ARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELA--REALAEKKSLEKQAEALETQLAQQRSAVEQLRK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2226 ELTMVKLRLDETDKQKALLDEELQrvkgevndAVKQKAQVEDELAKVRIQ--MDELLKLKLKIEEQ--NRSLMKKdkdkt 2301
Cdd:pfam04012 119 QLAALETKIQQLKAKKNLLKARLK--------AAKAQEAVQTSLGSLSTSsaTDSFERIEEKIEEReaRADAAAE----- 185
|
170 180 190
....*....|....*....|....*....|..
gi 736215636 2302 qkvLAEEAGKMKSLAEEAARLSVEAEETARQR 2333
Cdd:pfam04012 186 ---LASAVDLDAKLEQAGIQMEVSEDVLARLK 214
|
|
| rpsP |
PRK14521 |
30S ribosomal protein S16; Provisional |
2152-2226 |
6.93e-03 |
|
30S ribosomal protein S16; Provisional
Pssm-ID: 237744 [Multi-domain] Cd Length: 186 Bit Score: 40.92 E-value: 6.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736215636 2152 EAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQKKQADAEMAKHKKEADQALKLKSQVEKE 2226
Cdd:PRK14521 96 EAQAEAKFEAWKEEKEGKVNAKKDKLSKAKKAAKKAALEAEKKVNEARAEAVAEKKAAEAAAVAAEEAAAAEEEE 170
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1947-2101 |
6.96e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1947 KSSSDSEMVRQKTI--VEETLRQKKIVEEE----IHIIRINFEKASKGKSDLENELKKLKVIAEETQK-----SKLKAEA 2015
Cdd:PRK09510 72 KSAKRAEEQRKKKEqqQAEELQQKQAAEQErlkqLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAkaaaaAKAKAEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2016 EAEKL----KKLAAEEEKKRKESEEKVKRITA-AEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEA 2090
Cdd:PRK09510 152 EAKRAaaaaKKAAAEAKKKAEAEAAKKAAAEAkKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAA 231
|
170
....*....|.
gi 736215636 2091 AQKCSSAEQKA 2101
Cdd:PRK09510 232 AEAKAAAEKAA 242
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1566-1807 |
7.07e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.52 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1566 KRKSEAEKEAAKQKQKALDDLQKFKMQAEEAERRMKQAEE--EKLRQIKvvEEVAQKSAATQLQSHSMSFNVKASKLEES 1643
Cdd:pfam12795 9 KLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDapAELRELR--QELAALQAKAEAAPKEILASLSLEELEQR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1644 LKKEQGTVLQLQEEAEQLRKQQEEANKAREQAEKELetwrqkanEALRLRLQAEEEAQKKSKTQEEAERQkveAERDAkk 1723
Cdd:pfam12795 87 LLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQL--------SEARQRLQQIRNRLNGPAPPGEPLSE---AQRWA-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1724 rAKAEDAALKQKdNAEKELEkqrtfaeqvaQQKLSAEQECIRLKADFDHAEQQRglLDNELQRLKKEVSatEKQRKLLEE 1803
Cdd:pfam12795 154 -LQAELAALKAQ-IDMLEQE----------LLSNNNRQDLLKARRDLLTLRIQR--LEQQLQALQELLN--EKRLQEAEQ 217
|
....
gi 736215636 1804 ELAK 1807
Cdd:pfam12795 218 AVAQ 221
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2155-2335 |
8.64e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2155 KQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASKRAAAEAEALKQkkQADAEMAKHKKEADQALKLKSQVEKE---LTMVK 2231
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQ--EARREREELQREEERLVQKEEQLDARaekLDNLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2232 LRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKvriqmDELLK-LKLKIEEQNRSLMKKDKDKTQKVLAEEAG 2310
Cdd:PRK12705 105 NQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQAR-----KLLLKlLDAELEEEKAQRVKKIEEEADLEAERKAQ 179
|
170 180
....*....|....*....|....*
gi 736215636 2311 KMksLAEEAARLsveAEETARQRQI 2335
Cdd:PRK12705 180 NI--LAQAMQRI---ASETASDLSV 199
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1952-2332 |
8.82e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1952 SEMVRQKTIVEETLrQKKIVEEEIHIIRINFEKASKGKSDL--ENELKKLKVIAEETQKSKLKAEAEAEKLKKLAAEEEK 2029
Cdd:COG5185 190 KGISELKKAEPSGT-VNSIKESETGNLGSESTLLEKAKEIIniEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2030 KRKESEEKVKRITAAEEEAARQCKAAQEEVARLEKKADEANKQKEKAEKEAEKQVIVAKEAAQKCS-SAEQKAQEVLSKN 2108
Cdd:COG5185 269 KLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETeTGIQNLTAEIEQG 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2109 KEDSLA-QQKMKEEFENakrlaqaaekakEKAEKEAALLRQKAAEAEKQKKSAEEEAAKQAKAQKDAEKLKKAAEEEASK 2187
Cdd:COG5185 349 QESLTEnLEAIKEEIEN------------IVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLK 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2188 RAAAEAEalkqKKQADAEMAKHKKEADQALKLKSQVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVED 2267
Cdd:COG5185 417 AADRQIE----ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIES 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736215636 2268 ELAKVRIQMdellklklkieEQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAARLSVEAEETARQ 2332
Cdd:COG5185 493 RVSTLKATL-----------EKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIP 546
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2288-2487 |
8.97e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2288 EQNRSLMKKDKDKTQKVLAEEAGKMKSLAEEAarlsvEAEETARQRQIAESNLAEQRALAEKMLKEKMQAIQEAT----K 2363
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEA-----EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARaelaE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2364 LKAEAQELQKQKDQAQEKAKKLLEDK---------QQIQQRLDKETEGFQ------KSLEAERkrqlevsaeAETLRLKV 2428
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPviqqlraqlAELEAELAELSARYTpnhpdvIALRAQI---------AALRAQLQ 308
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 736215636 2429 KELSDAQSKAENEAKKFKKQADEAKARLKDTEKQSTETVVQKLETQRLQstREADGLKE 2487
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLE--REVEVARE 365
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4331-4361 |
9.02e-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: 9.02e-03
10 20 30
....*....|....*....|....*....|.
gi 736215636 4331 AGILDTETLEKVSITEAIHRNLVDNITGQRL 4361
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1658-1903 |
9.05e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1658 AEQLRKQQEEANKAREQAEKELETWRQKANEALRLRLQAE--EEAQKKSKT-----QEEAERQKVEAERDAKKRAKAEDA 1730
Cdd:COG3206 106 DEDPLGEEASREAAIERLRKNLTVEPVKGSNVIEISYTSPdpELAAAVANAlaeayLEQNLELRREEARKALEFLEEQLP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1731 ALKQK-DNAEKELE--KQR-------TFAEQVAQQKLSAEQECIRLKADFDHAEQQRGLLDNELQRLKKEVSATEKQRKL 1800
Cdd:COG3206 186 ELRKElEEAEAALEefRQKnglvdlsEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 1801 --LEEELAKVRSEMDSLLKMKTEaekktmsNTEKSKQLLESEALKMKQLADEATRLRSVAEEAKKQRQTAEEEAARQRAE 1878
Cdd:COG3206 266 qqLRAQLAELEAELAELSARYTP-------NHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQ 338
|
250 260
....*....|....*....|....*
gi 736215636 1879 AEKILKEKLAAINEATRLRTEAEIA 1903
Cdd:COG3206 339 LEARLAELPELEAELRRLEREVEVA 363
|
|
| CH_PARVB_rpt2 |
cd21338 |
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ... |
50-161 |
9.24e-03 |
|
second calponin homology (CH) domain found in beta-parvin; 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. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409187 Cd Length: 130 Bit Score: 39.57 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 50 ADERDRVQKKTFTKWVNKHLMKSQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLKH 125
Cdd:cd21338 15 APDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTpesfDQKVHNVSFAFELMQD 94
|
90 100 110
....*....|....*....|....*....|....*.
gi 736215636 126 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 161
Cdd:cd21338 95 GGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2222-2666 |
9.37e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2222 QVEKELTMVKLRLDETDKQKALLDEELQRVKGEVNDAVKQKAQVEDELAKVRIQ---MDELLKLKLKIEEQNRSLMKKDK 2298
Cdd:COG5185 90 KEKKLDTKILQEYVNSLIKLPNYEWSADILISLLYLYKSEIVALKDELIKVEKLdeiADIEASYGEVETGIIKDIFGKLT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2299 DKTQKVLAEEagkMKSLAEEAARLSVEAEETARQRQIAESNlaeQRALAEKMLKEKMQAIQEATKLKAEAQELQKQKDQA 2378
Cdd:COG5185 170 QELNQNLKKL---EIFGLTLGLLKGISELKKAEPSGTVNSI---KESETGNLGSESTLLEKAKEIINIEEALKGFQDPES 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2379 QEKAKKLLEDKqqIQQRLDKETEGFQKSLEAERKRQLEVSAEAETLRLKVKELSD------AQSKAENEAKKFKKQADEA 2452
Cdd:COG5185 244 ELEDLAQTSDK--LEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEkiaeytKSIDIKKATESLEEQLAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2453 KARLKDTEKQS-TETVVQKLETQRLQSTREADGLKEAIADLEKEREKLKKEAEELQ--NKSNKMANTQKEEIEQQKAIIQ 2529
Cdd:COG5185 322 EAEQELEESKReTETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEelDSFKDTIESTKESLDEIPQNQR 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2530 KSFISERELLLKRQKAVEDEKKKLQKQFEDEV-------KKAEALKDEQERQRKLMEEEKKKLQAIMDAAVKKQKEAEAD 2602
Cdd:COG5185 402 GYAQEILATLEDTLKAADRQIEELQRQIEQATssneevsKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKE 481
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736215636 2603 MKNKQTE---------MEVLEKKRLDQEKQLGAENQKLREKLQCLEGASKQSATKQVASKTIEVQTDVVSEEQ 2666
Cdd:COG5185 482 DLNEELTqiesrvstlKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQAS 554
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
2371-2454 |
9.38e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 41.06 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736215636 2371 LQKQKDQAQEKAKKLLEDKQQIQQRLDKETEgfQKSLEAERKRQLEvsAEAETLRLKVKELSDAQSKAENEAKKFKKQAD 2450
Cdd:pfam11932 11 LAATLDQALDLAEKAVAAAAQSQKKIDKWDD--EKQELLAEYRALK--AELESLEVYNRQLERLVASQEQEIASLERQIE 86
|
....
gi 736215636 2451 EAKA 2454
Cdd:pfam11932 87 EIER 90
|
|
| |
